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1.  Guidelines for the use and interpretation of assays for monitoring autophagy 
Klionsky, Daniel J. | Abdalla, Fabio C. | Abeliovich, Hagai | Abraham, Robert T. | Acevedo-Arozena, Abraham | Adeli, Khosrow | Agholme, Lotta | Agnello, Maria | Agostinis, Patrizia | Aguirre-Ghiso, Julio A. | Ahn, Hyung Jun | Ait-Mohamed, Ouardia | Ait-Si-Ali, Slimane | Akematsu, Takahiko | Akira, Shizuo | Al-Younes, Hesham M. | Al-Zeer, Munir A. | Albert, Matthew L. | Albin, Roger L. | Alegre-Abarrategui, Javier | Aleo, Maria Francesca | Alirezaei, Mehrdad | Almasan, Alexandru | Almonte-Becerril, Maylin | Amano, Atsuo | Amaravadi, Ravi K. | Amarnath, Shoba | Amer, Amal O. | Andrieu-Abadie, Nathalie | Anantharam, Vellareddy | Ann, David K. | Anoopkumar-Dukie, Shailendra | Aoki, Hiroshi | Apostolova, Nadezda | Arancia, Giuseppe | Aris, John P. | Asanuma, Katsuhiko | Asare, Nana Y.O. | Ashida, Hisashi | Askanas, Valerie | Askew, David S. | Auberger, Patrick | Baba, Misuzu | Backues, Steven K. | Baehrecke, Eric H. | Bahr, Ben A. | Bai, Xue-Yuan | Bailly, Yannick | Baiocchi, Robert | Baldini, Giulia | Balduini, Walter | Ballabio, Andrea | Bamber, Bruce A. | Bampton, Edward T.W. | Juhász, Gábor | Bartholomew, Clinton R. | Bassham, Diane C. | Bast, Robert C. | Batoko, Henri | Bay, Boon-Huat | Beau, Isabelle | Béchet, Daniel M. | Begley, Thomas J. | Behl, Christian | Behrends, Christian | Bekri, Soumeya | Bellaire, Bryan | Bendall, Linda J. | Benetti, Luca | Berliocchi, Laura | Bernardi, Henri | Bernassola, Francesca | Besteiro, Sébastien | Bhatia-Kissova, Ingrid | Bi, Xiaoning | Biard-Piechaczyk, Martine | Blum, Janice S. | Boise, Lawrence H. | Bonaldo, Paolo | Boone, David L. | Bornhauser, Beat C. | Bortoluci, Karina R. | Bossis, Ioannis | Bost, Frédéric | Bourquin, Jean-Pierre | Boya, Patricia | Boyer-Guittaut, Michaël | Bozhkov, Peter V. | Brady, Nathan R | Brancolini, Claudio | Brech, Andreas | Brenman, Jay E. | Brennand, Ana | Bresnick, Emery H. | Brest, Patrick | Bridges, Dave | Bristol, Molly L. | Brookes, Paul S. | Brown, Eric J. | Brumell, John H. | Brunetti-Pierri, Nicola | Brunk, Ulf T. | Bulman, Dennis E. | Bultman, Scott J. | Bultynck, Geert | Burbulla, Lena F. | Bursch, Wilfried | Butchar, Jonathan P. | Buzgariu, Wanda | Bydlowski, Sergio P. | Cadwell, Ken | Cahová, Monika | Cai, Dongsheng | Cai, Jiyang | Cai, Qian | Calabretta, Bruno | Calvo-Garrido, Javier | Camougrand, Nadine | Campanella, Michelangelo | Campos-Salinas, Jenny | Candi, Eleonora | Cao, Lizhi | Caplan, Allan B. | Carding, Simon R. | Cardoso, Sandra M. | Carew, Jennifer S. | Carlin, Cathleen R. | Carmignac, Virginie | Carneiro, Leticia A.M. | Carra, Serena | Caruso, Rosario A. | Casari, Giorgio | Casas, Caty | Castino, Roberta | Cebollero, Eduardo | Cecconi, Francesco | Celli, Jean | Chaachouay, Hassan | Chae, Han-Jung | Chai, Chee-Yin | Chan, David C. | Chan, Edmond Y. | Chang, Raymond Chuen-Chung | Che, Chi-Ming | Chen, Ching-Chow | Chen, Guang-Chao | Chen, Guo-Qiang | Chen, Min | Chen, Quan | Chen, Steve S.-L. | Chen, WenLi | Chen, Xi | Chen, Xiangmei | Chen, Xiequn | Chen, Ye-Guang | Chen, Yingyu | Chen, Yongqiang | Chen, Yu-Jen | Chen, Zhixiang | Cheng, Alan | Cheng, Christopher H.K. | Cheng, Yan | Cheong, Heesun | Cheong, Jae-Ho | Cherry, Sara | Chess-Williams, Russ | Cheung, Zelda H. | Chevet, Eric | Chiang, Hui-Ling | Chiarelli, Roberto | Chiba, Tomoki | Chin, Lih-Shen | Chiou, Shih-Hwa | Chisari, Francis V. | Cho, Chi Hin | Cho, Dong-Hyung | Choi, Augustine M.K. | Choi, DooSeok | Choi, Kyeong Sook | Choi, Mary E. | Chouaib, Salem | Choubey, Divaker | Choubey, Vinay | Chu, Charleen T. | Chuang, Tsung-Hsien | Chueh, Sheau-Huei | Chun, Taehoon | Chwae, Yong-Joon | Chye, Mee-Len | Ciarcia, Roberto | Ciriolo, Maria R. | Clague, Michael J. | Clark, Robert S.B. | Clarke, Peter G.H. | Clarke, Robert | Codogno, Patrice | Coller, Hilary A. | Colombo, María I. | Comincini, Sergio | Condello, Maria | Condorelli, Fabrizio | Cookson, Mark R. | Coombs, Graham H. | Coppens, Isabelle | Corbalan, Ramon | Cossart, Pascale | Costelli, Paola | Costes, Safia | Coto-Montes, Ana | Couve, Eduardo | Coxon, Fraser P. | Cregg, James M. | Crespo, José L. | Cronjé, Marianne J. | Cuervo, Ana Maria | Cullen, Joseph J. | Czaja, Mark J. | D'Amelio, Marcello | Darfeuille-Michaud, Arlette | Davids, Lester M. | Davies, Faith E. | De Felici, Massimo | de Groot, John F. | de Haan, Cornelis A.M. | De Martino, Luisa | De Milito, Angelo | De Tata, Vincenzo | Debnath, Jayanta | Degterev, Alexei | Dehay, Benjamin | Delbridge, Lea M.D. | Demarchi, Francesca | Deng, Yi Zhen | Dengjel, Jörn | Dent, Paul | Denton, Donna | Deretic, Vojo | Desai, Shyamal D. | Devenish, Rodney J. | Di Gioacchino, Mario | Di Paolo, Gilbert | Di Pietro, Chiara | Díaz-Araya, Guillermo | Díaz-Laviada, Inés | Diaz-Meco, Maria T. | Diaz-Nido, Javier | Dikic, Ivan | Dinesh-Kumar, Savithramma P. | Ding, Wen-Xing | Distelhorst, Clark W. | Diwan, Abhinav | Djavaheri-Mergny, Mojgan | Dokudovskaya, Svetlana | Dong, Zheng | Dorsey, Frank C. | Dosenko, Victor | Dowling, James J. | Doxsey, Stephen | Dreux, Marlène | Drew, Mark E. | Duan, Qiuhong | Duchosal, Michel A. | Duff, Karen E. | Dugail, Isabelle | Durbeej, Madeleine | Duszenko, Michael | Edelstein, Charles L. | Edinger, Aimee L. | Egea, Gustavo | Eichinger, Ludwig | Eissa, N. Tony | Ekmekcioglu, Suhendan | El-Deiry, Wafik S. | Elazar, Zvulun | Elgendy, Mohamed | Ellerby, Lisa M. | Eng, Kai Er | Engelbrecht, Anna-Mart | Engelender, Simone | Erenpreisa, Jekaterina | Escalante, Ricardo | Esclatine, Audrey | Eskelinen, Eeva-Liisa | Espert, Lucile | Espina, Virginia | Fan, Huizhou | Fan, Jia | Fan, Qi-Wen | Fan, Zhen | Fang, Shengyun | Fang, Yongqi | Fanto, Manolis | Fanzani, Alessandro | Farkas, Thomas | Farre, Jean-Claude | Faure, Mathias | Fechheimer, Marcus | Feng, Carl G. | Feng, Jian | Feng, Qili | Feng, Youji | Fésüs, László | Feuer, Ralph | Figueiredo-Pereira, Maria E. | Fimia, Gian Maria | Fingar, Diane C. | Finkbeiner, Steven | Finkel, Toren | Finley, Kim D. | Fiorito, Filomena | Fisher, Edward A. | Fisher, Paul B. | Flajolet, Marc | Florez-McClure, Maria L. | Florio, Salvatore | Fon, Edward A. | Fornai, Francesco | Fortunato, Franco | Fotedar, Rati | Fowler, Daniel H. | Fox, Howard S. | Franco, Rodrigo | Frankel, Lisa B. | Fransen, Marc | Fuentes, José M. | Fueyo, Juan | Fujii, Jun | Fujisaki, Kozo | Fujita, Eriko | Fukuda, Mitsunori | Furukawa, Ruth H. | Gaestel, Matthias | Gailly, Philippe | Gajewska, Malgorzata | Galliot, Brigitte | Galy, Vincent | Ganesh, Subramaniam | Ganetzky, Barry | Ganley, Ian G. | Gao, Fen-Biao | Gao, George F. | Gao, Jinming | Garcia, Lorena | Garcia-Manero, Guillermo | Garcia-Marcos, Mikel | Garmyn, Marjan | Gartel, Andrei L. | Gatti, Evelina | Gautel, Mathias | Gawriluk, Thomas R. | Gegg, Matthew E. | Geng, Jiefei | Germain, Marc | Gestwicki, Jason E. | Gewirtz, David A. | Ghavami, Saeid | Ghosh, Pradipta | Giammarioli, Anna M. | Giatromanolaki, Alexandra N. | Gibson, Spencer B. | Gilkerson, Robert W. | Ginger, Michael L. | Ginsberg, Henry N. | Golab, Jakub | Goligorsky, Michael S. | Golstein, Pierre | Gomez-Manzano, Candelaria | Goncu, Ebru | Gongora, Céline | Gonzalez, Claudio D. | Gonzalez, Ramon | González-Estévez, Cristina | González-Polo, Rosa Ana | Gonzalez-Rey, Elena | Gorbunov, Nikolai V. | Gorski, Sharon | Goruppi, Sandro | Gottlieb, Roberta A. | Gozuacik, Devrim | Granato, Giovanna Elvira | Grant, Gary D. | Green, Kim N. | Gregorc, Ales | Gros, Frédéric | Grose, Charles | Grunt, Thomas W. | Gual, Philippe | Guan, Jun-Lin | Guan, Kun-Liang | Guichard, Sylvie M. | Gukovskaya, Anna S. | Gukovsky, Ilya | Gunst, Jan | Gustafsson, Åsa B. | Halayko, Andrew J. | Hale, Amber N. | Halonen, Sandra K. | Hamasaki, Maho | Han, Feng | Han, Ting | Hancock, Michael K. | Hansen, Malene | Harada, Hisashi | Harada, Masaru | Hardt, Stefan E. | Harper, J. Wade | Harris, Adrian L. | Harris, James | Harris, Steven D. | Hashimoto, Makoto | Haspel, Jeffrey A. | Hayashi, Shin-ichiro | Hazelhurst, Lori A. | He, Congcong | He, You-Wen | Hébert, Marie-Josée | Heidenreich, Kim A. | Helfrich, Miep H. | Helgason, Gudmundur V. | Henske, Elizabeth P. | Herman, Brian | Herman, Paul K. | Hetz, Claudio | Hilfiker, Sabine | Hill, Joseph A. | Hocking, Lynne J. | Hofman, Paul | Hofmann, Thomas G. | Höhfeld, Jörg | Holyoake, Tessa L. | Hong, Ming-Huang | Hood, David A. | Hotamisligil, Gökhan S. | Houwerzijl, Ewout J. | Høyer-Hansen, Maria | Hu, Bingren | Hu, Chien-an A. | Hu, Hong-Ming | Hua, Ya | Huang, Canhua | Huang, Ju | Huang, Shengbing | Huang, Wei-Pang | Huber, Tobias B. | Huh, Won-Ki | Hung, Tai-Ho | Hupp, Ted R. | Hur, Gang Min | Hurley, James B. | Hussain, Sabah N.A. | Hussey, Patrick J. | Hwang, Jung Jin | Hwang, Seungmin | Ichihara, Atsuhiro | Ilkhanizadeh, Shirin | Inoki, Ken | Into, Takeshi | Iovane, Valentina | Iovanna, Juan L. | Ip, Nancy Y. | Isaka, Yoshitaka | Ishida, Hiroyuki | Isidoro, Ciro | Isobe, Ken-ichi | Iwasaki, Akiko | Izquierdo, Marta | Izumi, Yotaro | Jaakkola, Panu M. | Jäättelä, Marja | Jackson, George R. | Jackson, William T. | Janji, Bassam | Jendrach, Marina | Jeon, Ju-Hong | Jeung, Eui-Bae | Jiang, Hong | Jiang, Hongchi | Jiang, Jean X. | Jiang, Ming | Jiang, Qing | Jiang, Xuejun | Jiang, Xuejun | Jiménez, Alberto | Jin, Meiyan | Jin, Shengkan V. | Joe, Cheol O. | Johansen, Terje | Johnson, Daniel E. | Johnson, Gail V.W. | Jones, Nicola L. | Joseph, Bertrand | Joseph, Suresh K. | Joubert, Annie M. | Juhász, Gábor | Juillerat-Jeanneret, Lucienne | Jung, Chang Hwa | Jung, Yong-Keun | Kaarniranta, Kai | Kaasik, Allen | Kabuta, Tomohiro | Kadowaki, Motoni | Kågedal, Katarina | Kamada, Yoshiaki | Kaminskyy, Vitaliy O. | Kampinga, Harm H. | Kanamori, Hiromitsu | Kang, Chanhee | Kang, Khong Bee | Kang, Kwang Il | Kang, Rui | Kang, Yoon-A | Kanki, Tomotake | Kanneganti, Thirumala-Devi | Kanno, Haruo | Kanthasamy, Anumantha G. | Kanthasamy, Arthi | Karantza, Vassiliki | Kaushal, Gur P. | Kaushik, Susmita | Kawazoe, Yoshinori | Ke, Po-Yuan | Kehrl, John H. | Kelekar, Ameeta | Kerkhoff, Claus | Kessel, David H. | Khalil, Hany | Kiel, Jan A.K.W. | Kiger, Amy A. | Kihara, Akio | Kim, Deok Ryong | Kim, Do-Hyung | Kim, Dong-Hou | Kim, Eun-Kyoung | Kim, Hyung-Ryong | Kim, Jae-Sung | Kim, Jeong Hun | Kim, Jin Cheon | Kim, John K. | Kim, Peter K. | Kim, Seong Who | Kim, Yong-Sun | Kim, Yonghyun | Kimchi, Adi | Kimmelman, Alec C. | King, Jason S. | Kinsella, Timothy J. | Kirkin, Vladimir | Kirshenbaum, Lorrie A. | Kitamoto, Katsuhiko | Kitazato, Kaio | Klein, Ludger | Klimecki, Walter T. | Klucken, Jochen | Knecht, Erwin | Ko, Ben C.B. | Koch, Jan C. | Koga, Hiroshi | Koh, Jae-Young | Koh, Young Ho | Koike, Masato | Komatsu, Masaaki | Kominami, Eiki | Kong, Hee Jeong | Kong, Wei-Jia | Korolchuk, Viktor I. | Kotake, Yaichiro | Koukourakis, Michael I. | Flores, Juan B. Kouri | Kovács, Attila L. | Kraft, Claudine | Krainc, Dimitri | Krämer, Helmut | Kretz-Remy, Carole | Krichevsky, Anna M. | Kroemer, Guido | Krüger, Rejko | Krut, Oleg | Ktistakis, Nicholas T. | Kuan, Chia-Yi | Kucharczyk, Roza | Kumar, Ashok | Kumar, Raj | Kumar, Sharad | Kundu, Mondira | Kung, Hsing-Jien | Kurz, Tino | Kwon, Ho Jeong | La Spada, Albert R. | Lafont, Frank | Lamark, Trond | Landry, Jacques | Lane, Jon D. | Lapaquette, Pierre | Laporte, Jocelyn F. | László, Lajos | Lavandero, Sergio | Lavoie, Josée N. | Layfield, Robert | Lazo, Pedro A. | Le, Weidong | Le Cam, Laurent | Ledbetter, Daniel J. | Lee, Alvin J.X. | Lee, Byung-Wan | Lee, Gyun Min | Lee, Jongdae | lee, Ju-hyun | Lee, Michael | Lee, Myung-Shik | Lee, Sug Hyung | Leeuwenburgh, Christiaan | Legembre, Patrick | Legouis, Renaud | Lehmann, Michael | Lei, Huan-Yao | Lei, Qun-Ying | Leib, David A. | Leiro, José | Lemasters, John J. | Lemoine, Antoinette | Lesniak, Maciej S. | Lev, Dina | Levenson, Victor V. | Levine, Beth | Levy, Efrat | Li, Faqiang | Li, Jun-Lin | Li, Lian | Li, Sheng | Li, Weijie | Li, Xue-Jun | Li, Yan-Bo | Li, Yi-Ping | Liang, Chengyu | Liang, Qiangrong | Liao, Yung-Feng | Liberski, Pawel P. | Lieberman, Andrew | Lim, Hyunjung J. | Lim, Kah-Leong | Lim, Kyu | Lin, Chiou-Feng | Lin, Fu-Cheng | Lin, Jian | Lin, Jiandie D. | Lin, Kui | Lin, Wan-Wan | Lin, Weei-Chin | Lin, Yi-Ling | Linden, Rafael | Lingor, Paul | Lippincott-Schwartz, Jennifer | Lisanti, Michael P. | Liton, Paloma B. | Liu, Bo | Liu, Chun-Feng | Liu, Kaiyu | Liu, Leyuan | Liu, Qiong A. | Liu, Wei | Liu, Young-Chau | Liu, Yule | Lockshin, Richard A. | Lok, Chun-Nam | Lonial, Sagar | Loos, Benjamin | Lopez-Berestein, Gabriel | López-Otín, Carlos | Lossi, Laura | Lotze, Michael T. | Low, Peter | Lu, Binfeng | Lu, Bingwei | Lu, Bo | Lu, Zhen | Luciano, Fréderic | Lukacs, Nicholas W. | Lund, Anders H. | Lynch-Day, Melinda A. | Ma, Yong | Macian, Fernando | MacKeigan, Jeff P. | Macleod, Kay F. | Madeo, Frank | Maiuri, Luigi | Maiuri, Maria Chiara | Malagoli, Davide | Malicdan, May Christine V. | Malorni, Walter | Man, Na | Mandelkow, Eva-Maria | Manon, Stephen | Manov, Irena | Mao, Kai | Mao, Xiang | Mao, Zixu | Marambaud, Philippe | Marazziti, Daniela | Marcel, Yves L. | Marchbank, Katie | Marchetti, Piero | Marciniak, Stefan J. | Marcondes, Mateus | Mardi, Mohsen | Marfe, Gabriella | Mariño, Guillermo | Markaki, Maria | Marten, Mark R. | Martin, Seamus J. | Martinand-Mari, Camille | Martinet, Wim | Martinez-Vicente, Marta | Masini, Matilde | Matarrese, Paola | Matsuo, Saburo | Matteoni, Raffaele | Mayer, Andreas | Mazure, Nathalie M. | McConkey, David J. | McConnell, Melanie J. | McDermott, Catherine | McDonald, Christine | McInerney, Gerald M. | McKenna, Sharon L. | McLaughlin, BethAnn | McLean, Pamela J. | McMaster, Christopher R. | McQuibban, G. Angus | Meijer, Alfred J. | Meisler, Miriam H. | Meléndez, Alicia | Melia, Thomas J. | Melino, Gerry | Mena, Maria A. | Menendez, Javier A. | Menna-Barreto, Rubem F. S. | Menon, Manoj B. | Menzies, Fiona M. | Mercer, Carol A. | Merighi, Adalberto | Merry, Diane E. | Meschini, Stefania | Meyer, Christian G. | Meyer, Thomas F. | Miao, Chao-Yu | Miao, Jun-Ying | Michels, Paul A.M. | Michiels, Carine | Mijaljica, Dalibor | Milojkovic, Ana | Minucci, Saverio | Miracco, Clelia | Miranti, Cindy K. | Mitroulis, Ioannis | Miyazawa, Keisuke | Mizushima, Noboru | Mograbi, Baharia | Mohseni, Simin | Molero, Xavier | Mollereau, Bertrand | Mollinedo, Faustino | Momoi, Takashi | Monastyrska, Iryna | Monick, Martha M. | Monteiro, Mervyn J. | Moore, Michael N. | Mora, Rodrigo | Moreau, Kevin | Moreira, Paula I. | Moriyasu, Yuji | Moscat, Jorge | Mostowy, Serge | Mottram, Jeremy C. | Motyl, Tomasz | Moussa, Charbel E.-H. | Müller, Sylke | Muller, Sylviane | Münger, Karl | Münz, Christian | Murphy, Leon O. | Murphy, Maureen E. | Musarò, Antonio | Mysorekar, Indira | Nagata, Eiichiro | Nagata, Kazuhiro | Nahimana, Aimable | Nair, Usha | Nakagawa, Toshiyuki | Nakahira, Kiichi | Nakano, Hiroyasu | Nakatogawa, Hitoshi | Nanjundan, Meera | Naqvi, Naweed I. | Narendra, Derek P. | Narita, Masashi | Navarro, Miguel | Nawrocki, Steffan T. | Nazarko, Taras Y. | Nemchenko, Andriy | Netea, Mihai G. | Neufeld, Thomas P. | Ney, Paul A. | Nezis, Ioannis P. | Nguyen, Huu Phuc | Nie, Daotai | Nishino, Ichizo | Nislow, Corey | Nixon, Ralph A. | Noda, Takeshi | Noegel, Angelika A. | Nogalska, Anna | Noguchi, Satoru | Notterpek, Lucia | Novak, Ivana | Nozaki, Tomoyoshi | Nukina, Nobuyuki | Nürnberger, Thorsten | Nyfeler, Beat | Obara, Keisuke | Oberley, Terry D. | Oddo, Salvatore | Ogawa, Michinaga | Ohashi, Toya | Okamoto, Koji | Oleinick, Nancy L. | Oliver, F. Javier | Olsen, Laura J. | Olsson, Stefan | Opota, Onya | Osborne, Timothy F. | Ostrander, Gary K. | Otsu, Kinya | Ou, Jing-hsiung James | Ouimet, Mireille | Overholtzer, Michael | Ozpolat, Bulent | Paganetti, Paolo | Pagnini, Ugo | Pallet, Nicolas | Palmer, Glen E. | Palumbo, Camilla | Pan, Tianhong | Panaretakis, Theocharis | Pandey, Udai Bhan | Papackova, Zuzana | Papassideri, Issidora | Paris, Irmgard | Park, Junsoo | Park, Ohkmae K. | Parys, Jan B. | Parzych, Katherine R. | Patschan, Susann | Patterson, Cam | Pattingre, Sophie | Pawelek, John M. | Peng, Jianxin | Perlmutter, David H. | Perrotta, Ida | Perry, George | Pervaiz, Shazib | Peter, Matthias | Peters, Godefridus J. | Petersen, Morten | Petrovski, Goran | Phang, James M. | Piacentini, Mauro | Pierre, Philippe | Pierrefite-Carle, Valérie | Pierron, Gérard | Pinkas-Kramarski, Ronit | Piras, Antonio | Piri, Natik | Platanias, Leonidas C. | Pöggeler, Stefanie | Poirot, Marc | Poletti, Angelo | Poüs, Christian | Pozuelo-Rubio, Mercedes | Prætorius-Ibba, Mette | Prasad, Anil | Prescott, Mark | Priault, Muriel | Produit-Zengaffinen, Nathalie | Progulske-Fox, Ann | Proikas-Cezanne, Tassula | Przedborski, Serge | Przyklenk, Karin | Puertollano, Rosa | Puyal, Julien | Qian, Shu-Bing | Qin, Liang | Qin, Zheng-Hong | Quaggin, Susan E. | Raben, Nina | Rabinowich, Hannah | Rabkin, Simon W. | Rahman, Irfan | Rami, Abdelhaq | Ramm, Georg | Randall, Glenn | Randow, Felix | Rao, V. Ashutosh | Rathmell, Jeffrey C. | Ravikumar, Brinda | Ray, Swapan K. | Reed, Bruce H. | Reed, John C. | Reggiori, Fulvio | Régnier-Vigouroux, Anne | Reichert, Andreas S. | Reiners, John J. | Reiter, Russel J. | Ren, Jun | Revuelta, José L. | Rhodes, Christopher J. | Ritis, Konstantinos | Rizzo, Elizete | Robbins, Jeffrey | Roberge, Michel | Roca, Hernan | Roccheri, Maria C. | Rocchi, Stephane | Rodemann, H. Peter | Rodríguez de Córdoba, Santiago | Rohrer, Bärbel | Roninson, Igor B. | Rosen, Kirill | Rost-Roszkowska, Magdalena M. | Rouis, Mustapha | Rouschop, Kasper M.A. | Rovetta, Francesca | Rubin, Brian P. | Rubinsztein, David C. | Ruckdeschel, Klaus | Rucker, Edmund B. | Rudich, Assaf | Rudolf, Emil | Ruiz-Opazo, Nelson | Russo, Rossella | Rusten, Tor Erik | Ryan, Kevin M. | Ryter, Stefan W. | Sabatini, David M. | Sadoshima, Junichi | Saha, Tapas | Saitoh, Tatsuya | Sakagami, Hiroshi | Sakai, Yasuyoshi | Salekdeh, Ghasem Hoseini | Salomoni, Paolo | Salvaterra, Paul M. | Salvesen, Guy | Salvioli, Rosa | Sanchez, Anthony M.J. | Sánchez-Alcázar, José A. | Sánchez-Prieto, Ricardo | Sandri, Marco | Sankar, Uma | Sansanwal, Poonam | Santambrogio, Laura | Saran, Shweta | Sarkar, Sovan | Sarwal, Minnie | Sasakawa, Chihiro | Sasnauskiene, Ausra | Sass, Miklós | Sato, Ken | Sato, Miyuki | Schapira, Anthony H.V. | Scharl, Michael | Schätzl, Hermann M. | Scheper, Wiep | Schiaffino, Stefano | Schneider, Claudio | Schneider, Marion E. | Schneider-Stock, Regine | Schoenlein, Patricia V. | Schorderet, Daniel F. | Schüller, Christoph | Schwartz, Gary K. | Scorrano, Luca | Sealy, Linda | Seglen, Per O. | Segura-Aguilar, Juan | Seiliez, Iban | Seleverstov, Oleksandr | Sell, Christian | Seo, Jong Bok | Separovic, Duska | Setaluri, Vijayasaradhi | Setoguchi, Takao | Settembre, Carmine | Shacka, John J. | Shanmugam, Mala | Shapiro, Irving M. | Shaulian, Eitan | Shaw, Reuben J. | Shelhamer, James H. | Shen, Han-Ming | Shen, Wei-Chiang
Autophagy  2012;8(4):445-544.
In 2008 we published the first set of guidelines for standardizing research in autophagy. Since then, research on this topic has continued to accelerate, and many new scientists have entered the field. Our knowledge base and relevant new technologies have also been expanding. Accordingly, it is important to update these guidelines for monitoring autophagy in different organisms. Various reviews have described the range of assays that have been used for this purpose. Nevertheless, there continues to be confusion regarding acceptable methods to measure autophagy, especially in multicellular eukaryotes. A key point that needs to be emphasized is that there is a difference between measurements that monitor the numbers or volume of autophagic elements (e.g., autophagosomes or autolysosomes) at any stage of the autophagic process vs. those that measure flux through the autophagy pathway (i.e., the complete process); thus, a block in macroautophagy that results in autophagosome accumulation needs to be differentiated from stimuli that result in increased autophagic activity, defined as increased autophagy induction coupled with increased delivery to, and degradation within, lysosomes (in most higher eukaryotes and some protists such as Dictyostelium) or the vacuole (in plants and fungi). In other words, it is especially important that investigators new to the field understand that the appearance of more autophagosomes does not necessarily equate with more autophagy. In fact, in many cases, autophagosomes accumulate because of a block in trafficking to lysosomes without a concomitant change in autophagosome biogenesis, whereas an increase in autolysosomes may reflect a reduction in degradative activity. Here, we present a set of guidelines for the selection and interpretation of methods for use by investigators who aim to examine macroautophagy and related processes, as well as for reviewers who need to provide realistic and reasonable critiques of papers that are focused on these processes. These guidelines are not meant to be a formulaic set of rules, because the appropriate assays depend in part on the question being asked and the system being used. In addition, we emphasize that no individual assay is guaranteed to be the most appropriate one in every situation, and we strongly recommend the use of multiple assays to monitor autophagy. In these guidelines, we consider these various methods of assessing autophagy and what information can, or cannot, be obtained from them. Finally, by discussing the merits and limits of particular autophagy assays, we hope to encourage technical innovation in the field.
doi:10.4161/auto.19496
PMCID: PMC3404883  PMID: 22966490
LC3; autolysosome; autophagosome; flux; lysosome; phagophore; stress; vacuole
2.  A large-scale analysis of autophagy-related gene expression identifies new regulators of autophagy 
Autophagy  2015;11(11):2114-2122.
Autophagy is a pathway mediating vacuolar degradation and recycling of proteins and organelles, which plays crucial roles in cellular physiology. To ensure its proper cytoprotective function, the induction and amplitude of autophagy are tightly regulated, and defects in its regulation are associated with various diseases. Transcriptional control of autophagy is a critical aspect of autophagy regulation, which remains largely unexplored. In particular, very few transcription factors involved in the activation or repression of autophagy-related gene expression have been characterized. To identify such regulators, we analyzed the expression of representative ATG genes in a large collection of DNA-binding mutant deletion strains in growing conditions as well as after nitrogen or glucose starvation. This analysis identified several proteins involved in the transcriptional control of ATG genes. Further analyses showed a correlation between variations in expression and autophagy magnitude, thus identifying new positive and negative regulators of the autophagy pathway. By providing a detailed analysis of the regulatory network of the ATG genes our study paves the way for future research on autophagy regulation and signaling.
doi:10.1080/15548627.2015.1099796
PMCID: PMC4824583  PMID: 26649943
autophagy; gene expression; stress; transcription factor; yeast
3.  Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition) 
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Yongshun | Chen, Yu-Jen | Chen, Yue-Qin | Chen, Yujie | Chen, Zhen | Chen, Zhong | Cheng, Alan | Cheng, Christopher HK | Cheng, Hua | Cheong, Heesun | Cherry, Sara | Chesney, Jason | Cheung, Chun Hei Antonio | Chevet, Eric | Chi, Hsiang Cheng | Chi, Sung-Gil | Chiacchiera, Fulvio | Chiang, Hui-Ling | Chiarelli, Roberto | Chiariello, Mario | Chieppa, Marcello | Chin, Lih-Shen | Chiong, Mario | Chiu, Gigi NC | Cho, Dong-Hyung | Cho, Ssang-Goo | Cho, William C | Cho, Yong-Yeon | Cho, Young-Seok | Choi, Augustine MK | Choi, Eui-Ju | Choi, Eun-Kyoung | Choi, Jayoung | Choi, Mary E | Choi, Seung-Il | Chou, Tsui-Fen | Chouaib, Salem | Choubey, Divaker | Choubey, Vinay | Chow, Kuan-Chih | Chowdhury, Kamal | Chu, Charleen T | Chuang, Tsung-Hsien | Chun, Taehoon | Chung, Hyewon | Chung, Taijoon | Chung, Yuen-Li | Chwae, Yong-Joon | Cianfanelli, Valentina | Ciarcia, Roberto | Ciechomska, Iwona A | Ciriolo, Maria Rosa | Cirone, Mara | Claerhout, Sofie | Clague, Michael J | Clària, Joan | Clarke, Peter GH | Clarke, Robert | Clementi, Emilio | Cleyrat, Cédric | Cnop, Miriam | Coccia, Eliana M | Cocco, Tiziana | Codogno, Patrice | Coers, Jörn | Cohen, Ezra EW | Colecchia, David | Coletto, Luisa | Coll, Núria S | Colucci-Guyon, Emma | Comincini, Sergio | Condello, Maria | Cook, Katherine L | Coombs, Graham H | Cooper, Cynthia D | Cooper, J Mark | Coppens, Isabelle | Corasaniti, Maria Tiziana | Corazzari, Marco | Corbalan, Ramon | Corcelle-Termeau, Elisabeth | Cordero, Mario D | Corral-Ramos, Cristina | Corti, Olga | Cossarizza, Andrea | Costelli, Paola | Costes, Safia | Cotman, Susan L | Coto-Montes, Ana | Cottet, Sandra | Couve, Eduardo | Covey, Lori R | Cowart, L Ashley | Cox, Jeffery S | Coxon, Fraser P | Coyne, Carolyn B | Cragg, Mark S | Craven, Rolf J | Crepaldi, Tiziana | Crespo, Jose L | Criollo, Alfredo | Crippa, Valeria | Cruz, Maria Teresa | Cuervo, Ana Maria | Cuezva, Jose M | Cui, Taixing | Cutillas, Pedro R | Czaja, Mark J | Czyzyk-Krzeska, Maria F | Dagda, Ruben K | Dahmen, Uta | Dai, Chunsun | Dai, Wenjie | Dai, Yun | Dalby, Kevin N | Dalla Valle, Luisa | Dalmasso, Guillaume | D'Amelio, Marcello | Damme, Markus | Darfeuille-Michaud, Arlette | Dargemont, Catherine | Darley-Usmar, Victor M | Dasarathy, Srinivasan | Dasgupta, Biplab | Dash, Srikanta | Dass, Crispin R | Davey, Hazel Marie | Davids, Lester M | Dávila, David | Davis, Roger J | Dawson, Ted M | Dawson, Valina L | Daza, Paula | de Belleroche, Jackie | de Figueiredo, Paul | de Figueiredo, Regina Celia Bressan Queiroz | de la Fuente, José | De Martino, Luisa | De Matteis, Antonella | De Meyer, Guido RY | De Milito, Angelo | De Santi, Mauro | de Souza, Wanderley | De Tata, Vincenzo | De Zio, Daniela | Debnath, Jayanta | Dechant, Reinhard | Decuypere, Jean-Paul | Deegan, Shane | Dehay, Benjamin | Del Bello, Barbara | Del Re, Dominic P | Delage-Mourroux, Régis | Delbridge, Lea MD | Deldicque, Louise | Delorme-Axford, Elizabeth | Deng, Yizhen | Dengjel, Joern | Denizot, Melanie | Dent, Paul | Der, Channing J | Deretic, Vojo | Derrien, Benoît | Deutsch, Eric | Devarenne, Timothy P | Devenish, Rodney J | Di Bartolomeo, Sabrina | Di Daniele, Nicola | Di Domenico, Fabio | Di Nardo, Alessia | Di Paola, Simone | Di Pietro, Antonio | Di Renzo, Livia | DiAntonio, Aaron | Díaz-Araya, Guillermo | Díaz-Laviada, Ines | Diaz-Meco, Maria T | Diaz-Nido, Javier | Dickey, Chad A | Dickson, Robert C | Diederich, Marc | Digard, Paul | Dikic, Ivan | Dinesh-Kumar, Savithrama P | Ding, Chan | Ding, Wen-Xing | Ding, Zufeng | Dini, Luciana | Distler, Jörg HW | Diwan, Abhinav | Djavaheri-Mergny, Mojgan | Dmytruk, Kostyantyn | Dobson, Renwick CJ | Doetsch, Volker | Dokladny, Karol | Dokudovskaya, Svetlana | Donadelli, Massimo | Dong, X Charlie | Dong, Xiaonan | Dong, Zheng | Donohue, Terrence M | Doran, Kelly S | D'Orazi, Gabriella | Dorn, Gerald W | Dosenko, Victor | Dridi, Sami | Drucker, Liat | Du, Jie | Du, Li-Lin | Du, Lihuan | du Toit, André | Dua, Priyamvada | Duan, Lei | Duann, Pu | Dubey, Vikash Kumar | Duchen, Michael R | Duchosal, Michel A | Duez, Helene | Dugail, Isabelle | Dumit, Verónica I | Duncan, Mara C | Dunlop, Elaine A | Dunn, William A | Dupont, Nicolas | Dupuis, Luc | Durán, Raúl V | Durcan, Thomas M | Duvezin-Caubet, Stéphane | Duvvuri, Umamaheswar | Eapen, Vinay | Ebrahimi-Fakhari, Darius | Echard, Arnaud | Eckhart, Leopold | Edelstein, Charles L | Edinger, Aimee L | Eichinger, Ludwig | Eisenberg, Tobias | Eisenberg-Lerner, Avital | Eissa, N Tony | El-Deiry, Wafik S | El-Khoury, Victoria | Elazar, Zvulun | Eldar-Finkelman, Hagit | Elliott, Chris JH | Emanuele, Enzo | Emmenegger, Urban | Engedal, Nikolai | Engelbrecht, Anna-Mart | Engelender, Simone | Enserink, Jorrit M | Erdmann, Ralf | Erenpreisa, Jekaterina | Eri, Rajaraman | Eriksen, Jason L | Erman, Andreja | Escalante, Ricardo | Eskelinen, Eeva-Liisa | Espert, Lucile | Esteban-Martínez, Lorena | Evans, Thomas J | Fabri, Mario | Fabrias, Gemma | Fabrizi, Cinzia | Facchiano, Antonio | Færgeman, Nils J | Faggioni, Alberto | Fairlie, W Douglas | Fan, Chunhai | Fan, Daping | Fan, Jie | Fang, Shengyun | Fanto, Manolis | Fanzani, Alessandro | Farkas, Thomas | Faure, Mathias | Favier, Francois B | Fearnhead, Howard | Federici, Massimo | Fei, Erkang | Felizardo, Tania C | Feng, Hua | Feng, Yibin | Feng, Yuchen | Ferguson, Thomas A | Fernández, Álvaro F | Fernandez-Barrena, Maite G | Fernandez-Checa, Jose C | Fernández-López, Arsenio | Fernandez-Zapico, Martin E | Feron, Olivier | Ferraro, Elisabetta | Ferreira-Halder, Carmen Veríssima | Fesus, Laszlo | Feuer, Ralph | Fiesel, Fabienne C | Filippi-Chiela, Eduardo C | Filomeni, Giuseppe | Fimia, Gian Maria | Fingert, John H | Finkbeiner, Steven | Finkel, Toren | Fiorito, Filomena | Fisher, Paul B | Flajolet, Marc | Flamigni, Flavio | Florey, Oliver | Florio, Salvatore | Floto, R Andres | Folini, Marco | Follo, Carlo | Fon, Edward A | Fornai, Francesco | Fortunato, Franco | Fraldi, Alessandro | Franco, Rodrigo | Francois, Arnaud | François, Aurélie | Frankel, Lisa B | Fraser, Iain DC | Frey, Norbert | Freyssenet, Damien G | Frezza, Christian | Friedman, Scott L | Frigo, Daniel E | Fu, Dongxu | Fuentes, José M | Fueyo, Juan | Fujitani, Yoshio | Fujiwara, Yuuki | Fujiya, Mikihiro | Fukuda, Mitsunori | Fulda, Simone | Fusco, Carmela | Gabryel, Bozena | Gaestel, Matthias | Gailly, Philippe | Gajewska, Malgorzata | Galadari, Sehamuddin | Galili, Gad | Galindo, Inmaculada | Galindo, Maria F | Galliciotti, Giovanna | Galluzzi, Lorenzo | Galluzzi, Luca | Galy, Vincent | Gammoh, Noor | Gandy, Sam | Ganesan, Anand K | Ganesan, Swamynathan | Ganley, Ian G | Gannagé, Monique | Gao, Fen-Biao | Gao, Feng | Gao, Jian-Xin | García Nannig, Lorena | García Véscovi, Eleonora | Garcia-Macía, Marina | Garcia-Ruiz, Carmen | Garg, Abhishek D | Garg, Pramod Kumar | Gargini, Ricardo | Gassen, Nils Christian | Gatica, Damián | Gatti, Evelina | Gavard, Julie | Gavathiotis, Evripidis | Ge, Liang | Ge, Pengfei | Ge, Shengfang | Gean, Po-Wu | Gelmetti, Vania | Genazzani, Armando A | Geng, Jiefei | Genschik, Pascal | Gerner, Lisa | Gestwicki, Jason E | Gewirtz, David A | Ghavami, Saeid | Ghigo, Eric | Ghosh, Debabrata | Giammarioli, Anna Maria | Giampieri, Francesca | Giampietri, Claudia | Giatromanolaki, Alexandra | Gibbings, Derrick J | Gibellini, Lara | Gibson, Spencer B | Ginet, Vanessa | Giordano, Antonio | Giorgini, Flaviano | Giovannetti, Elisa | Girardin, Stephen E | Gispert, Suzana | Giuliano, Sandy | Gladson, Candece L | Glavic, Alvaro | Gleave, Martin | Godefroy, Nelly | Gogal, Robert M | Gokulan, Kuppan | Goldman, Gustavo H | Goletti, Delia | Goligorsky, Michael S | Gomes, Aldrin V | Gomes, Ligia C | Gomez, Hernando | Gomez-Manzano, Candelaria | Gómez-Sánchez, Rubén | Gonçalves, Dawit AP | Goncu, Ebru | Gong, Qingqiu | Gongora, Céline | Gonzalez, Carlos B | Gonzalez-Alegre, Pedro | Gonzalez-Cabo, Pilar | González-Polo, Rosa Ana | Goping, Ing Swie | Gorbea, Carlos | Gorbunov, Nikolai V | Goring, Daphne R | Gorman, Adrienne M | Gorski, Sharon M | Goruppi, Sandro | Goto-Yamada, Shino | Gotor, Cecilia | Gottlieb, Roberta A | Gozes, Illana | Gozuacik, Devrim | Graba, Yacine | Graef, Martin | Granato, Giovanna E | Grant, Gary Dean | Grant, Steven | Gravina, Giovanni Luca | Green, Douglas R | Greenhough, Alexander | Greenwood, Michael T | Grimaldi, Benedetto | Gros, Frédéric | Grose, Charles | Groulx, Jean-Francois | Gruber, Florian | Grumati, Paolo | Grune, Tilman | Guan, Jun-Lin | Guan, Kun-Liang | Guerra, Barbara | Guillen, Carlos | Gulshan, Kailash | Gunst, Jan | Guo, Chuanyong | Guo, Lei | Guo, Ming | Guo, Wenjie | Guo, Xu-Guang | Gust, Andrea A | Gustafsson, Åsa B | Gutierrez, Elaine | Gutierrez, Maximiliano G | Gwak, Ho-Shin | Haas, Albert | Haber, James E | Hadano, Shinji | Hagedorn, Monica | Hahn, David R | Halayko, Andrew J | Hamacher-Brady, Anne | Hamada, Kozo | Hamai, Ahmed | Hamann, Andrea | Hamasaki, Maho | Hamer, Isabelle | Hamid, Qutayba | Hammond, Ester M | Han, Feng | Han, Weidong | Handa, James T | Hanover, John A | Hansen, Malene | Harada, Masaru | Harhaji-Trajkovic, Ljubica | Harper, J Wade | Harrath, Abdel Halim | Harris, Adrian L | Harris, James | Hasler, Udo | Hasselblatt, Peter | Hasui, Kazuhisa | Hawley, Robert G | Hawley, Teresa S | He, Congcong | He, Cynthia Y | He, Fengtian | He, Gu | He, Rong-Rong | He, Xian-Hui | He, You-Wen | He, Yu-Ying | Heath, Joan K | Hébert, Marie-Josée | Heinzen, Robert A | Helgason, Gudmundur Vignir | Hensel, Michael | Henske, Elizabeth P | Her, Chengtao | Herman, Paul K | Hernández, Agustín | Hernandez, Carlos | Hernández-Tiedra, Sonia | Hetz, Claudio | Hiesinger, P Robin | Higaki, Katsumi | Hilfiker, Sabine | Hill, Bradford G | Hill, Joseph A | Hill, William D | Hino, Keisuke | Hofius, Daniel | Hofman, Paul | Höglinger, Günter U | Höhfeld, Jörg | Holz, Marina K | Hong, Yonggeun | Hood, David A | Hoozemans, Jeroen JM | Hoppe, Thorsten | Hsu, Chin | Hsu, Chin-Yuan | Hsu, Li-Chung | Hu, Dong | Hu, Guochang | Hu, Hong-Ming | Hu, Hongbo | Hu, Ming Chang | Hu, Yu-Chen | Hu, Zhuo-Wei | Hua, Fang | Hua, Ya | Huang, Canhua | Huang, Huey-Lan | Huang, Kuo-How | Huang, Kuo-Yang | Huang, Shile | Huang, Shiqian | Huang, Wei-Pang | Huang, Yi-Ran | Huang, Yong | Huang, Yunfei | Huber, Tobias B | Huebbe, Patricia | Huh, Won-Ki | Hulmi, Juha J | Hur, Gang Min | Hurley, James H | Husak, Zvenyslava | Hussain, Sabah NA | Hussain, Salik | Hwang, Jung Jin | Hwang, Seungmin | Hwang, Thomas IS | Ichihara, Atsuhiro | Imai, Yuzuru | Imbriano, Carol | Inomata, Megumi | Into, Takeshi | Iovane, Valentina | Iovanna, Juan L | Iozzo, Renato V | Ip, Nancy Y | Irazoqui, Javier E | Iribarren, Pablo | Isaka, Yoshitaka | Isakovic, Aleksandra J | Ischiropoulos, Harry | Isenberg, Jeffrey S | Ishaq, Mohammad | Ishida, Hiroyuki | Ishii, Isao | Ishmael, Jane E | Isidoro, Ciro | Isobe, Ken-ichi | Isono, Erika | Issazadeh-Navikas, Shohreh | Itahana, Koji | Itakura, Eisuke | Ivanov, Andrei I | Iyer, Anand Krishnan V | Izquierdo, José M | Izumi, Yotaro | Izzo, Valentina | Jäättelä, Marja | Jaber, Nadia | Jackson, Daniel John | Jackson, William T | Jacob, Tony George | Jacques, Thomas S | Jagannath, Chinnaswamy | Jain, Ashish | Jana, Nihar Ranjan | Jang, Byoung Kuk | Jani, Alkesh | Janji, Bassam | Jannig, Paulo Roberto | Jansson, Patric J | Jean, Steve | Jendrach, Marina | Jeon, Ju-Hong | Jessen, Niels | Jeung, Eui-Bae | Jia, Kailiang | Jia, Lijun | Jiang, Hong | Jiang, Hongchi | Jiang, Liwen | Jiang, Teng | Jiang, Xiaoyan | Jiang, Xuejun | Jiang, Xuejun | Jiang, Ying | Jiang, Yongjun | Jiménez, Alberto | Jin, Cheng | Jin, Hongchuan | Jin, Lei | Jin, Meiyan | Jin, Shengkan | Jinwal, Umesh Kumar | Jo, Eun-Kyeong | Johansen, Terje | Johnson, Daniel E | Johnson, Gail VW | Johnson, James D | Jonasch, Eric | Jones, Chris | Joosten, Leo AB | Jordan, Joaquin | Joseph, Anna-Maria | Joseph, Bertrand | Joubert, Annie M | Ju, Dianwen | Ju, Jingfang | Juan, Hsueh-Fen | Juenemann, Katrin | Juhász, Gábor | Jung, Hye Seung | Jung, Jae U | Jung, Yong-Keun | Jungbluth, Heinz | Justice, Matthew J | Jutten, Barry | Kaakoush, Nadeem O | Kaarniranta, Kai | Kaasik, Allen | Kabuta, Tomohiro | Kaeffer, Bertrand | Kågedal, Katarina | Kahana, Alon | Kajimura, Shingo | Kakhlon, Or | Kalia, Manjula | Kalvakolanu, Dhan V | Kamada, Yoshiaki | Kambas, Konstantinos | Kaminskyy, Vitaliy O | Kampinga, Harm H | Kandouz, Mustapha | Kang, Chanhee | Kang, Rui | Kang, Tae-Cheon | Kanki, Tomotake | Kanneganti, Thirumala-Devi | Kanno, Haruo | Kanthasamy, Anumantha G | Kantorow, Marc | Kaparakis-Liaskos, Maria | Kapuy, Orsolya | Karantza, Vassiliki | Karim, Md Razaul | Karmakar, Parimal | Kaser, Arthur | Kaushik, Susmita | Kawula, Thomas | Kaynar, A Murat | Ke, Po-Yuan | Ke, Zun-Ji | Kehrl, John H | Keller, Kate E | Kemper, Jongsook Kim
Autophagy  2016;12(1):1-222.
doi:10.1080/15548627.2015.1100356
PMCID: PMC4835977  PMID: 26799652
autolysosome; autophagosome; chaperone-mediated autophagy; flux; LC3; lysosome; macroautophagy; phagophore; stress; vacuole
4.  A missing piece of the puzzle: Atg11 functions as a scaffold to activate Atg1 for selective autophagy 
Autophagy  2015;11(12):2139-2141.
The mechanism regulating Atg1 kinase activity for the initiation of selective macroautophagy (hereafter autophagy) under nutrient-rich conditions has been a long-standing question. Canonically in yeast, nutrient starvation or rapamycin treatment repress TOR complex 1 and stimulate the Atg1 complex (including at least Atg1, Atg13, Atg17, Atg29 and Atg31), which allows the recruitment of downstream autophagy-related (Atg) components to the phagophore assembly site (PAS), culminating in phagophore formation, and, subsequently, autophagosome biogenesis. Atg1 also functions under conditions promoting selective autophagy that do not necessarily require nutrient deprivation for induction. However, there has been some debate as to whether Atg1 catalytic activity plays a more important role under conditions of nutrient starvation-induced autophagy (i.e., bulk autophagy) vs. selective autophagy (e.g., the cytoplasm-to-vacuole targeting [Cvt] pathway). A recent paper by Kamber and colleagues investigates the mechanism regulating Atg1 activity during selective autophagy.
doi:10.1080/15548627.2015.1116672
PMCID: PMC4835187  PMID: 26566077
Atg19; Cvt; pexophagy; prApe1; yeast
5.  Atg41/Icy2 regulates autophagosome formation 
Autophagy  2015;11(12):2288-2299.
Macroautophagy (hereafter autophagy) is one of the major degradation systems in eukaryotic cells, and its dysfunction may result in diseases ranging from neurodegeneration to cancer. Although most of the autophagy-related (Atg) proteins that function in this pathway were first identified in yeast, many were subsequently shown to have homologs in higher eukaryotes including humans, and the overall mechanism of autophagy is highly conserved. The most prominent feature of autophagy is the formation of a double-membrane sequestering compartment, the phagophore; this transient organelle surrounds part of the cytoplasm and matures into an autophagosome, which subsequently fuses with the vacuole or lysosome to allow degradation of the cargo. Much attention has focused on the process involved in phagophore nucleation and expansion, but many questions remain. Here, we identified the yeast protein Icy2, which we now name Atg41, as playing a role in autophagosome formation. Atg41 interacts with the transmembrane protein Atg9, a key component involved in autophagosome biogenesis, and both proteins display a similar localization profile. Under autophagy-inducing conditions the expression level of Atg41 increases dramatically and is regulated by the transcription factor Gcn4. This work provides further insight into the mechanism of Atg9 function and the dynamics of sequestering membrane formation during autophagy.
doi:10.1080/15548627.2015.1107692
PMCID: PMC4835205  PMID: 26565778
autophagy; lysosome; stress; vacuole; yeast
6.  Analysis of the native conformation of the LIR/AIM motif in the Atg8/LC3/GABARAP-binding proteins 
Autophagy  2015;11(12):2153-2159.
The Atg8/LC3/GABARAP family of proteins, a group that has structural homology with ubiquitin, connects with a large set of binding partners to function in macroautophagy (hereafter autophagy). This interaction occurs primarily via a conserved motif termed the LC3-interacting region (LIR), or the Atg8-interacting motif (AIM). The consensus sequence for this motif, [W/F/Y]xx[L/I/V], can be found in many proteins, but only some of them are physiological partners containing a functional LIR/AIM. Because the structure of many full-length partners has not been, or cannot be, solved, the structural context of the LIR/AIM within the native protein conformation is not obvious. Here we suggest that the functional LIR/AIM is a short linear motif (SLiM) protein-binding module, arising from an intrinsically disordered region. This finding enables the rapid elimination of some false Atg8/LC3/GABARAP-binding proteins, and connects the exponentially growing knowledge on disordered SLiMs with autophagy.
doi:10.1080/15548627.2015.1111503
PMCID: PMC4835208  PMID: 26565669
AIM motif; Atg8; GABARAP; intrinsic disorder; LC3; LIR motif; SLiM
8.  Wouter G van Doorn, December 13, 1951–May 16, 2015  
Autophagy  2015;11(8):1197.
 
doi:10.1080/15548627.2015.1062962
PMCID: PMC4590605  PMID: 26273908
9.  Posttranslationally-modified structures in the autophagy machinery: an integrative perspective 
The FEBS journal  2015;282(18):3474-3488.
Autophagy is self-cleaning process that occurs at a constitutive basal level, and is upregulated in response to stress. Macroautophagy (hereafter autophagy) is the most robust type of autophagy, where cargo (specific or nonspecific) is engulfed within a double-membrane structure termed an autophagosome. This process needs to be tightly regulated to maintain normal cellular homeostasis and prevent dysfunction; therefore, a fuller knowledge of the mechanisms of autophagy regulation is crucial for understanding the entire pathway. The autophagy-related (Atg) proteins are the primary components that carry out autophagy. Many of these proteins are conserved from yeast to human. A number of significant discoveries with regard to protein functional domains, protein-protein interactions, or posttranslational modifications of proteins involved in autophagy have been reported in parallel with, or followed by, solving the NMR or crystal structures of autophagy proteins or their protein domains. In this work, we summarize structural insights gathered to date on the proteins of the autophagy machinery that are modulated by a posttranslational modification, specifically phosphorylation, acetylation, ubiquitination, and/or SUMOylation. For each protein, we link the reported results with information on the propensity of the corresponding amino acid sequence toward order/disorder. This integrative approach yields a comprehensive overview for each posttranslationally modified protein, and also reveals areas for further investigation.
Graphical Abstract
doi:10.1111/febs.13356
PMCID: PMC4573826  PMID: 26108642
autophagy; intrinsically disordered region; posttranslational modification; protein structure; stress
10.  One step closer to understanding mammalian macroautophagy initiation: Interplay of 2 HORMA architectures in the ULK1 complex 
Autophagy  2015;11(11):1953-1955.
ULK1 and ATG13 assemble with RB1CC1/FIP200 and ATG101 to form a macroautophagy (hereafter autophagy) induction (ULK1) complex in higher eukaryotes. The yeast counterpart, the Atg1 complex, is comprised of Atg1 and Atg13 (ULK1 and ATG13 homologs), Atg17 (a proposed functional homolog of RB1CC1), and either the Atg101 subunit (in Schizosaccharomyces pombe) or the Atg29-Atg31 heterodimer (in Saccharomyces cerevisiae). With mutual exclusivity of, and no detectable homology between, the Atg29-Atg31 dimer and Atg101, knowledge about the roles of these proteins in autophagy induction is an important piece in the puzzle of understanding the molecular mechanism of autophagy initiation. A recent study reporting the structure of the S. pombe homolog Atg101 bound to the Atg13HORMA domain is a notable contribution to this knowledge (see the punctum in this issue of the journal).
doi:10.1080/15548627.2015.1087635
PMCID: PMC4824602  PMID: 26325630
Atg protein; autophagy; stress; structure; vacuole; yeast
11.  TOR-dependent post-transcriptional regulation of autophagy 
Autophagy  2015;11(12):2390-2392.
Regulation of autophagy is required to maintain cellular equilibrium and prevent disease. While extensive study of post-translational mechanisms has yielded important insights into autophagy induction, less is known about post-transcriptional mechanisms that could potentiate homeostatic control. In our study, we showed that the RNA-binding protein, Dhh1 in Saccharomyces cerevisiae and Vad1 in the pathogenic yeast Cryptococcus neoformans is involved in recruitment and degradation of key autophagy mRNAs. In addition, phosphorylation of the decapping protein Dcp2 by the target of rapamycin (TOR), facilitates decapping and degradation of autophagy-related mRNAs, resulting in repression of autophagy under nutrient-replete conditions. The post-transcriptional regulatory process is conserved in both mouse and human cells and plays a role in autophagy-related modulation of the inflammasome product IL1B. These results were then applied to provide mechanistic insight into autoimmunity of a patient with a PIK3CD/p110δ gain-of-function mutation. These results thus identify an important new post-transcriptional mechanism of autophagy regulation that is highly conserved between yeast and mammals.
doi:10.1080/15548627.2015.1091142
PMCID: PMC4835197  PMID: 26569496
autoimmunity; autophagy; phosphorylation; TOR; translation
12.  The amino acid transporter SLC38A9 regulates MTORC1 and autophagy 
Autophagy  2015;11(10):1709-1710.
The mechanistic target of rapamycin (serine/threonine kinase) complex 1 (MTORC1) is a master regulator of macroautophagy (hereafter autophagy) that responds to different environmental nutrients, including amino acids, glucose, and growth factors. The identity of the amino acid-sensing component of the MTORC1 machinery had remained elusive until a lysosomal low-affinity amino acid transporter, SLC38A9 (solute carrier family 38, member 9), was recently characterized as a novel component of the Ragulator-RRAG GTPase complex by 3 independent research groups.
doi:10.1080/15548627.2015.1084461
PMCID: PMC4824568  PMID: 26506891
autophagy; lysosome; RRAG GTPase; stress; TOR
13.  TP53INP2/DOR protein chaperones deacetylated nuclear LC3 to the cytoplasm to promote macroautophagy 
Autophagy  2015;11(9):1441-1442.
doi:10.1080/15548627.2015.1074373
PMCID: PMC4590662  PMID: 26213321
autophagy; LC3; lysosome; nucleus; stress
14.  mTORC1 maintains metabolic balance 
Cell Research  2015;25(10):1085-1086.
doi:10.1038/cr.2015.107
PMCID: PMC4650624  PMID: 26358187
15.  TOS-sing aside the glycolytic role of HK2/hexokinase-II to activate autophagy 
Autophagy  2015;11(6):865-866.
Hexokinase is the first enzyme in the glycolytic pathway catalyzing the reaction in which glucose is phosphorylated into glucose-6-phosphate. Mammals possess 4 isoforms of hexokinase; HK2 (hexokinase 2) is the predominant form in insulin-sensitive tissues such as adipocytes, as well as skeletal and cardiac muscle. In addition to its function in glucose metabolism, HK2 is associated with cardiomyocyte protection against mitochondrial-mediated apoptotic cell death; whether or not HK2 played a role in cardioprotective autophagy was yet to be discovered. However, in a recent study highlighted by a punctum in this issue of Autophagy, Roberts et al. addressed this possibility, uncovering a direct link between HK2, TORC1, and autophagy regulation.
doi:10.1080/15548627.2015.1042196
PMCID: PMC4502652  PMID: 26075875
autophagy; cardiomyocytes; hexokinase-II; MTORC1; TOR signaling motif
16.  Tor-dependent post-transcriptional regulation of autophagy: Implications for cancer therapeutics 
Molecular & Cellular Oncology  2015;3(5):e1078923.
ABSTRACT
Paradoxically, both anticancer immunosurveillance and tumor progression have been associated with intact autophagy, which is regulated by the target of rapamycin (Tor1). Here, we describe the potential impact on the design of cancer therapeutics of a newly described highly conserved post-transcriptional mechanism whereby Tor regulates autophagy.
doi:10.1080/23723556.2015.1078923
PMCID: PMC5068182  PMID: 27857968
Autoimmunity; autophagy; oncology; pharmacology; phosphorylation; Tor; tumor immunology
17.  The symphony of autophagy and calcium signaling 
Autophagy  2015;11(7):973-974.
Posttranslational regulation of macroautophagy (hereafter autophagy), including phosphorylating and dephosphorylating components of the autophagy-related (Atg) core machinery and the corresponding upstream transcriptional factors, is important for the precise modulation of autophagy levels. Several kinases that are involved in phosphorylating autophagy-related proteins have been identified in both yeast and mammalian cells. However, there has been much less research published with regard to the identification of the complementary phosphatases that function in autophagy. A recent study identified PPP3/calcineurin, a calcium-dependent phosphatase, as a regulator of autophagy, and demonstrated that one of the key targets of PPP3/calcineurin is TFEB, a master transcriptional factor that controls autophagy and lysosomal function in mammalian cells.
doi:10.1080/15548627.2015.1058475
PMCID: PMC4590665  PMID: 26046237
autophagy; calcineurin; MCOLN1; stress; TFEB
18.  Developing a set of guidelines for your research field: a practical approach 
Molecular Biology of the Cell  2016;27(5):733-738.
Since 2008, the autophagy community has periodically published a set of guidelines, currently titled “Guidelines for the Use and Interpretation of Assays for Monitoring Autophagy.” The newest version of the guidelines was published in 2016. There are many reasons for establishing a set of guidelines in a given research field. This Perspective explores some of these reasons, including standardizing nomenclature for better communication, improving reproducibility, and making it easier for newcomers to enter the field. It also includes the approach I have used to generate and update the guidelines that are now widely used in the autophagy field. The suggestions are not meant to be formulaic, and the method is certainly not perfect. Instead, this should be viewed as a starting set of, well, guidelines.
doi:10.1091/mbc.E15-09-0618
PMCID: PMC4803299  PMID: 26915690
19.  Toward an understanding of autophagosome-lysosome fusion: The unsuspected role of ATG14 
Autophagy  2015;11(4):583-584.
Although largely overlooked relative to the process of phagophore formation, the mechanism through which autophagosomes fuse with lysosomes is a critical aspect of macroautophagy that is not fully understood. In particular, this step must be carefully regulated to prevent premature fusion of an incomplete autophagosome (that is, a phagophore) with a lysosome, because such an event would not allow access of the partially sequestered cargo to the lysosome lumen. The identification of the autophagosome-associated SNARE protein STX17 (syntaxin 17) provided some clue in the understanding of this process. STX17 is recruited specifically to mature autophagosomes, and functions in mediating autophagosome-lysosome fusion by forming a complex with the Qbc SNARE SNAP29 and the lysosomal R-SNARE VAMP8. Additionally, STX17 plays a role in the early events of autophagy by interacting with the phosphatidylinositol 3-kinase complex component ATG14. Upon autophagy induction STX17 is strictly required for ATG14 recruitment to the ER-mitochondria contact sites, a critical step for the assembly of the phagophore and therefore for autophagosome formation. In their recent paper, Diao and collaborators now show that the ATG14-STX17-SNAP29 interaction mediates autophagosome-lysosome tethering and fusion events, thus revealing a novel function of ATG14 in the later steps of the autophagy pathway.
doi:10.1080/15548627.2015.1029220
PMCID: PMC4502729  PMID: 25920502
autophagy; fusion; lysosome; SNARE; stress
20.  Long-distance autophagy 
Autophagy  2015;11(2):193-194.
doi:10.1080/15548627.2015.1009790
PMCID: PMC4502707  PMID: 25831012
lysosome; macroautophagy; neuron; phagophore; stress
21.  Autophagy regulates cytoplasmic remodeling during cell reprogramming in a zebrafish model of muscle regeneration 
Autophagy  2016;12(10):1864-1875.
ABSTRACT
Cell identity involves both selective gene activity and specialization of cytoplasmic architecture and protein machinery. Similarly, reprogramming differentiated cells requires both genetic program alterations and remodeling of the cellular architecture. While changes in genetic and epigenetic programs have been well documented in dedifferentiating cells, the pathways responsible for remodeling the cellular architecture and eliminating specialized protein complexes are not as well understood. Here, we utilize a zebrafish model of adult muscle regeneration to study cytoplasmic remodeling during cell dedifferentiation. We describe activation of autophagy early in the regenerative response to muscle injury, while blocking autophagy using chloroquine or Atg5 and Becn1 knockdown reduced the rate of regeneration with accumulation of sarcomeric and nuclear debris. We further identify Casp3/caspase 3 as a candidate mediator of cellular reprogramming and Fgf signaling as an important activator of autophagy in dedifferentiating myocytes. We conclude that autophagy plays a critical role in cell reprogramming by regulating cytoplasmic remodeling, facilitating the transition to a less differentiated cell identity.
doi:10.1080/15548627.2016.1207015
PMCID: PMC5066936  PMID: 27467399
Atg5; autolysosome; dedifferentiation; electron microscopy; extraocular muscle; regeneration; reprogramming; stem cell; strabismus; zebrafish
22.  Alternative autophagy, brefeldin A and viral trafficking pathways 
Autophagy  2016;12(9):1429-1430.
ABSTRACT
Two topics that have attracted recent attention in the field of autophagy concern the source of the membrane that is used to form the autophagosome during macroautophagy and the role of noncanonical autophagic pathways. The 2 topics may converge when considering the intersection of autophagy with viral infection. We suggest that noncanonical autophagy, which is sensitive to treatment with brefeldin A, may converge with the infectious cycles of certain DNA and RNA viruses that utilize membrane from the ER and cis-Golgi.
doi:10.1080/15548627.2016.1203489
PMCID: PMC5082769  PMID: 27439673
autophagy; Beclin 1; brefeldin A; coronavirus; Ebola virus; herpesvirus
23.  Rph1 mediates the nutrient-limitation signaling pathway leading to transcriptional activation of autophagy 
Autophagy  2015;11(4):718-719.
To maintain proper cellular homeostasis, the magnitude of autophagy activity has to be finely tuned in response to environmental changes. Many aspects of autophagy regulation have been extensively studied: pathways integrating signals through the master regulators TORC1 and PKA lead to multiple post-translational modifications affecting the functions, protein-protein interactions, and localization of Atg proteins. The expression of several ATG genes increases sharply upon autophagy induction conditions, and defects in ATG gene expression are associated with various diseases, pointing to the importance of transcriptional regulation of autophagy. Yet, how changes in ATG gene expression affect the rate of autophagy is not well characterized, and transcriptional regulators of the autophagy pathway remain largely unknown. To identify such regulators, we analyzed the expression of several ATG genes in a library of DNA-binding protein mutants. This led to the identification of Rph1 as a master transcriptional regulator of autophagy.
doi:10.1080/15548627.2015.1018503
PMCID: PMC4502745  PMID: 25751780
autophagy; lysosome; stress; vacuole; yeast
24.  The yeast Saccharomyces cerevisiae: an overview of methods to study autophagy progression 
Macroautophagy (hereafter autophagy) is a highly evolutionarily conserved process essential for sustaining cellular integrity, homeostasis, and survival. Most eukaryotic cells constitutively undergo autophagy at a low basal level. However, various stimuli, including starvation, organelle deterioration, stress, and pathogen infection, potently upregulate autophagy. The hallmark morphological feature of autophagy is the formation of the double-membrane vesicle known as the autophagosome. In yeast, flux through the pathway culminates in autophagosome-vacuole fusion, and the subsequent degradation of the resulting autophagic bodies and cargo by vacuolar hydrolases, followed by efflux of the breakdown products. Importantly, aberrant autophagy is associated with diverse human pathologies. Thus, there is a need for ongoing work in this area to further understand the cellular factors regulating this process. The field of autophagy research has grown exponentially in recent years, and although numerous model organisms are being used to investigate autophagy, the baker’s yeast Saccharomyces cerevisiae remains highly relevant, as there are significant and unique benefits to working with this organism. In this review, we will focus on the current methods available to evaluate and monitor autophagy in S. cerevisiae, which in several cases have also been subsequently exploited in higher eukaryotes.
doi:10.1016/j.ymeth.2014.12.008
PMCID: PMC4355233  PMID: 25526918
Atg8; autophagosome; mitophagy; PAS; phagophore; vacuole
25.  Quiltophagy—autophagy as folk art 
Autophagy  2015;11(2):195-199.
Over the years macroautophagy (hereafter autophagy) has been depicted artistically through painting, music, dance, videos, and poetry. A unifying idea behind these different aesthetic approaches is that people learn in different ways. Thus, some learners may be engaged by a detailed, but static, painting, whereas others may find insight through the dynamic visualization provided by a dance. While each of these formats has advantages, they also have a common weakness—whether delivered through watercolor on a canvas, words on a paper, or movement captured in a video, they are all 2-dimensional. Yet, some people are tactile learners. In this paper, a quilter describes a project she created with the goal of demonstrating autophagy using a 3-dimensional approach, in which different fiber textures could be used to elaborate certain parts of the process.
doi:10.1080/15548627.2015.1017196
PMCID: PMC4502796  PMID: 25714985
autophagy; fabric; lysosome; quilt; stress; vacuole; yarn; yeast

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