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1.  A comprehensive glossary of autophagy-related molecules and processes (2nd edition) 
Autophagy  2011;7(11):1273-1294.
The study of autophagy is rapidly expanding, and our knowledge of the molecular mechanism and its connections to a wide range of physiological processes has increased substantially in the past decade. The vocabulary associated with autophagy has grown concomitantly. In fact, it is difficult for readers—even those who work in the field—to keep up with the ever-expanding terminology associated with the various autophagy-related processes. Accordingly, we have developed a comprehensive glossary of autophagy-related terms that is meant to provide a quick reference for researchers who need a brief reminder of the regulatory effects of transcription factors and chemical agents that induce or inhibit autophagy, the function of the autophagy-related proteins, and the roles of accessory components and structures that are associated with autophagy.
doi:10.4161/auto.7.11.17661
PMCID: PMC3359482  PMID: 21997368
autophagy; lysosome; mitophagy; pexophagy; stress; vacuole
2.  Regulation of autophagy by lysosomal positioning 
Autophagy  2011;7(8):927-928.
The mammalian target of rapamycin (mTOR) is a well-conserved negative regulator of autophagy. Here we review our recent data describing how lysosomal positioning influences and coordinates mTOR activity, autophagosome biogenesis and autophagosome-lysosome fusion. In this way, lysosomal positioning regulates many diverse cellular responses to starvation and subsequent nutrient replenishment.
doi:10.4161/auto.7.8.15862
PMCID: PMC3149695  PMID: 21521941
autophagy; lysosome; mTOR; intracellular pH; ARL8; kinesin
3.  The Parkinson disease protein α-synuclein inhibits autophagy 
Autophagy  2011;7(4):429-431.
Parkinson disease (PD) is the most common movement disorder affecting people. It is characterized by the accumulation of the protein α-synuclein in Lewy body inclusions in vulnerable neurons. α-Synuclein overexpression caused by gene multiplications is sufficient to cause this disease, suggesting that α-synuclein accumulation is toxic. Here we review our recent study showing that α-synuclein inhibits autophagy. We discuss our mechanistic understanding of this phenomenon and also speculate how a deficiency in autophagy may contribute to a range of pleiotropic features of PD biology.
doi:10.4161/auto.7.4.14393
PMCID: PMC3127221  PMID: 21157184
Parkinson disease; alpha-synuclein; autophagy; Rab1a; Atg9
4.  Plasma membrane helps autophagosomes grow 
Autophagy  2010;6(8):1184-1186.
The membrane origin of autophagosomes has long been a mystery and it may involve multiple sources. In this punctum, we discuss our recent finding that the plasma membrane contributes to the formation of pre-autophagic structures via clathrin-mediated endocytosis. Our study suggests that Atg16L1 interacts with clathrin heavy-chain/AP2 and is also localized on vesicles (positive for clathrin or cholera toxin B) close to the plasma membrane. Live-cell imaging studies revealed that the plasma membrane contributes to Atg16L1-positive structures and that this process and autophagosome formation are impaired by knockdowns of genes regulating clathrin-mediated endocytosis.
doi:10.4161/auto.6.8.13428
PMCID: PMC3039720  PMID: 20861674
autophagy; plasma membrane; endocytosis; phagophore; origin
5.  Impaired autophagy in Lafora disease 
Autophagy  2010;6(7):991-993.
Lafora disease (LD) is a progressive, lethal, autosomal recessive, neurodegenerative disorder that manifests with myoclonus epilepsy. LD is characterized by the presence of intracellular inclusion bodies called Lafora bodies (LB), in brain, spinal cord and other tissues. More than 50 percent of LD is caused by mutations in EPM2A that encodes laforin. Here we review our recent findings that revealed that laforin regulates autophagy. We consider how autophagy compromise may predispose to LB formation and neurodegeneration in LD, and discuss future investigations suggested by our data.
doi:10.4161/auto.6.7.13308
PMCID: PMC3039746  PMID: 20818165
autophagy; glycogen metabolism; Lafora disease; laforin; malin; neurodegeneration

Results 1-5 (5)