PMCCPMCCPMCC

Search tips
Search criteria 

Advanced

 
Logo of molmedLink to Publisher's site
 
Mol Med. 1998 December; 4(12): 751–769.
PMCID: PMC2230389

Janus kinases and focal adhesion kinases play in the 4.1 band: a superfamily of band 4.1 domains important for cell structure and signal transduction.

Abstract

The band 4.1 domain was first identified in the red blood cell protein band 4.1, and subsequently in ezrin, radixin, and moesin (ERM proteins) and other proteins, including tumor suppressor merlin/schwannomin, talin, unconventional myosins VIIa and X, and protein tyrosine phosphatases. Recently, the presence of a structurally related domain has been demonstrated in the N-terminal region of two groups of tyrosine kinases: the focal adhesion kinases (FAK) and the Janus kinases (JAK). Additional proteins containing the 4.1/JEF (JAK, ERM, FAK) domain include plant kinesin-like calmodulin-binding proteins (KCBP) and a number of uncharacterized open reading frames identified by systematic DNA sequencing. Phylogenetic analysis of amino acid sequences suggests that band 4.1/JEF domains can be grouped in several families that have probably diverged early during evolution. Hydrophobic cluster analysis indicates that the band 4.1/JEF domains might consist of a duplicated module of approximately 140 residues and a central hinge region. A conserved property of the domain is its capacity to bind to the membrane-proximal region of the C-terminal cytoplasmic tail of proteins with a single transmembrane segment. Many proteins with band 4.1/JEF domains undergo regulated intra- or intermolecular homotypic interactions. Additional properties common to band 4.1/JEF domains of several proteins are binding of phosphoinositides and regulation by GTPases of the Rho family. Many proteins with band 4. 1/JEF domains are associated with the actin-based cytoskeleton and are enriched at points of contact with other cells or the extracellular matrix, from which they can exert control over cell growth. Thus, proteins with band 4.1/JEF domain are at the crossroads between cytoskeletal organization and signal transduction in multicellular organisms. Their importance is underlined by the variety of diseases that can result from their mutations.

Full text

Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (4.2M), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References.

Images in this article

Click on the image to see a larger version.

Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Pawson T, Scott JD. Signaling through scaffold, anchoring, and adaptor proteins. Science. 1997 Dec 19;278(5346):2075–2080. [PubMed]
  • Casey PJ. Protein lipidation in cell signaling. Science. 1995 Apr 14;268(5208):221–225. [PubMed]
  • Shao X, Davletov BA, Sutton RB, Südhof TC, Rizo J. Bipartite Ca2+-binding motif in C2 domains of synaptotagmin and protein kinase C. Science. 1996 Jul 12;273(5272):248–251. [PubMed]
  • Kuriyan J, Cowburn D. Modular peptide recognition domains in eukaryotic signaling. Annu Rev Biophys Biomol Struct. 1997;26:259–288. [PubMed]
  • Sudol M. From Src Homology domains to other signaling modules: proposal of the 'protein recognition code'. Oncogene. 1998 Sep 17;17(11 REVIEWS):1469–1474. [PubMed]
  • Pawson T. Protein modules and signalling networks. Nature. 1995 Feb 16;373(6515):573–580. [PubMed]
  • Hüttelmaier S, Mayboroda O, Harbeck B, Jarchau T, Jockusch BM, Rüdiger M. The interaction of the cell-contact proteins VASP and vinculin is regulated by phosphatidylinositol-4,5-bisphosphate. Curr Biol. 1998 Apr 23;8(9):479–488. [PubMed]
  • Fushman D, Najmabadi-Haske T, Cahill S, Zheng J, LeVine H, 3rd, Cowburn D. The solution structure and dynamics of the pleckstrin homology domain of G protein-coupled receptor kinase 2 (beta-adrenergic receptor kinase 1). A binding partner of Gbetagamma subunits. J Biol Chem. 1998 Jan 30;273(5):2835–2843. [PubMed]
  • Arpin M, Algrain M, Louvard D. Membrane-actin microfilament connections: an increasing diversity of players related to band 4.1. Curr Opin Cell Biol. 1994 Feb;6(1):136–141. [PubMed]
  • Tsukita S, Yonemura S. ERM (ezrin/radixin/moesin) family: from cytoskeleton to signal transduction. Curr Opin Cell Biol. 1997 Feb;9(1):70–75. [PubMed]
  • Leto TL, Marchesi VT. A structural model of human erythrocyte protein 4.1. J Biol Chem. 1984 Apr 10;259(7):4603–4608. [PubMed]
  • Anderson RA, Marchesi VT. Regulation of the association of membrane skeletal protein 4.1 with glycophorin by a polyphosphoinositide. Nature. 1985 Nov 21;318(6043):295–298. [PubMed]
  • Chishti AH, Kim AC, Marfatia SM, Lutchman M, Hanspal M, Jindal H, Liu SC, Low PS, Rouleau GA, Mohandas N, et al. The FERM domain: a unique module involved in the linkage of cytoplasmic proteins to the membrane. Trends Biochem Sci. 1998 Aug;23(8):281–282. [PubMed]
  • Schultz J, Milpetz F, Bork P, Ponting CP. SMART, a simple modular architecture research tool: identification of signaling domains. Proc Natl Acad Sci U S A. 1998 May 26;95(11):5857–5864. [PubMed]
  • Gaboriaud C, Bissery V, Benchetrit T, Mornon JP. Hydrophobic cluster analysis: an efficient new way to compare and analyse amino acid sequences. FEBS Lett. 1987 Nov 16;224(1):149–155. [PubMed]
  • Callebaut I, Labesse G, Durand P, Poupon A, Canard L, Chomilier J, Henrissat B, Mornon JP. Deciphering protein sequence information through hydrophobic cluster analysis (HCA): current status and perspectives. Cell Mol Life Sci. 1997 Aug;53(8):621–645. [PubMed]
  • Woodcock S, Mornon JP, Henrissat B. Detection of secondary structure elements in proteins by hydrophobic cluster analysis. Protein Eng. 1992 Oct;5(7):629–635. [PubMed]
  • Marfatia SM, Leu RA, Branton D, Chishti AH. Identification of the protein 4.1 binding interface on glycophorin C and p55, a homologue of the Drosophila discs-large tumor suppressor protein. J Biol Chem. 1995 Jan 13;270(2):715–719. [PubMed]
  • Hemming NJ, Anstee DJ, Mawby WJ, Reid ME, Tanner MJ. Localization of the protein 4.1-binding site on human erythrocyte glycophorins C and D. Biochem J. 1994 Apr 1;299(Pt 1):191–196. [PubMed]
  • Lombardo CR, Willardson BM, Low PS. Localization of the protein 4.1-binding site on the cytoplasmic domain of erythrocyte membrane band 3. J Biol Chem. 1992 May 15;267(14):9540–9546. [PubMed]
  • Nunomura W, Takakuwa Y, Tokimitsu R, Krauss SW, Kawashima M, Mohandas N. Regulation of CD44-protein 4.1 interaction by Ca2+ and calmodulin. Implications for modulation of CD44-ankyrin interaction. J Biol Chem. 1997 Nov 28;272(48):30322–30328. [PubMed]
  • Jöns T, Drenckhahn D. Identification of the binding interface involved in linkage of cytoskeletal protein 4.1 to the erythrocyte anion exchanger. EMBO J. 1992 Aug;11(8):2863–2867. [PubMed]
  • Marfatia SM, Lue RA, Branton D, Chishti AH. In vitro binding studies suggest a membrane-associated complex between erythroid p55, protein 4.1, and glycophorin C. J Biol Chem. 1994 Mar 25;269(12):8631–8634. [PubMed]
  • Marfatia SM, Morais-Cabral JH, Kim AC, Byron O, Chishti AH. The PDZ domain of human erythrocyte p55 mediates its binding to the cytoplasmic carboxyl terminus of glycophorin C. Analysis of the binding interface by in vitro mutagenesis. J Biol Chem. 1997 Sep 26;272(39):24191–24197. [PubMed]
  • Huang JP, Tang CJ, Kou GH, Marchesi VT, Benz EJ, Jr, Tang TK. Genomic structure of the locus encoding protein 4.1. Structural basis for complex combinational patterns of tissue-specific alternative RNA splicing. J Biol Chem. 1993 Feb 15;268(5):3758–3766. [PubMed]
  • Baklouti F, Huang SC, Vulliamy TJ, Delaunay J, Benz EJ., Jr Organization of the human protein 4.1 genomic locus: new insights into the tissue-specific alternative splicing of the pre-mRNA. Genomics. 1997 Feb 1;39(3):289–302. [PubMed]
  • Walensky LD, Gascard P, Fields ME, Blackshaw S, Conboy JG, Mohandas N, Snyder SH. The 13-kD FK506 binding protein, FKBP13, interacts with a novel homologue of the erythrocyte membrane cytoskeletal protein 4.1. J Cell Biol. 1998 Apr 6;141(1):143–153. [PMC free article] [PubMed]
  • Takeuchi K, Kawashima A, Nagafuchi A, Tsukita S. Structural diversity of band 4.1 superfamily members. J Cell Sci. 1994 Jul;107(Pt 7):1921–1928. [PubMed]
  • Kelly GM, Reversade B. Characterization of a cDNA encoding a novel band 4.1-like protein in zebrafish. Biochem Cell Biol. 1997;75(5):623–632. [PubMed]
  • Fehon RG, Dawson IA, Artavanis-Tsakonas S. A Drosophila homologue of membrane-skeleton protein 4.1 is associated with septate junctions and is encoded by the coracle gene. Development. 1994 Mar;120(3):545–557. [PubMed]
  • Koyano Y, Kawamoto T, Shen M, Yan W, Noshiro M, Fujii K, Kato Y. Molecular cloning and characterization of CDEP, a novel human protein containing the ezrin-like domain of the band 4.1 superfamily and the Dbl homology domain of Rho guanine nucleotide exchange factors. Biochem Biophys Res Commun. 1997 Dec 18;241(2):369–375. [PubMed]
  • Menegoz M, Gaspar P, Le Bert M, Galvez T, Burgaya F, Palfrey C, Ezan P, Arnos F, Girault JA. Paranodin, a glycoprotein of neuronal paranodal membranes. Neuron. 1997 Aug;19(2):319–331. [PubMed]
  • Peles E, Nativ M, Lustig M, Grumet M, Schilling J, Martinez R, Plowman GD, Schlessinger J. Identification of a novel contactin-associated transmembrane receptor with multiple domains implicated in protein-protein interactions. EMBO J. 1997 Mar 3;16(5):978–988. [PubMed]
  • Baumgartner S, Littleton JT, Broadie K, Bhat MA, Harbecke R, Lengyel JA, Chiquet-Ehrismann R, Prokop A, Bellen HJ. A Drosophila neurexin is required for septate junction and blood-nerve barrier formation and function. Cell. 1996 Dec 13;87(6):1059–1068. [PubMed]
  • Littleton JT, Bhat MA, Bellen HJ. Deciphering the function of neurexins at cellular junctions. J Cell Biol. 1997 May 19;137(4):793–796. [PMC free article] [PubMed]
  • Hata Y, Butz S, Südhof TC. CASK: a novel dlg/PSD95 homolog with an N-terminal calmodulin-dependent protein kinase domain identified by interaction with neurexins. J Neurosci. 1996 Apr 15;16(8):2488–2494. [PubMed]
  • Cohen AR, Woods DF, Marfatia SM, Walther Z, Chishti AH, Anderson JM, Wood DF. Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to the basolateral membrane of epithelial cells. J Cell Biol. 1998 Jul 13;142(1):129–138. [PMC free article] [PubMed]
  • Altschul SF, Madden TL, Schäffer AA, Zhang J, Zhang Z, Miller W, Lipman DJ. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 1997 Sep 1;25(17):3389–3402. [PMC free article] [PubMed]
  • Turunen O, Sainio M, Jäskeläinen J, Carpén O, Vaheri A. Structure-function relationships in the ezrin family and the effect of tumor-associated point mutations in neurofibromatosis 2 protein. Biochim Biophys Acta. 1998 Sep 8;1387(1-2):1–16. [PubMed]
  • Roy C, Martin M, Mangeat P. A dual involvement of the amino-terminal domain of ezrin in F- and G-actin binding. J Biol Chem. 1997 Aug 8;272(32):20088–20095. [PubMed]
  • Tsukita S, Yonemura S, Tsukita S. ERM proteins: head-to-tail regulation of actin-plasma membrane interaction. Trends Biochem Sci. 1997 Feb;22(2):53–58. [PubMed]
  • Serrador JM, Alonso-Lebrero JL, del Pozo MA, Furthmayr H, Schwartz-Albiez R, Calvo J, Lozano F, Sánchez-Madrid F. Moesin interacts with the cytoplasmic region of intercellular adhesion molecule-3 and is redistributed to the uropod of T lymphocytes during cell polarization. J Cell Biol. 1997 Sep 22;138(6):1409–1423. [PMC free article] [PubMed]
  • Yonemura S, Hirao M, Doi Y, Takahashi N, Kondo T, Tsukita S, Tsukita S. Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2. J Cell Biol. 1998 Feb 23;140(4):885–895. [PMC free article] [PubMed]
  • Murthy A, Gonzalez-Agosti C, Cordero E, Pinney D, Candia C, Solomon F, Gusella J, Ramesh V. NHE-RF, a regulatory cofactor for Na(+)-H+ exchange, is a common interactor for merlin and ERM (MERM) proteins. J Biol Chem. 1998 Jan 16;273(3):1273–1276. [PubMed]
  • Reczek D, Berryman M, Bretscher A. Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family. J Cell Biol. 1997 Oct 6;139(1):169–179. [PMC free article] [PubMed]
  • Takahashi K, Sasaki T, Mammoto A, Takaishi K, Kameyama T, Tsukita S, Takai Y. Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein. J Biol Chem. 1997 Sep 12;272(37):23371–23375. [PubMed]
  • Mackay DJ, Esch F, Furthmayr H, Hall A. Rho- and rac-dependent assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: an essential role for ezrin/radixin/moesin proteins. J Cell Biol. 1997 Aug 25;138(4):927–938. [PMC free article] [PubMed]
  • Magendantz M, Henry MD, Lander A, Solomon F. Interdomain interactions of radixin in vitro. J Biol Chem. 1995 Oct 27;270(43):25324–25327. [PubMed]
  • Bretscher A, Gary R, Berryman M. Soluble ezrin purified from placenta exists as stable monomers and elongated dimers with masked C-terminal ezrin-radixin-moesin association domains. Biochemistry. 1995 Dec 26;34(51):16830–16837. [PubMed]
  • Berryman M, Gary R, Bretscher A. Ezrin oligomers are major cytoskeletal components of placental microvilli: a proposal for their involvement in cortical morphogenesis. J Cell Biol. 1995 Dec;131(5):1231–1242. [PMC free article] [PubMed]
  • Niggli V, Andréoli C, Roy C, Mangeat P. Identification of a phosphatidylinositol-4,5-bisphosphate-binding domain in the N-terminal region of ezrin. FEBS Lett. 1995 Dec 4;376(3):172–176. [PubMed]
  • Hirao M, Sato N, Kondo T, Yonemura S, Monden M, Sasaki T, Takai Y, Tsukita S, Tsukita S. Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway. J Cell Biol. 1996 Oct;135(1):37–51. [PMC free article] [PubMed]
  • Matsui T, Maeda M, Doi Y, Yonemura S, Amano M, Kaibuchi K, Tsukita S, Tsukita S. Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association. J Cell Biol. 1998 Feb 9;140(3):647–657. [PMC free article] [PubMed]
  • Rouleau GA, Merel P, Lutchman M, Sanson M, Zucman J, Marineau C, Hoang-Xuan K, Demczuk S, Desmaze C, Plougastel B, et al. Alteration in a new gene encoding a putative membrane-organizing protein causes neuro-fibromatosis type 2. Nature. 1993 Jun 10;363(6429):515–521. [PubMed]
  • Trofatter JA, MacCollin MM, Rutter JL, Murrell JR, Duyao MP, Parry DM, Eldridge R, Kley N, Menon AG, Pulaski K, et al. A novel moesin-, ezrin-, radixin-like gene is a candidate for the neurofibromatosis 2 tumor suppressor. Cell. 1993 Mar 12;72(5):791–800. [PubMed]
  • Sainio M, Zhao F, Heiska L, Turunen O, den Bakker M, Zwarthoff E, Lutchman M, Rouleau GA, Jäskeläinen J, Vaheri A, et al. Neurofibromatosis 2 tumor suppressor protein colocalizes with ezrin and CD44 and associates with actin-containing cytoskeleton. J Cell Sci. 1997 Sep;110(Pt 18):2249–2260. [PubMed]
  • Xu L, Gonzalez-Agosti C, Beauchamp R, Pinney D, Sterner C, Ramesh V. Analysis of molecular domains of epitope-tagged merlin isoforms in Cos-7 cells and primary rat Schwann cells. Exp Cell Res. 1998 Jan 10;238(1):231–240. [PubMed]
  • Deguen B, Mérel P, Goutebroze L, Giovannini M, Reggio H, Arpin M, Thomas G. Impaired interaction of naturally occurring mutant NF2 protein with actin-based cytoskeleton and membrane. Hum Mol Genet. 1998 Feb;7(2):217–226. [PubMed]
  • Xu HM, Gutmann DH. Merlin differentially associates with the microtubule and actin cytoskeleton. J Neurosci Res. 1998 Feb 1;51(3):403–415. [PubMed]
  • Scoles DR, Huynh DP, Morcos PA, Coulsell ER, Robinson NG, Tamanoi F, Pulst SM. Neurofibromatosis 2 tumour suppressor schwannomin interacts with betaII-spectrin. Nat Genet. 1998 Apr;18(4):354–359. [PubMed]
  • McCartney BM, Fehon RG. Distinct cellular and subcellular patterns of expression imply distinct functions for the Drosophila homologues of moesin and the neurofibromatosis 2 tumor suppressor, merlin. J Cell Biol. 1996 May;133(4):843–852. [PMC free article] [PubMed]
  • LaJeunesse DR, McCartney BM, Fehon RG. Structural analysis of Drosophila merlin reveals functional domains important for growth control and subcellular localization. J Cell Biol. 1998 Jun 29;141(7):1589–1599. [PMC free article] [PubMed]
  • McClatchey AI, Saotome I, Mercer K, Crowley D, Gusella JF, Bronson RT, Jacks T. Mice heterozygous for a mutation at the Nf2 tumor suppressor locus develop a range of highly metastatic tumors. Genes Dev. 1998 Apr 15;12(8):1121–1133. [PubMed]
  • Boedigheimer MJ, Nguyen KP, Bryant PJ. Expanded functions in the apical cell domain to regulate the growth rate of imaginal discs. Dev Genet. 1997;20(2):103–110. [PubMed]
  • Matsumine A, Ogai A, Senda T, Okumura N, Satoh K, Baeg GH, Kawahara T, Kobayashi S, Okada M, Toyoshima K, et al. Binding of APC to the human homolog of the Drosophila discs large tumor suppressor protein. Science. 1996 May 17;272(5264):1020–1023. [PubMed]
  • Taylor JM, Richardson A, Parsons JT. Modular domains of focal adhesion-associated proteins. Curr Top Microbiol Immunol. 1998;228:135–163. [PubMed]
  • Chen HC, Appeddu PA, Parsons JT, Hildebrand JD, Schaller MD, Guan JL. Interaction of focal adhesion kinase with cytoskeletal protein talin. J Biol Chem. 1995 Jul 14;270(28):16995–16999. [PubMed]
  • Titus MA. Unconventional myosins: new frontiers in actin-based motors. Trends Cell Biol. 1997 Mar;7(3):119–123. [PubMed]
  • Mermall V, Post PL, Mooseker MS. Unconventional myosins in cell movement, membrane traffic, and signal transduction. Science. 1998 Jan 23;279(5350):527–533. [PubMed]
  • Reddy AS, Safadi F, Narasimhulu SB, Golovkin M, Hu X. A novel plant calmodulin-binding protein with a kinesin heavy chain motor domain. J Biol Chem. 1996 Mar 22;271(12):7052–7060. [PubMed]
  • Bowser J, Reddy AS. Localization of a kinesin-like calmodulin-binding protein in dividing cells of Arabidopsis and tobacco. Plant J. 1997 Dec;12(6):1429–1437. [PubMed]
  • Yang Q, Tonks NK. Isolation of a cDNA clone encoding a human protein-tyrosine phosphatase with homology to the cytoskeletal-associated proteins band 4.1, ezrin, and talin. Proc Natl Acad Sci U S A. 1991 Jul 15;88(14):5949–5953. [PubMed]
  • Gu MX, York JD, Warshawsky I, Majerus PW. Identification, cloning, and expression of a cytosolic megakaryocyte protein-tyrosine-phosphatase with sequence homology to cytoskeletal protein 4.1. Proc Natl Acad Sci U S A. 1991 Jul 1;88(13):5867–5871. [PubMed]
  • Sawada M, Ogata M, Fujino Y, Hamaoka T. cDNA cloning of a novel protein tyrosine phosphatase with homology to cytoskeletal protein 4.1 and its expression in T-lineage cells. Biochem Biophys Res Commun. 1994 Aug 30;203(1):479–484. [PubMed]
  • Smith AL, Mitchell PJ, Shipley J, Gusterson BA, Rogers MV, Crompton MR. Pez: a novel human cDNA encoding protein tyrosine phosphatase- and ezrin-like domains. Biochem Biophys Res Commun. 1995 Apr 26;209(3):959–965. [PubMed]
  • Møller NP, Møller KB, Lammers R, Kharitonenkov A, Sures I, Ullrich A. Src kinase associates with a member of a distinct subfamily of protein-tyrosine phosphatases containing an ezrin-like domain. Proc Natl Acad Sci U S A. 1994 Aug 2;91(16):7477–7481. [PubMed]
  • Higashitsuji H, Arii S, Furutani M, Imamura M, Kaneko Y, Takenawa J, Nakayama H, Fujita J. Enhanced expression of multiple protein tyrosine phosphatases in the regenerating mouse liver: isolation of PTP-RL10, a novel cytoplasmic-type phosphatase with sequence homology to cytoskeletal protein 4.1. Oncogene. 1995 Jan 19;10(2):407–414. [PubMed]
  • L'Abbé D, Banville D, Tong Y, Stocco R, Masson S, Ma S, Fantus G, Shen SH. Identification of a novel protein tyrosine phosphatase with sequence homology to the cytoskeletal proteins of the band 4.1 family. FEBS Lett. 1994 Dec 19;356(2-3):351–356. [PubMed]
  • Maekawa K, Imagawa N, Nagamatsu M, Harada S. Molecular cloning of a novel protein-tyrosine phosphatase containing a membrane-binding domain and GLGF repeats. FEBS Lett. 1994 Jan 10;337(2):200–206. [PubMed]
  • Hendriks W, Schepens J, Bächner D, Rijss J, Zeeuwen P, Zechner U, Hameister H, Wieringa B. Molecular cloning of a mouse epithelial protein-tyrosine phosphatase with similarities to submembranous proteins. J Cell Biochem. 1995 Dec;59(4):418–430. [PubMed]
  • Banville D, Ahmad S, Stocco R, Shen SH. A novel protein-tyrosine phosphatase with homology to both the cytoskeletal proteins of the band 4.1 family and junction-associated guanylate kinases. J Biol Chem. 1994 Sep 2;269(35):22320–22327. [PubMed]
  • Saras J, Claesson-Welsh L, Heldin CH, Gonez LJ. Cloning and characterization of PTPL1, a protein tyrosine phosphatase with similarities to cytoskeletal-associated proteins. J Biol Chem. 1994 Sep 30;269(39):24082–24089. [PubMed]
  • Sato T, Irie S, Kitada S, Reed JC. FAP-1: a protein tyrosine phosphatase that associates with Fas. Science. 1995 Apr 21;268(5209):411–415. [PubMed]
  • Cuppen E, Nagata S, Wieringa B, Hendriks W. No evidence for involvement of mouse protein-tyrosine phosphatase-BAS-like Fas-associated phosphatase-1 in Fas-mediated apoptosis. J Biol Chem. 1997 Nov 28;272(48):30215–30220. [PubMed]
  • Schaller MD, Borgman CA, Cobb BS, Vines RR, Reynolds AB, Parsons JT. pp125FAK a structurally distinctive protein-tyrosine kinase associated with focal adhesions. Proc Natl Acad Sci U S A. 1992 Jun 1;89(11):5192–5196. [PubMed]
  • Hanks SK, Calalb MB, Harper MC, Patel SK. Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin. Proc Natl Acad Sci U S A. 1992 Sep 15;89(18):8487–8491. [PubMed]
  • Ilić D, Furuta Y, Kanazawa S, Takeda N, Sobue K, Nakatsuji N, Nomura S, Fujimoto J, Okada M, Yamamoto T. Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice. Nature. 1995 Oct 12;377(6549):539–544. [PubMed]
  • Otey CA. pp125FAK in the focal adhesion. Int Rev Cytol. 1996;167:161–183. [PubMed]
  • Ilić D, Damsky CH, Yamamoto T. Focal adhesion kinase: at the crossroads of signal transduction. J Cell Sci. 1997 Feb;110(Pt 4):401–407. [PubMed]
  • Richardson A, Parsons JT. Signal transduction through integrins: a central role for focal adhesion kinase? Bioessays. 1995 Mar;17(3):229–236. [PubMed]
  • Schlaepfer DD, Hunter T. Integrin signalling and tyrosine phosphorylation: just the FAKs? Trends Cell Biol. 1998 Apr;8(4):151–157. [PubMed]
  • Hildebrand JD, Schaller MD, Parsons JT. Identification of sequences required for the efficient localization of the focal adhesion kinase, pp125FAK, to cellular focal adhesions. J Cell Biol. 1993 Nov;123(4):993–1005. [PMC free article] [PubMed]
  • Schaller MD, Otey CA, Hildebrand JD, Parsons JT. Focal adhesion kinase and paxillin bind to peptides mimicking beta integrin cytoplasmic domains. J Cell Biol. 1995 Sep;130(5):1181–1187. [PMC free article] [PubMed]
  • Chan PY, Kanner SB, Whitney G, Aruffo A. A transmembrane-anchored chimeric focal adhesion kinase is constitutively activated and phosphorylated at tyrosine residues identical to pp125FAK. J Biol Chem. 1994 Aug 12;269(32):20567–20574. [PubMed]
  • Eide BL, Turck CW, Escobedo JA. Identification of Tyr-397 as the primary site of tyrosine phosphorylation and pp60src association in the focal adhesion kinase, pp125FAK. Mol Cell Biol. 1995 May;15(5):2819–2827. [PMC free article] [PubMed]
  • Burgaya F, Toutant M, Studler JM, Costa A, Le Bert M, Gelman M, Girault JA. Alternatively spliced focal adhesion kinase in rat brain with increased autophosphorylation activity. J Biol Chem. 1997 Nov 7;272(45):28720–28725. [PubMed]
  • Lev S, Moreno H, Martinez R, Canoll P, Peles E, Musacchio JM, Plowman GD, Rudy B, Schlessinger J. Protein tyrosine kinase PYK2 involved in Ca(2+)-induced regulation of ion channel and MAP kinase functions. Nature. 1995 Aug 31;376(6543):737–745. [PubMed]
  • Sasaki H, Nagura K, Ishino M, Tobioka H, Kotani K, Sasaki T. Cloning and characterization of cell adhesion kinase beta, a novel protein-tyrosine kinase of the focal adhesion kinase subfamily. J Biol Chem. 1995 Sep 8;270(36):21206–21219. [PubMed]
  • Avraham S, London R, Fu Y, Ota S, Hiregowdara D, Li J, Jiang S, Pasztor LM, White RA, Groopman JE, et al. Identification and characterization of a novel related adhesion focal tyrosine kinase (RAFTK) from megakaryocytes and brain. J Biol Chem. 1995 Nov 17;270(46):27742–27751. [PubMed]
  • Yu H, Li X, Marchetto GS, Dy R, Hunter D, Calvo B, Dawson TL, Wilm M, Anderegg RJ, Graves LM, et al. Activation of a novel calcium-dependent protein-tyrosine kinase. Correlation with c-Jun N-terminal kinase but not mitogen-activated protein kinase activation. J Biol Chem. 1996 Nov 22;271(47):29993–29998. [PubMed]
  • Herzog H, Nicholl J, Hort YJ, Sutherland GR, Shine J. Molecular cloning and assignment of FAK2, a novel human focal adhesion kinase, to 8p11.2-p22 by nonisotopic in situ hybridization. Genomics. 1996 Mar 15;32(3):484–486. [PubMed]
  • Schaller MD, Sasaki T. Differential signaling by the focal adhesion kinase and cell adhesion kinase beta. J Biol Chem. 1997 Oct 3;272(40):25319–25325. [PubMed]
  • Dikic I, Tokiwa G, Lev S, Courtneidge SA, Schlessinger J. A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation. Nature. 1996 Oct 10;383(6600):547–550. [PubMed]
  • Siciliano JC, Toutant M, Derkinderen P, Sasaki T, Girault JA. Differential regulation of proline-rich tyrosine kinase 2/cell adhesion kinase beta (PYK2/CAKbeta) and pp125(FAK) by glutamate and depolarization in rat hippocampus. J Biol Chem. 1996 Nov 15;271(46):28942–28946. [PubMed]
  • Hiregowdara D, Avraham H, Fu Y, London R, Avraham S. Tyrosine phosphorylation of the related adhesion focal tyrosine kinase in megakaryocytes upon stem cell factor and phorbol myristate acetate stimulation and its association with paxillin. J Biol Chem. 1997 Apr 18;272(16):10804–10810. [PubMed]
  • Raja S, Avraham S, Avraham H. Tyrosine phosphorylation of the novel protein-tyrosine kinase RAFTK during an early phase of platelet activation by an integrin glycoprotein IIb-IIIa-independent mechanism. J Biol Chem. 1997 Apr 18;272(16):10941–10947. [PubMed]
  • Soltoff SP, Avraham H, Avraham S, Cantley LC. Activation of P2Y2 receptors by UTP and ATP stimulates mitogen-activated kinase activity through a pathway that involves related adhesion focal tyrosine kinase and protein kinase C. J Biol Chem. 1998 Jan 30;273(5):2653–2660. [PubMed]
  • Pellegrini S, Dusanter-Fourt I. The structure, regulation and function of the Janus kinases (JAKs) and the signal transducers and activators of transcription (STATs). Eur J Biochem. 1997 Sep 15;248(3):615–633. [PubMed]
  • Bork P, Gibson TJ. Applying motif and profile searches. Methods Enzymol. 1996;266:162–184. [PubMed]
  • Richter MF, Duménil G, Uzé G, Fellous M, Pellegrini S. Specific contribution of Tyk2 JH regions to the binding and the expression of the interferon alpha/beta receptor component IFNAR1. J Biol Chem. 1998 Sep 18;273(38):24723–24729. [PubMed]
  • Murakami M, Narazaki M, Hibi M, Yawata H, Yasukawa K, Hamaguchi M, Taga T, Kishimoto T. Critical cytoplasmic region of the interleukin 6 signal transducer gp130 is conserved in the cytokine receptor family. Proc Natl Acad Sci U S A. 1991 Dec 15;88(24):11349–11353. [PubMed]
  • Nelson BH, Lord JD, Greenberg PD. A membrane-proximal region of the interleukin-2 receptor gamma c chain sufficient for Jak kinase activation and induction of proliferation in T cells. Mol Cell Biol. 1996 Jan;16(1):309–317. [PMC free article] [PubMed]
  • Kaplan DH, Greenlund AC, Tanner JW, Shaw AS, Schreiber RD. Identification of an interferon-gamma receptor alpha chain sequence required for JAK-1 binding. J Biol Chem. 1996 Jan 5;271(1):9–12. [PubMed]
  • Zhu T, Goh EL, Lobie PE. Growth hormone stimulates the tyrosine phosphorylation and association of p125 focal adhesion kinase (FAK) with JAK2. Fak is not required for stat-mediated transcription. J Biol Chem. 1998 Apr 24;273(17):10682–10689. [PubMed]
  • Rankin S, Morii N, Narumiya S, Rozengurt E. Botulinum C3 exoenzyme blocks the tyrosine phosphorylation of p125FAK and paxillin induced by bombesin and endothelin. FEBS Lett. 1994 Nov 14;354(3):315–319. [PubMed]
  • Seufferlein T, Rozengurt E. Sphingosylphosphorylcholine rapidly induces tyrosine phosphorylation of p125FAK and paxillin, rearrangement of the actin cytoskeleton and focal contact assembly. Requirement of p21rho in the signaling pathway. J Biol Chem. 1995 Oct 13;270(41):24343–24351. [PubMed]
  • Flinn HM, Ridley AJ. Rho stimulates tyrosine phosphorylation of focal adhesion kinase, p130 and paxillin. J Cell Sci. 1996 May;109(Pt 5):1133–1141. [PubMed]
  • Eder PS, Soong CJ, Tao M. Phosphorylation reduces the affinity of protein 4.1 for spectrin. Biochemistry. 1986 Apr 8;25(7):1764–1770. [PubMed]
  • Gould KL, Bretscher A, Esch FS, Hunter T. cDNA cloning and sequencing of the protein-tyrosine kinase substrate, ezrin, reveals homology to band 4.1. EMBO J. 1989 Dec 20;8(13):4133–4142. [PubMed]
  • Hungerford JE, Compton MT, Matter ML, Hoffstrom BG, Otey CA. Inhibition of pp125FAK in cultured fibroblasts results in apoptosis. J Cell Biol. 1996 Dec;135(5):1383–1390. [PMC free article] [PubMed]
  • Delaunay J, Alloisio N, Morle L, Baklouti F, Dalla Venezia N, Maillet P, Wilmotte R. Molecular genetics of hereditary elliptocytosis and hereditary spherocytosis. Ann Genet. 1996;39(4):209–221. [PubMed]
  • Lutchman M, Rouleau GA. Neurofibromatosis type 2: a new mechanism of tumor suppression. Trends Neurosci. 1996 Sep;19(9):373–377. [PubMed]
  • Stemmer-Rachamimov AO, Xu L, Gonzalez-Agosti C, Burwick JA, Pinney D, Beauchamp R, Jacoby LB, Gusella JF, Ramesh V, Louis DN. Universal absence of merlin, but not other ERM family members, in schwannomas. Am J Pathol. 1997 Dec;151(6):1649–1654. [PubMed]
  • Gutmann DH, Giordano MJ, Fishback AS, Guha A. Loss of merlin expression in sporadic meningiomas, ependymomas and schwannomas. Neurology. 1997 Jul;49(1):267–270. [PubMed]
  • Hasson T, Mooseker MS. The growing family of myosin motors and their role in neurons and sensory cells. Curr Opin Neurobiol. 1997 Oct;7(5):615–623. [PubMed]
  • Macchi P, Villa A, Giliani S, Sacco MG, Frattini A, Porta F, Ugazio AG, Johnston JA, Candotti F, O'Shea JJ, et al. Mutations of Jak-3 gene in patients with autosomal severe combined immune deficiency (SCID). Nature. 1995 Sep 7;377(6544):65–68. [PubMed]
  • MacCollin M, Ramesh V, Jacoby LB, Louis DN, Rubio MP, Pulaski K, Trofatter JA, Short MP, Bove C, Eldridge R, et al. Mutational analysis of patients with neurofibromatosis 2. Am J Hum Genet. 1994 Aug;55(2):314–320. [PubMed]
  • Luo H, Hanratty WP, Dearolf CR. An amino acid substitution in the Drosophila hopTum-l Jak kinase causes leukemia-like hematopoietic defects. EMBO J. 1995 Apr 3;14(7):1412–1420. [PubMed]
  • Saitou N, Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol. 1987 Jul;4(4):406–425. [PubMed]

Articles from Molecular Medicine are provided here courtesy of The Feinstein Institute for Medical Research at North Shore LIJ