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TCGAP, a multidomain Rho GTPase‐activating protein involved in insulin‐stimulated glucose transport
dc.contributor.authorChiang, Shian‐hueyen_US
dc.contributor.authorHwang, Josephen_US
dc.contributor.authorLegendre, Marieen_US
dc.contributor.authorZhang, Meien_US
dc.contributor.authorKimura, Akikoen_US
dc.contributor.authorSaltiel, Alan R.en_US
dc.date.accessioned2014-01-08T20:34:45Z
dc.date.available2014-01-08T20:34:45Z
dc.date.issued2003-06-01en_US
dc.identifier.citationChiang, Shian‐huey ; Hwang, Joseph; Legendre, Marie; Zhang, Mei; Kimura, Akiko; Saltiel, Alan R. (2003). "TCGAP, a multidomain Rho GTPaseâ activating protein involved in insulinâ stimulated glucose transport." The EMBO Journal 22(11): 2679-2691. <http://hdl.handle.net/2027.42/102135>en_US
dc.identifier.issn0261-4189en_US
dc.identifier.issn1460-2075en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/102135
dc.publisherJohn Wiley & Sons, Ltden_US
dc.subject.otherTCGAPen_US
dc.subject.otherCdc42en_US
dc.subject.otherGLUT4 Translocationen_US
dc.subject.otherInsulinen_US
dc.subject.otherTC10en_US
dc.titleTCGAP, a multidomain Rho GTPase‐activating protein involved in insulin‐stimulated glucose transporten_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelMolecular, Cellular and Developmental Biologyen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.identifier.pmid12773384en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/102135/1/emboj7595173-sup-0001.pdf
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/102135/2/emboj7595173.pdf
dc.identifier.doi10.1093/emboj/cdg262en_US
dc.identifier.sourceThe EMBO Journalen_US
dc.identifier.citedreferenceSaltiel AR and Pessin JE ( 2002 ) Insulin signaling pathways in time and space. Trends Cell Biol, 12, 65 – 71.en_US
dc.identifier.citedreferenceMartin TF ( 2001 ) PI(4,5)P(2) regulation of surface membrane traffic. Curr Opin Cell Biol, 13, 493 – 499.en_US
dc.identifier.citedreferenceMin J et al. ( 1999 ) Synip: a novel insulin‐regulated syntaxin 4‐binding protein mediating GLUT4 translocation in adipocytes. Mol Cell, 3, 751 – 760.en_US
dc.identifier.citedreferenceMiura K, Jacques KM, Stauffer S, Kubosaki A, Zhu K, Hirsch DS, Resau J, Zheng Y and Randazzo PA ( 2002 ) ARAP1: a point of convergence for Arf and Rho signaling. Mol Cell, 9, 109 – 119.en_US
dc.identifier.citedreferenceOlson AL, Knight JB and Pessin JE ( 1997 ) Syntaxin 4, VAMP2 and/or VAMP3/cellubrevin are functional target membrane and vesicle SNAP receptors for insulin‐stimulated GLUT4 translocation in adipocytes. Mol Cell Biol, 17, 2425 – 2435.en_US
dc.identifier.citedreferencePayrastre B, Missy K, Giuriato S, Bodin S, Plantavid M and Gratacap M ( 2001 ) Phosphoinositides: key players in cell signalling, in time and space. Cell Signal, 13, 377 – 387.en_US
dc.identifier.citedreferencePessin JE, Thurmond DC, Elmendorf JS, Coker KJ and Okada S ( 1999 ) Molecular basis of insulin‐stimulated GLUT4 vesicle trafficking. Location! Location! Location! J Biol Chem, 274, 2593 – 2596.en_US
dc.identifier.citedreferenceRibon V, Printen JA, Hoffman NG, Kay BK and Saltiel AR ( 1998 ) A novel, multifuntional c‐Cbl binding protein in insulin receptor signaling in 3T3‐L1 adipocytes. Mol Cell Biol, 18, 872 – 879.en_US
dc.identifier.citedreferenceSaltiel AR and Kahn CR ( 2001 ) Insulin signalling and the regulation of glucose and lipid metabolism. Nature, 414, 799 – 806.en_US
dc.identifier.citedreferenceSato TK, Darsow T and Emr SD ( 1998 ) Vam7p, a SNAP‐25‐like molecule and Vam3p, a syntaxin homolog, function together in yeast vacuolar protein trafficking. Mol Cell Biol, 18, 5308 – 5319.en_US
dc.identifier.citedreferenceSato TK, Overduin M and Emr SD ( 2001 ) Location, location, location: membrane targeting directed by PX domains. Science, 294, 1881 – 1885.en_US
dc.identifier.citedreferenceSechi AS and Wehland J ( 2000 ) The actin cytoskeleton and plasma membrane connection: PtdIns(4,5)P(2) influences cytoskeletal protein activity at the plasma membrane. J Cell Sci, 113, 3685 – 3695.en_US
dc.identifier.citedreferenceTapon N and Hall A ( 1997 ) Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton. Curr Opin Cell Biol, 9, 86 – 92.en_US
dc.identifier.citedreferenceThurmond DC, Kanzaki M, Khan AH and Pessin JE ( 2000 ) Munc18c function is required for insulin‐stimulated plasma membrane fusion of GLUT4 and insulin‐responsive amino peptidase storage vesicles. Mol Cell Biol, 20, 379 – 388.en_US
dc.identifier.citedreferenceTontonoz P, Hu E, Graves RA, Budavari AI and Spiegelman BM ( 1994 ) mPPARγ2: tissue‐specific regulator of an adipocyte enhancer. Genes Dev, 8, 1224 – 1234.en_US
dc.identifier.citedreferenceVarnai P, Lin X, Lee SB, Tuymetova G, Bondeva T, Spat A, Rhee SG, Hajnoczky G and Balla T ( 2002 ) Inositol lipid binding and membrane localization of isolated pleckstrin homology (PH) domains. Studies on the PH domains of phospholipase Cδ1 and p130. J Biol Chem, 277, 27412 – 27422.en_US
dc.identifier.citedreferenceVignal E, De Toledo M, Comunale F, Ladopoulou A, Gauthier‐Rouviere C, Blangy A and Fort P ( 2000 ) Characterization of TCL, a new GTPase of the rho family related to TC10 andCcdc42. J Biol Chem, 275, 36457 – 36464.en_US
dc.identifier.citedreferenceWaters SB, Holt KH, Ross SE, Syu LJ, Guan KL, Saltiel AR, Koretzky GA and Pessin JE ( 1995 ) Desensitization of Ras activation by a feedback disassociation of the SOS–Grb2 complex. J Biol Chem, 270, 20883 – 20886.en_US
dc.identifier.citedreferenceWatson RT, Shigematsu S, Chiang SH, Mora S, Kanzaki M, Macara IG, Saltiel AR and Pessin JE ( 2001 ) Lipid raft microdomain compartmentalization of TC10 is required for insulin signaling and GLUT4 translocation. J Cell Biol, 154, 829 – 840.en_US
dc.identifier.citedreferenceWientjes FB and Segal AW ( 2003 ) PX domain takes shape. Curr Opin Hematol, 10, 2 – 7.en_US
dc.identifier.citedreferenceWurmser AE and Emr SD ( 1998 ) Phosphoinositide signaling and turnover: PtdIns(3)P, a regulator of membrane traffic, is transported to the vacuole and degraded by a process that requires lumenal vacuolar hydrolase activities. EMBO J, 17, 4930 – 4942.en_US
dc.identifier.citedreferenceXu Y, Seet LF, Hanson B and Hong W ( 2001 ) The Phox homology (PX) domain, a new player in phosphoinositide signalling. Biochem J, 360, 513 – 530.en_US
dc.identifier.citedreferenceZhong Q, Lazar CS, Tronchere H, Sato T, Meerloo T, Yeo M, Songyang Z, Emr SD and Gill GN ( 2002 ) Endosomal localization and function of sorting nexin 1. Proc Natl Acad Sci USA, 99, 6767 – 6772.en_US
dc.identifier.citedreferenceAgo T, Takeya R, Hiroaki H, Kuribayashi F, Ito T, Kohda D and Sumimoto H ( 2001 ) The PX domain as a novel phosphoinositide‐binding module. Biochem Biophys Res Commun, 287, 733 – 738.en_US
dc.identifier.citedreferenceBaumann CA, Ribon V, Kanzaki M, Thurmond DC, Mora S, Shigematsu S, Bickel PE, Pessin JE and Saltiel AR ( 2000 ) CAP defines a second signalling pathway required for insulin‐stimulated glucose transport. Nature, 407, 202 – 207.en_US
dc.identifier.citedreferenceBenard V, Bohl BP and Bokoch GM ( 1999 ) Characterization of rac and cdc42 activation in chemoattractant‐stimulated human neutrophils using a novel assay for active GTPases. J Biol Chem, 274, 13198 – 13204.en_US
dc.identifier.citedreferenceBollag G and McCormick F ( 1991 ) Differential regulation of rasGAP and neurofibromatosis gene product activities. Nature, 351, 576 – 579.en_US
dc.identifier.citedreferenceBrill S, Li S, Lyman CW, Church DM, Wasmuth JJ, Weissbach L, Bernards A and Snijders AJ ( 1996 ) The Ras GTPase‐activating‐protein‐related human protein IQGAP2 harbors a potential actin binding domain and interacts with calmodulin and Rho family GTPases. Mol Cell Biol, 16, 4869 – 4878.en_US
dc.identifier.citedreferenceCheever ML, Sato TK, de Beer T, Kutateladze TG, Emr SD and Overduin M ( 2001 ) Phox domain interaction with PtdIns(3)P targets the Vam7 t‐SNARE to vacuole membranes. Nat Cell Biol, 3, 613 – 618.en_US
dc.identifier.citedreferenceChiang SH, Baumann CA, Kanzaki M, Thurmond DC, Watson RT, Neudauer CL, Macara IG, Pessin JE and Saltiel AR ( 2001 ) Insulin‐stimulated GLUT4 translocation requires the CAP‐dependent activation of TC10. Nature, 410, 944 – 948.en_US
dc.identifier.citedreferenceChiang SH, Hou JC, Hwang J, Pessin JE and Saltiel AR ( 2002 ) Cloning and functional characterization of related TC10 isoforms, a subfamily of Rho proteins involved in insulin‐stimulated glucose transport. J Biol Chem, 277, 13067 – 13073.en_US
dc.identifier.citedreferenceDumenil G, Sansonetti P and Tran Van Nhieu G ( 2000 ) Src tyrosine kinase activity down‐regulates Rho‐dependent responses during Shigella entry into epithelial cells and stress fibre formation. J Cell Sci, 113, 71 – 80.en_US
dc.identifier.citedreferenceEllson CD, Andrews S, Stephens LR and Hawkins PT ( 2002 ) The PX domain: a new phosphoinositide‐binding module. J Cell Sci, 115, 1099 – 1105.en_US
dc.identifier.citedreferenceEndo M, Shirouzu M and Yokoyama S ( 2003 ) The Cdc42 binding and scaffolding activities of the fission yeast adaptor protein Scd2. J Biol Chem, 278, 843 – 852.en_US
dc.identifier.citedreferenceFerrell JE,Jr ( 2000 ) What do scaffold proteins really do? Sci STKE, 2000, PE1.en_US
dc.identifier.citedreferenceGarcia P, Gupta R, Shah S, Morris AJ, Rudge SA, Scarlata S, Petrova V, McLaughlin S and Rebecchi MJ ( 1995 ) The pleckstrin homology domain of phospholipase C‐δ 1 binds with high affinity to phosphatidylinositol 4,5‐bisphosphate in bilayer membranes. Biochemistry, 34, 16228 – 16234.en_US
dc.identifier.citedreferenceGmeiner WH, Xu I, Horita DA, Smithgall TE, Engen JR, Smith DL and Byrd RA ( 2001 ) Intramolecular binding of a proximal PPII helix to an SH3 domain in the fusion protein SH3Hck:PPIIhGAP. Cell Biochem Biophys, 35, 115 – 126.en_US
dc.identifier.citedreferenceHall A ( 1992 ) Ras‐related GTPases and the cytoskeleton. Mol Biol Cell, 3, 475 – 479.en_US
dc.identifier.citedreferenceHiroaki H, Ago T, Ito T, Sumimoto H and Kohda D ( 2001 ) Solution structure of the PX domain, a target of the SH3 domain. Nat Struct Biol, 8, 526 – 530.en_US
dc.identifier.citedreferenceItoh T and Takenawa T ( 2002 ) Phosphoinositide‐binding domains: functional units for temporal and spatial regulation of intracellular signalling. Cell Signal, 14, 733 – 743.en_US
dc.identifier.citedreferenceJenna S, Hussain NK, Danek EI, Triki I, Wasiak S, McPherson PS and Lamarche‐Vane N ( 2002 ) The activity of the GTPase‐activating protein CdGAP is regulated by the endocytic protein intersectin. J Biol Chem, 277, 6366 – 6373.en_US
dc.identifier.citedreferenceKaibuchi K, Kuroda S and Amano M ( 1999 ) Regulation of the cytoskeleton and cell adhesion by the Rho family GTPases in mammalian cells. Annu Rev Biochem, 68, 459 – 486.en_US
dc.identifier.citedreferenceKarathanassis D, Stahelin RV, Bravo J, Perisic O, Pacold CM, Cho W and Williams RL ( 2002 ) Binding of the PX domain of p47(phox) to phosphatidylinositol 3,4‐bisphosphate and phosphatidic acid is masked by an intramolecular interaction. EMBO J, 21, 5057 – 5068.en_US
dc.identifier.citedreferenceKimura A, Baumann CA, Chiang SH and Saltiel AR ( 2001 ) The sorbin homology domain: a motif for the targeting of proteins to lipid rafts. Proc Natl Acad Sci USA, 98, 9098 – 9103.en_US
dc.identifier.citedreferenceKnudsen BS, Zheng J, Feller SM, Mayer JP, Burrell SK, Cowburn D and Hanafusa H ( 1995 ) Affinity and specificity requirements for the first Src homology 3 domain of the Crk proteins. EMBO J, 14, 2191 – 2198.en_US
dc.identifier.citedreferenceKozma R, Ahmed S, Best A and Lim L ( 1996 ) The GTPase‐activating protein n‐chimaerin cooperates with Rac1 and Cdc42Hs to induce the formation of lamellipodia and filopodia. Mol Cell Biol, 16, 5069 – 5080.en_US
dc.identifier.citedreferenceLemmon MA, Ferguson KM, O'Brien R, Sigler PB and Schlessinger J ( 1995 ) Specific and high‐affinity binding of inositol phosphates to an isolated pleckstrin homology domain. Proc Natl Acad Sci USA, 92, 10472 – 10476.en_US
dc.identifier.citedreferenceLiu J, Kimura A, Baumann CA and Saltiel AR ( 2002 ) APS facilitates c‐Cbl tyrosine phosphorylation and GLUT4 translocation in response to insulin in 3T3‐L1 adipocytes. Mol Cell Biol, 22, 3599 – 3609.en_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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