메뉴 건너뛰기




Volumn 9, Issue 12, 2008, Pages 2221-2235

ARAP1 regulates EGF receptor trafficking and signalling

Author keywords

ARAP1; EGF; EGF R; Endocytosis; MVB; RNAi; Signalling; Trafficking

Indexed keywords

ARF PROTEIN; EPIDERMAL GROWTH FACTOR RECEPTOR; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; PHOSPHATIDYLINOSITIDE; PROTEIN ARAP1; RHO FACTOR; UNCLASSIFIED DRUG;

EID: 56249148556     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/j.1600-0854.2008.00823.x     Document Type: Article
Times cited : (35)

References (56)
  • 5
    • 33845718110 scopus 로고    scopus 로고
    • Arap2 effects on the actin cytoskeleton are dependent on Arf6-specific Gtpase-activating-protein activity and binding to Rhoa-Gtp
    • Yoon HY, Miura K, Cuthbert EJ, Davis KK, Ahvazi B, Casanova JE, Randazzo PA. Arap2 effects on the actin cytoskeleton are dependent on Arf6-specific Gtpase-activating-protein activity and binding to Rhoa-Gtp. J Cell Sci 2006;119:4650-4666.
    • (2006) J Cell Sci , vol.119 , pp. 4650-4666
    • Yoon, H.Y.1    Miura, K.2    Cuthbert, E.J.3    Davis, K.K.4    Ahvazi, B.5    Casanova, J.E.6    Randazzo, P.A.7
  • 6
    • 33644979926 scopus 로고    scopus 로고
    • Arap3 is essential for formation of lamellipodia after growth factor stimulation
    • Krugmann S, Andrews S, Stephens L, Hawkins PT. Arap3 is essential for formation of lamellipodia after growth factor stimulation. J Cell Sci 2006;119:425-432.
    • (2006) J Cell Sci , vol.119 , pp. 425-432
    • Krugmann, S.1    Andrews, S.2    Stephens, L.3    Hawkins, P.T.4
  • 8
    • 12344338685 scopus 로고    scopus 로고
    • Arap3 is transiently tyrosine phosphorylated in cells attaching to fibronectin and inhibits cell spreading in a Rhogap-dependent manner
    • I ST, Nie Z, Stewart A, Najdovska M, Hall NE, He H, Randazzo PA, Lock P. Arap3 is transiently tyrosine phosphorylated in cells attaching to fibronectin and inhibits cell spreading in a Rhogap-dependent manner. J Cell Sci 2004;117:6071-6084.
    • (2004) J Cell Sci , vol.117 , pp. 6071-6084
    • I Stacey, T.T.1    Nie, Z.2    Stewart, A.3    Najdovska, M.4    Hall, N.E.5    He, H.6    Randazzo, P.A.7    Lock, P.8
  • 9
    • 40049092624 scopus 로고    scopus 로고
    • Arf and Rho GAP adapter protein ARAP1 participates in the mobilization of TRAIL-R1/DR4 to the plasma membrane
    • Simova S, Klima M, Cermak L, Sourkova V, Andera L. Arf and Rho GAP adapter protein ARAP1 participates in the mobilization of TRAIL-R1/DR4 to the plasma membrane. Apoptosis 2008;13:423-436.
    • (2008) Apoptosis , vol.13 , pp. 423-436
    • Simova, S.1    Klima, M.2    Cermak, L.3    Sourkova, V.4    Andera, L.5
  • 10
    • 0344196904 scopus 로고    scopus 로고
    • SAM domains: Uniform structure, diversity of function
    • Kim CA, Bowie JU. SAM domains: Uniform structure, diversity of function. Trends Biochem Sci 2003;28:625-628.
    • (2003) Trends Biochem Sci , vol.28 , pp. 625-628
    • Kim, C.A.1    Bowie, J.U.2
  • 11
  • 13
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 2006;127:635-648.
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 14
    • 28444439900 scopus 로고    scopus 로고
    • Organelle identity and the signposts for membrane traffic
    • Behnia R, Munro S. Organelle identity and the signposts for membrane traffic. Nature 2005;438:597-604.
    • (2005) Nature , vol.438 , pp. 597-604
    • Behnia, R.1    Munro, S.2
  • 17
    • 33645078650 scopus 로고    scopus 로고
    • Regulation of membrane traffic by phosphoinositide 3-kinases
    • Lindmo K, Stenmark H. Regulation of membrane traffic by phosphoinositide 3-kinases. J Cell Sci 2006;119:605-614.
    • (2006) J Cell Sci , vol.119 , pp. 605-614
    • Lindmo, K.1    Stenmark, H.2
  • 18
    • 20544464167 scopus 로고    scopus 로고
    • The role of the phosphoinositides at the Golgi complex
    • De Matteis MA, Di Campli A, Godi A. The role of the phosphoinositides at the Golgi complex. Biochim Biophys Acta 2005;1744:396-405.
    • (2005) Biochim Biophys Acta , vol.1744 , pp. 396-405
    • De Matteis, M.A.1    Di Campli, A.2    Godi, A.3
  • 19
    • 33749836234 scopus 로고    scopus 로고
    • Phosphoinositides in cell regulation and membrane dynamics
    • Di Paolo G, De Camilli P. Phosphoinositides in cell regulation and membrane dynamics. Nature 2006;443:651-657.
    • (2006) Nature , vol.443 , pp. 651-657
    • Di Paolo, G.1    De Camilli, P.2
  • 21
    • 0025359062 scopus 로고
    • Kinase activity controls the sorting of the epidermal growth factor receptor within the multivesicular body
    • Felder S, Miller K, Moehren G, Ullrich A, Schlessinger J, Hopkins CR. Kinase activity controls the sorting of the epidermal growth factor receptor within the multivesicular body. Cell 1990;61:623-634.
    • (1990) Cell , vol.61 , pp. 623-634
    • Felder, S.1    Miller, K.2    Moehren, G.3    Ullrich, A.4    Schlessinger, J.5    Hopkins, C.R.6
  • 22
    • 0021204118 scopus 로고
    • Autophosphorylation sites on the epidermal growth factor receptor
    • Downward J, Parker P, Waterfield MD. Autophosphorylation sites on the epidermal growth factor receptor. Nature 1984;311:483-485.
    • (1984) Nature , vol.311 , pp. 483-485
    • Downward, J.1    Parker, P.2    Waterfield, M.D.3
  • 23
    • 0025777103 scopus 로고
    • Internalization and down-regulation of the human epidermal growth factor receptor are regulated by the carboxyl-terminal tyrosines
    • Helin K, Beguinot L. Internalization and down-regulation of the human epidermal growth factor receptor are regulated by the carboxyl-terminal tyrosines. J Biol Chem 1991;266:8363-8368.
    • (1991) J Biol Chem , vol.266 , pp. 8363-8368
    • Helin, K.1    Beguinot, L.2
  • 24
    • 0028838012 scopus 로고
    • Dimerization of cell surface receptors in signal transduction
    • Heldin CH. Dimerization of cell surface receptors in signal transduction. Cell 1995;80:213-223.
    • (1995) Cell , vol.80 , pp. 213-223
    • Heldin, C.H.1
  • 25
    • 0033583220 scopus 로고    scopus 로고
    • C-Src-mediated phosphorylation of the epidermal growth factor receptor on Tyr845 and Tyr1101 is associated with modulation of receptor function
    • Biscardi JS, Maa MC, Tice DA, Cox ME, Leu TH, Parsons SJ. C-Src-mediated phosphorylation of the epidermal growth factor receptor on Tyr845 and Tyr1101 is associated with modulation of receptor function. J Biol Chem 1999;274:8335-8343.
    • (1999) J Biol Chem , vol.274 , pp. 8335-8343
    • Biscardi, J.S.1    Maa, M.C.2    Tice, D.A.3    Cox, M.E.4    Leu, T.H.5    Parsons, S.J.6
  • 27
    • 0033536637 scopus 로고    scopus 로고
    • The tyrosine kinase negative regulator C-Cbl as a ring-type, E2-dependent ubiquitin-protein ligase
    • Joazeiro CA, Wing SS, Huang H, Leverson JD, Hunter T, Liu YC. The tyrosine kinase negative regulator C-Cbl as a ring-type, E2-dependent ubiquitin-protein ligase. Science 1999;286:309-312.
    • (1999) Science , vol.286 , pp. 309-312
    • Joazeiro, C.A.1    Wing, S.S.2    Huang, H.3    Leverson, J.D.4    Hunter, T.5    Liu, Y.C.6
  • 28
    • 0033564877 scopus 로고    scopus 로고
    • The C-terminus of the kinase-defective neuregulin receptor Erbb-3 confers mitogenic superiority and dictates endocytic routing
    • Waterman H, Alroy I, Strano S, Seger R, Yarden Y. The C-terminus of the kinase-defective neuregulin receptor Erbb-3 confers mitogenic superiority and dictates endocytic routing. EMBO J 1999;18:3348-3358.
    • (1999) EMBO J , vol.18 , pp. 3348-3358
    • Waterman, H.1    Alroy, I.2    Strano, S.3    Seger, R.4    Yarden, Y.5
  • 29
    • 0034614652 scopus 로고    scopus 로고
    • The evolutionarily conserved N-terminal region of Cbl is sufficient to enhance down-regulation of the epidermal growth factor receptor
    • Lill NL, Douillard P, Awwad RA, Ota S, Lupher ML Jr, Miyake S, Meissner-Lula N, Hsu VW, Band H. The evolutionarily conserved N-terminal region of Cbl is sufficient to enhance down-regulation of the epidermal growth factor receptor. J Biol Chem 2000;275:367-377.
    • (2000) J Biol Chem , vol.275 , pp. 367-377
    • Lill, N.L.1    Douillard, P.2    Awwad, R.A.3    Ota, S.4    Lupher Jr., M.L.5    Miyake, S.6    Meissner-Lula, N.7    Hsu, V.W.8    Band, H.9
  • 30
    • 0034949705 scopus 로고    scopus 로고
    • C-Cbl ubiquitinates the Egf receptor at the plasma membrane and remains receptor associated throughout the endocytic route
    • de Melker AA, van der Horst G, Calafat J, Jansen H, Borst J. C-Cbl ubiquitinates the Egf receptor at the plasma membrane and remains receptor associated throughout the endocytic route. J Cell Sci 2001;114:2167-2178.
    • (2001) J Cell Sci , vol.114 , pp. 2167-2178
    • de Melker, A.A.1    van der Horst, G.2    Calafat, J.3    Jansen, H.4    Borst, J.5
  • 31
    • 0037075547 scopus 로고    scopus 로고
    • Cbl-Cin85-endophilin complex mediates ligand-induced downregulation of Egf receptors
    • Soubeyran P, Kowanetz K, Szymkiewicz I, Langdon WY, Dikic I. Cbl-Cin85-endophilin complex mediates ligand-induced downregulation of Egf receptors. Nature 2002;416:183-187.
    • (2002) Nature , vol.416 , pp. 183-187
    • Soubeyran, P.1    Kowanetz, K.2    Szymkiewicz, I.3    Langdon, W.Y.4    Dikic, I.5
  • 32
    • 4344602943 scopus 로고    scopus 로고
    • C-Cbl-mediated ubiquitinylation is required for epidermal growth factor receptor exit from the early endosomes
    • Ravid T, Heidinger JM, Gee P, Khan EM, Goldkorn T. C-Cbl-mediated ubiquitinylation is required for epidermal growth factor receptor exit from the early endosomes. J Biol Chem 2004;279:37153-37162.
    • (2004) J Biol Chem , vol.279 , pp. 37153-37162
    • Ravid, T.1    Heidinger, J.M.2    Gee, P.3    Khan, E.M.4    Goldkorn, T.5
  • 34
    • 0035408008 scopus 로고    scopus 로고
    • Ras-activated endocytosis is mediated by the Rab5 guanine nucleotide exchange activity of Rin1
    • Tall GG, Barbieri MA, Stahl PD, Horazdovsky BF. Ras-activated endocytosis is mediated by the Rab5 guanine nucleotide exchange activity of Rin1. Dev Cell 2001;1:73-82.
    • (2001) Dev Cell , vol.1 , pp. 73-82
    • Tall, G.G.1    Barbieri, M.A.2    Stahl, P.D.3    Horazdovsky, B.F.4
  • 36
    • 0345829921 scopus 로고    scopus 로고
    • Endocytosis of epidermal growth factor receptor regulated by Grb2-mediated recruitment of the Rab5 Gtpase-activating protein Rn-tre
    • Martinu L, Santiago-Walker A, Qi H, Chou MM. Endocytosis of epidermal growth factor receptor regulated by Grb2-mediated recruitment of the Rab5 Gtpase-activating protein Rn-tre. J Biol Chem 2002;277:50996-51002.
    • (2002) J Biol Chem , vol.277 , pp. 50996-51002
    • Martinu, L.1    Santiago-Walker, A.2    Qi, H.3    Chou, M.M.4
  • 37
    • 2442650416 scopus 로고    scopus 로고
    • Rab5 is a signalling Gtpase involved in actin remodelling by receptor tyrosine kinases
    • Lanzetti L, Palamidessi A, Areces L, Scita G, Di Fiore PP. Rab5 is a signalling Gtpase involved in actin remodelling by receptor tyrosine kinases. Nature 2004;429:309-314.
    • (2004) Nature , vol.429 , pp. 309-314
    • Lanzetti, L.1    Palamidessi, A.2    Areces, L.3    Scita, G.4    Di Fiore, P.P.5
  • 39
    • 33644869303 scopus 로고    scopus 로고
    • Rab7 activity affects epidermal growth factor: Epidermal growth factor receptor degradation by regulating endocytic trafficking from the late endosome
    • Ceresa BP, Bahr SJ. Rab7 activity affects epidermal growth factor: epidermal growth factor receptor degradation by regulating endocytic trafficking from the late endosome. J Biol Chem 2006;281:1099-1106.
    • (2006) J Biol Chem , vol.281 , pp. 1099-1106
    • Ceresa, B.P.1    Bahr, S.J.2
  • 40
    • 34247874425 scopus 로고    scopus 로고
    • Involvement of Rabring7 in Egf receptor degradation as an E3 ligase
    • Sakane A, Hatakeyama S, Sasaki T. Involvement of Rabring7 in Egf receptor degradation as an E3 ligase. Biochem Biophys Res Commun 2007;357:1058-1064.
    • (2007) Biochem Biophys Res Commun , vol.357 , pp. 1058-1064
    • Sakane, A.1    Hatakeyama, S.2    Sasaki, T.3
  • 43
    • 1542714469 scopus 로고    scopus 로고
    • Interactions of Gga3 with the ubiquitin sorting machinery
    • Puertollano R, Bonifacino JS. Interactions of Gga3 with the ubiquitin sorting machinery. Nat Cell Biol 2004;6:244-251.
    • (2004) Nat Cell Biol , vol.6 , pp. 244-251
    • Puertollano, R.1    Bonifacino, J.S.2
  • 44
    • 24344478722 scopus 로고    scopus 로고
    • Epidermal growth factor-dependent phosphorylation of the Gga3 adaptor protein regulates its recruitment to membranes
    • Kametaka S, Mattera R, Bonifacino JS. Epidermal growth factor-dependent phosphorylation of the Gga3 adaptor protein regulates its recruitment to membranes. Mol Cell Biol 2005;25:7988-8000.
    • (2005) Mol Cell Biol , vol.25 , pp. 7988-8000
    • Kametaka, S.1    Mattera, R.2    Bonifacino, J.S.3
  • 45
    • 33846628565 scopus 로고    scopus 로고
    • Rhob and the mammalian Diaphanous-related formin mDia2 in endosome trafficking
    • Wallar BJ, Deward AD, Resau JH, Alberts AS. Rhob and the mammalian Diaphanous-related formin mDia2 in endosome trafficking. Exp Cell Res 2007;313:560-571.
    • (2007) Exp Cell Res , vol.313 , pp. 560-571
    • Wallar, B.J.1    Deward, A.D.2    Resau, J.H.3    Alberts, A.S.4
  • 46
    • 0035945343 scopus 로고    scopus 로고
    • Human Vps34 is required for internal vesicle formation within multivesicular endosomes
    • Futter CE, Collinson LM, Backer JM, Hopkins CR. Human Vps34 is required for internal vesicle formation within multivesicular endosomes. J Cell Biol 2001;155:1251-1264.
    • (2001) J Cell Biol , vol.155 , pp. 1251-1264
    • Futter, C.E.1    Collinson, L.M.2    Backer, J.M.3    Hopkins, C.R.4
  • 47
    • 0037169336 scopus 로고    scopus 로고
    • Hrs regulates endosome membrane invagination and tyrosine kinase receptor signaling in Drosophila
    • Lloyd TE, Atkinson R, Wu MN, Zhou Y, Pennetta G, Bellen HJ. Hrs regulates endosome membrane invagination and tyrosine kinase receptor signaling in Drosophila. Cell 2002;108:261-269.
    • (2002) Cell , vol.108 , pp. 261-269
    • Lloyd, T.E.1    Atkinson, R.2    Wu, M.N.3    Zhou, Y.4    Pennetta, G.5    Bellen, H.J.6
  • 49
    • 37749018903 scopus 로고    scopus 로고
    • Biogenesis and function of multivesicular bodies
    • Piper RC, Katzmann DJ. Biogenesis and function of multivesicular bodies. Annu Rev Cell Dev Biol 2007;23:519-547.
    • (2007) Annu Rev Cell Dev Biol , vol.23 , pp. 519-547
    • Piper, R.C.1    Katzmann, D.J.2
  • 50
    • 33749505651 scopus 로고    scopus 로고
    • Cooperation of phosphoinositides and BAR domain proteins in endosomal tubulation
    • Shinozaki-Narikawa N, Kodama T, Shibasaki Y. Cooperation of phosphoinositides and BAR domain proteins in endosomal tubulation. Traffic 2006;7:1539-1550.
    • (2006) Traffic , vol.7 , pp. 1539-1550
    • Shinozaki-Narikawa, N.1    Kodama, T.2    Shibasaki, Y.3
  • 51
    • 33748136028 scopus 로고    scopus 로고
    • Cool-1 functions as an essential regulatory node for Egf receptor- and Src-mediated cell growth
    • Feng Q, Baird D, Peng X, Wang J, Ly T, Guan JL, Cerione RA. Cool-1 functions as an essential regulatory node for Egf receptor- and Src-mediated cell growth. Nat Cell Biol 2006;8:945-956.
    • (2006) Nat Cell Biol , vol.8 , pp. 945-956
    • Feng, Q.1    Baird, D.2    Peng, X.3    Wang, J.4    Ly, T.5    Guan, J.L.6    Cerione, R.A.7
  • 54
    • 0036231098 scopus 로고    scopus 로고
    • Bilayered clathrin coats on endosomal vacuoles are involved in protein sorting toward lysosomes
    • Sachse M, Urbe S, Oorschot V, Strous GJ, Klumperman J. Bilayered clathrin coats on endosomal vacuoles are involved in protein sorting toward lysosomes. Mol Biol Cell 2002;13:1313-1328.
    • (2002) Mol Biol Cell , vol.13 , pp. 1313-1328
    • Sachse, M.1    Urbe, S.2    Oorschot, V.3    Strous, G.J.4    Klumperman, J.5
  • 55
    • 0025233925 scopus 로고
    • Three-dimensional electron microscopy: Structure of the Golgi apparatus
    • Rambourg A, Clermont Y. Three-dimensional electron microscopy: Structure of the Golgi apparatus. Eur J Cell Biol 1990;51:189-200.
    • (1990) Eur J Cell Biol , vol.51 , pp. 189-200
    • Rambourg, A.1    Clermont, Y.2
  • 56
    • 0035945348 scopus 로고    scopus 로고
    • Peri-Golgi vesicles contain retrograde but not anterograde proteins consistent with the cisternal progression model of intra-Golgi transport
    • Martinez-Menarguez JA, Prekeris R, Oorschot VM, Scheller R, Slot JW, Geuze HJ, Klumperman J. Peri-Golgi vesicles contain retrograde but not anterograde proteins consistent with the cisternal progression model of intra-Golgi transport. J Cell Biol 2001;155:1213-1224.
    • (2001) J Cell Biol , vol.155 , pp. 1213-1224
    • Martinez-Menarguez, J.A.1    Prekeris, R.2    Oorschot, V.M.3    Scheller, R.4    Slot, J.W.5    Geuze, H.J.6    Klumperman, J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.