메뉴 건너뛰기




Volumn 24, Issue , 2006, Pages 771-800

Compartmentalized Ras/MAPK signaling

Author keywords

Cell signaling; GTPases; MAP kinase; Oncogenes

Indexed keywords

FLUORESCENT DYE; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; MITOGEN ACTIVATED PROTEIN KINASE; NOTCH RECEPTOR; PHOSPHOLIPASE C GAMMA; RAP1 PROTEIN; RAS PROTEIN; SMAD PROTEIN; TOLL LIKE RECEPTOR; TYROSINE KINASE RECEPTOR;

EID: 33644864788     PISSN: 07320582     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.immunol.24.021605.090723     Document Type: Review
Times cited : (338)

References (171)
  • 2
    • 0035834388 scopus 로고    scopus 로고
    • The guanine nucleotide-binding switch in three dimensions
    • Vetter IR, Wittinghofer A. 2001. The guanine nucleotide-binding switch in three dimensions. Science 294:1299-304
    • (2001) Science , vol.294 , pp. 1299-1304
    • Vetter, I.R.1    Wittinghofer, A.2
  • 4
    • 0003000807 scopus 로고    scopus 로고
    • Tools of the trade: Use of dominant-inhibitory mutants of Ras-family GTPases
    • Feig LA. 1999. Tools of the trade: use of dominant-inhibitory mutants of Ras-family GTPases. Nat. Cell Biol. 1:E25-27
    • (1999) Nat. Cell Biol. , vol.1
    • Feig, L.A.1
  • 5
    • 0000953693 scopus 로고
    • An unidentified virus which causes the rapid production of tumours in mice
    • Harvey JJ. 1964. An unidentified virus which causes the rapid production of tumours in mice. Nature 204:1104-5
    • (1964) Nature , vol.204 , pp. 1104-1105
    • Harvey, J.J.1
  • 7
    • 0019440568 scopus 로고
    • Analysis of two divergent rat genomic clones homologous to the transforming gene of Harvey murine sarcoma virus
    • DeFeo D, Gonda MA, Young HA, Chang EH, Lowy DR, et al. 1981. Analysis of two divergent rat genomic clones homologous to the transforming gene of Harvey murine sarcoma virus. Proc. Natl. Acad. Sci. USA 78:3328-32
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 3328-3332
    • DeFeo, D.1    Gonda, M.A.2    Young, H.A.3    Chang, E.H.4    Lowy, D.R.5
  • 8
    • 0019855643 scopus 로고
    • The p21 src genes of Harvey and Kirsten sarcoma viruses originate from divergent members of a family of normal vertebrate genes
    • Ellis RW, DeFeo D, Shih TY, Gonda MA, Young HA, et al. 1981. The p21 src genes of Harvey and Kirsten sarcoma viruses originate from divergent members of a family of normal vertebrate genes. Nature 292:506-11
    • (1981) Nature , vol.292 , pp. 506-511
    • Ellis, R.W.1    DeFeo, D.2    Shih, T.Y.3    Gonda, M.A.4    Young, H.A.5
  • 10
    • 0024376173 scopus 로고
    • Ras oncogenes in human cancer: A review
    • Bos JL. 1989. Ras oncogenes in human cancer: a review. Cancer Res. 49:4682-89
    • (1989) Cancer Res. , vol.49 , pp. 4682-4689
    • Bos, J.L.1
  • 11
    • 0034092777 scopus 로고    scopus 로고
    • Ras regulation and function in lymphocytes
    • Genot E, Cantrell DA. 2000. Ras regulation and function in lymphocytes. Curr. Opin. Immunol. 12:289-94
    • (2000) Curr. Opin. Immunol. , vol.12 , pp. 289-294
    • Genot, E.1    Cantrell, D.A.2
  • 13
    • 0036359608 scopus 로고    scopus 로고
    • Transgenic analysis of thymocyte signal transduction
    • Cantrell DA. 2002. Transgenic analysis of thymocyte signal transduction. Nat. Rev. Immunol. 2:20-27
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 20-27
    • Cantrell, D.A.1
  • 15
    • 0033136274 scopus 로고    scopus 로고
    • Immature thymocytes employ distinct signaling pathways for allelic exclusion versus differentiation and expansion
    • Gartner F, Alt FW, Monroe R, Chu M, Sleckman BP, et al. 1999. Immature thymocytes employ distinct signaling pathways for allelic exclusion versus differentiation and expansion. Immunity 10:537-46
    • (1999) Immunity , vol.10 , pp. 537-546
    • Gartner, F.1    Alt, F.W.2    Monroe, R.3    Chu, M.4    Sleckman, B.P.5
  • 16
    • 0034303371 scopus 로고    scopus 로고
    • RasGRP is essential for mouse thymocyte differentiation and TCR signaling
    • Dower NA, Stang SL, Bottorff DA, Ebinu JO, Dickie P, et al. 2000. RasGRP is essential for mouse thymocyte differentiation and TCR signaling. Nat. Immunol. 1:317-21
    • (2000) Nat. Immunol. , vol.1 , pp. 317-321
    • Dower, N.A.1    Stang, S.L.2    Bottorff, D.A.3    Ebinu, J.O.4    Dickie, P.5
  • 17
    • 0042432047 scopus 로고    scopus 로고
    • Autoimmunity as the consequence of a spontaneous mutation in Rasgrp1
    • Layer K, Lin G, Nencioni A, Hu W, Schmucker A, et al. 2003. Autoimmunity as the consequence of a spontaneous mutation in Rasgrp1. Immunity 19:243-55
    • (2003) Immunity , vol.19 , pp. 243-255
    • Layer, K.1    Lin, G.2    Nencioni, A.3    Hu, W.4    Schmucker, A.5
  • 18
    • 18944383647 scopus 로고    scopus 로고
    • A diacylglycerol-protein kinase C-RasGRP1 pathway directs Ras activation upon antigen receptor stimulation of T cells
    • Roose JP, Mollenauer M, Gupta VA, Stone J, Weiss A. 2005. A diacylglycerol-protein kinase C-RasGRP1 pathway directs Ras activation upon antigen receptor stimulation of T cells. Mol. Cell. Biol. 25:4426-41
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 4426-4441
    • Roose, J.P.1    Mollenauer, M.2    Gupta, V.A.3    Stone, J.4    Weiss, A.5
  • 19
    • 0018875887 scopus 로고
    • Localization of the src gene product of the Harvey strain of MSV to plasma membrane of transformed cells by electron microscopic immunocytochemistry
    • Willingham MC, Pastan I, Shih TY, Scolnick EM. 1980. Localization of the src gene product of the Harvey strain of MSV to plasma membrane of transformed cells by electron microscopic immunocytochemistry. Cell 19:1005-14
    • (1980) Cell , vol.19 , pp. 1005-1014
    • Willingham, M.C.1    Pastan, I.2    Shih, T.Y.3    Scolnick, E.M.4
  • 20
    • 0033538559 scopus 로고    scopus 로고
    • Endomembrane trafficking of ras: The CAAX motif targets proteins to the ER and Golgi
    • Choy E, Chiu VK, Silletti J, Feoktistov M, Morimoto T, et al. 1999. Endomembrane trafficking of ras: the CAAX motif targets proteins to the ER and Golgi. Cell 98:69-80
    • (1999) Cell , vol.98 , pp. 69-80
    • Choy, E.1    Chiu, V.K.2    Silletti, J.3    Feoktistov, M.4    Morimoto, T.5
  • 21
    • 0021528719 scopus 로고
    • Harvey murine sarcoma virus p21 ras protein: Biological and biochemical significance of the cysteine nearest the carboxy terminus
    • Willumsen BM, Norris K, Papageorge AG, Hubbert NL, Lowy DR. 1984. Harvey murine sarcoma virus p21 ras protein: biological and biochemical significance of the cysteine nearest the carboxy terminus. EMBO J. 3:2581-85
    • (1984) EMBO J. , vol.3 , pp. 2581-2585
    • Willumsen, B.M.1    Norris, K.2    Papageorge, A.G.3    Hubbert, N.L.4    Lowy, D.R.5
  • 22
    • 0026735063 scopus 로고
    • Protein isoprenylation and methylation at carboxyl terminal cysteine residues
    • Clarke S. 1992. Protein isoprenylation and methylation at carboxyl terminal cysteine residues. Annu. Rev. Biochem. 61:355-86
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 355-386
    • Clarke, S.1
  • 23
    • 0000081175 scopus 로고
    • Post-translational modification of the Ha-ras oncogene protein: Evidience for a third class of protein carboxyl methyltransferases
    • Clarke S, Vogel JP, Deschenes RJ, Stock JB. 1988. Post-translational modification of the Ha-ras oncogene protein: evidience for a third class of protein carboxyl methyltransferases. Proc. Natl. Acad. Sci. USA 85:4643-47
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 4643-4647
    • Clarke, S.1    Vogel, J.P.2    Deschenes, R.J.3    Stock, J.B.4
  • 24
    • 0029966304 scopus 로고    scopus 로고
    • Protein prenyltransferases
    • Casey PJ, Seabra MC. 1996. Protein prenyltransferases. J. Biol. Chem. 271:5289-92
    • (1996) J. Biol. Chem. , vol.271 , pp. 5289-5292
    • Casey, P.J.1    Seabra, M.C.2
  • 25
    • 0029898894 scopus 로고    scopus 로고
    • Protein prenylation: Molecular mechanisms and functional consequences
    • Zhang FL, Casey PJ. 1996. Protein prenylation: molecular mechanisms and functional consequences. Annu. Rev. Biochem. 65:241-69
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 241-269
    • Zhang, F.L.1    Casey, P.J.2
  • 26
    • 0033605596 scopus 로고    scopus 로고
    • Disruption of the mouse Rce1 gene results in defective Ras processing and mislocalization of Ras within cells
    • Kim E, Ambroziak P, Otto JC, Taylor B, Ashby M, et al. 1999. Disruption of the mouse Rce1 gene results in defective Ras processing and mislocalization of Ras within cells. J. Biol. Chem. 274:8383-90
    • (1999) J. Biol. Chem. , vol.274 , pp. 8383-8390
    • Kim, E.1    Ambroziak, P.2    Otto, J.C.3    Taylor, B.4    Ashby, M.5
  • 27
    • 0026346215 scopus 로고
    • Methylation and demethylation reactions of guanine nucleotide-binding proteins of rod outer segments
    • Pèrez-Sala D, Tan EW, Canada FJ, Rando RR. 1991. Methylation and demethylation reactions of guanine nucleotide-binding proteins of rod outer segments. Proc. Natl. Acad. Sci. USA 88:3043-46
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3043-3046
    • Pèrez-Sala, D.1    Tan, E.W.2    Canada, F.J.3    Rando, R.R.4
  • 28
    • 0037174987 scopus 로고    scopus 로고
    • Identification of a Ras palmitoyltransferase in Saccharomyces cerevisiae
    • Lobo S, Greentree WK, Linder ME, Deschenes RJ. 2002. Identification of a Ras palmitoyltransferase in Saccharomyces cerevisiae. J. Biol. Chem. 277:41268-73
    • (2002) J. Biol. Chem. , vol.277 , pp. 41268-41273
    • Lobo, S.1    Greentree, W.K.2    Linder, M.E.3    Deschenes, R.J.4
  • 29
    • 0032511057 scopus 로고    scopus 로고
    • Mammalian prenylcysteine carboxyl methyltransferase is in the endoplasmic reticulum
    • Dai Q, Choy E, Chiu V, Romano J, Slivka S, et al. 1998. Mammalian prenylcysteine carboxyl methyltransferase is in the endoplasmic reticulum. J. Biol. Chem. 273:15030-34
    • (1998) J. Biol. Chem. , vol.273 , pp. 15030-15034
    • Dai, Q.1    Choy, E.2    Chiu, V.3    Romano, J.4    Slivka, S.5
  • 30
    • 0030909336 scopus 로고    scopus 로고
    • Modulation of Ras and a-factor function by carboxyl-terminal proteolysis
    • Boyartchuk VL, Ashby MN, Rine J. 1997. Modulation of Ras and a-factor function by carboxyl-terminal proteolysis. Science 275:1796-800
    • (1997) Science , vol.275 , pp. 1796-1800
    • Boyartchuk, V.L.1    Ashby, M.N.2    Rine, J.3
  • 31
    • 0346668323 scopus 로고    scopus 로고
    • Erf4p and Erf2p form an endoplasmic reticulum-associated complex involved in the plasma membrane localization of yeast Ras proteins
    • Zhao L, Lobo S, Dong X, Ault AD, Deschenes RJ. 2002. Erf4p and Erf2p form an endoplasmic reticulum-associated complex involved in the plasma membrane localization of yeast Ras proteins. J. Biol. Chem. 277:49352-59
    • (2002) J. Biol. Chem. , vol.277 , pp. 49352-49359
    • Zhao, L.1    Lobo, S.2    Dong, X.3    Ault, A.D.4    Deschenes, R.J.5
  • 33
    • 0026037624 scopus 로고
    • A CAAX or a CAAL motif and a second signal are sufficient for plasma membrane targeting of ras proteins
    • Hancock JF, Cadwallader K, Paterson H, Marshall CJ. 1991. A CAAX or a CAAL motif and a second signal are sufficient for plasma membrane targeting of ras proteins. EMBO J. 10:4033-39
    • (1991) EMBO J. , vol.10 , pp. 4033-4039
    • Hancock, J.F.1    Cadwallader, K.2    Paterson, H.3    Marshall, C.J.4
  • 34
    • 0041689887 scopus 로고    scopus 로고
    • Palmitoylation and plasma membrane localization of Ras2p by a nonclassical trafficking pathway in Saccharomyces cerevisiae
    • Dong X, Mitchell DA, Lobo S, Zhao L, Bartels DJ, Deschenes RJ. 2003. Palmitoylation and plasma membrane localization of Ras2p by a nonclassical trafficking pathway in Saccharomyces cerevisiae. Mol. Cell. Biol. 23:6574-84
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 6574-6584
    • Dong, X.1    Mitchell, D.A.2    Lobo, S.3    Zhao, L.4    Bartels, D.J.5    Deschenes, R.J.6
  • 35
    • 22944460791 scopus 로고    scopus 로고
    • Depalmitoylated Ras traffics to and from the Golgi complex via a nonvesicular pathway
    • Goodwin JS, Drake KR, Rogers C, Wright L, Lippincott-Schwartz J, et al. 2005. Depalmitoylated Ras traffics to and from the Golgi complex via a nonvesicular pathway. J. Cell Biol. 170:261-72
    • (2005) J. Cell Biol. , vol.170 , pp. 261-272
    • Goodwin, J.S.1    Drake, K.R.2    Rogers, C.3    Wright, L.4    Lippincott-Schwartz, J.5
  • 36
    • 20144375061 scopus 로고    scopus 로고
    • An acylation cycle regulates localization and activity of palmitoylated Ras isoforms
    • Rocks O, Peyker A, Kahms M, Verveer PJ, Koerner C, et al. 2005. An acylation cycle regulates localization and activity of palmitoylated Ras isoforms. Science 307:1746-52
    • (2005) Science , vol.307 , pp. 1746-1752
    • Rocks, O.1    Peyker, A.2    Kahms, M.3    Verveer, P.J.4    Koerner, C.5
  • 38
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger J. 2000. Cell signaling by receptor tyrosine kinases. Cell 103:211-25
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 40
    • 7444245100 scopus 로고    scopus 로고
    • Renewing the conspiracy theory debate: Does Raf function alone to mediate Ras oncogenesis?
    • Repasky GA, Chenette EJ, Der CJ. 2004. Renewing the conspiracy theory debate: Does Raf function alone to mediate Ras oncogenesis? Trends Cell Biol. 14:639-47
    • (2004) Trends Cell Biol. , vol.14 , pp. 639-647
    • Repasky, G.A.1    Chenette, E.J.2    Der, C.J.3
  • 41
    • 0037102561 scopus 로고    scopus 로고
    • Distinct requirements for Ras oncogenesis in human versus mouse cells
    • Hamad NM, Elconin JH, Karnoub AE, Bai W, Rich JN, et al. 2002. Distinct requirements for Ras oncogenesis in human versus mouse cells. Genes Dev. 16:2045-57
    • (2002) Genes Dev. , vol.16 , pp. 2045-2057
    • Hamad, N.M.1    Elconin, J.H.2    Karnoub, A.E.3    Bai, W.4    Rich, J.N.5
  • 42
    • 0027965262 scopus 로고
    • Compartmentalization of SHC, GRB2 and mSOS, and hyperphosphorylation of Raf-1 by EGF but not insulin in liver parenchyma
    • Di Guglielmo GM, Baass PC, Ou WJ, Posner BI, Bergeron JJ. 1994. Compartmentalization of SHC, GRB2 and mSOS, and hyperphosphorylation of Raf-1 by EGF but not insulin in liver parenchyma. EMBO J. 13:4269-77
    • (1994) EMBO J. , vol.13 , pp. 4269-4277
    • Di Guglielmo, G.M.1    Baass, P.C.2    Ou, W.J.3    Posner, B.I.4    Bergeron, J.J.5
  • 44
    • 0033860695 scopus 로고    scopus 로고
    • The EGF receptor: A nexus for trafficking and signaling
    • Carpenter G. 2000. The EGF receptor: a nexus for trafficking and signaling. BioEssays 22:697-707
    • (2000) BioEssays , vol.22 , pp. 697-707
    • Carpenter, G.1
  • 45
    • 3142726114 scopus 로고    scopus 로고
    • The Cbl family and other ubiquitin ligases: Destructive forces in control of antigen receptor signaling
    • Duan L, Reddi AL, Ghosh A, Dimri M, Band H. 2004. The Cbl family and other ubiquitin ligases: destructive forces in control of antigen receptor signaling. Immunity 21:7-17
    • (2004) Immunity , vol.21 , pp. 7-17
    • Duan, L.1    Reddi, A.L.2    Ghosh, A.3    Dimri, M.4    Band, H.5
  • 46
    • 3342970389 scopus 로고    scopus 로고
    • Cbl-dependent ubiquitination is required for progression of EGF receptors into clathrin-coated pits
    • Stang E, Blystad FD, Kazazic M, Bertelsen V, Brodahl T, et al. 2004. Cbl-dependent ubiquitination is required for progression of EGF receptors into clathrin-coated pits. Mol. Biol. Cell 15:3591-604
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3591-3604
    • Stang, E.1    Blystad, F.D.2    Kazazic, M.3    Bertelsen, V.4    Brodahl, T.5
  • 47
    • 0032217156 scopus 로고    scopus 로고
    • c-Cbl/Sli-1 regulates endocytic sorting and ubiquitination of the epidermal growth factor receptor
    • Levkowitz G, Waterman H, Zamir E, Kam Z, Oved S, et al. 1998. c-Cbl/Sli-1 regulates endocytic sorting and ubiquitination of the epidermal growth factor receptor. Genes Dev. 12:3663-74
    • (1998) Genes Dev. , vol.12 , pp. 3663-3674
    • Levkowitz, G.1    Waterman, H.2    Zamir, E.3    Kam, Z.4    Oved, S.5
  • 48
    • 0029664998 scopus 로고    scopus 로고
    • Interactions of Cbl with two adapter proteins, Grb2 and Crk, upon T cell activation
    • Buday L, Khwaja A, Sipeki S, Farago A, Downward J. 1996. Interactions of Cbl with two adapter proteins, Grb2 and Crk, upon T cell activation. J. Biol. Chem. 271:6159-63
    • (1996) J. Biol. Chem. , vol.271 , pp. 6159-6163
    • Buday, L.1    Khwaja, A.2    Sipeki, S.3    Farago, A.4    Downward, J.5
  • 49
    • 0035313703 scopus 로고    scopus 로고
    • Expanding roles for β-arrestins as scaffolds and adapters in GPCR signaling and trafficking
    • Miller WE, Lefkowitz RJ. 2001. Expanding roles for β-arrestins as scaffolds and adapters in GPCR signaling and trafficking. Curr. Opin. Cell Biol. 13:139-45
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 139-145
    • Miller, W.E.1    Lefkowitz, R.J.2
  • 50
    • 0030812438 scopus 로고    scopus 로고
    • Molecular mechanism of desensitization of the chemokine receptor CCR-5: Receptor signaling and internalization are dissociable from its role as an HIV-1 co-receptor
    • Aramori I, Ferguson SS, Bieniasz PD, Zhang J, Cullen B, Cullen MG. 1997. Molecular mechanism of desensitization of the chemokine receptor CCR-5: receptor signaling and internalization are dissociable from its role as an HIV-1 co-receptor. EMBO J. 16:4606-16
    • (1997) EMBO J. , vol.16 , pp. 4606-4616
    • Aramori, I.1    Ferguson, S.S.2    Bieniasz, P.D.3    Zhang, J.4    Cullen, B.5    Cullen, M.G.6
  • 51
    • 0242333900 scopus 로고    scopus 로고
    • Regulation of membrane trafficking and subcellular organization of endocytic compartments revealed with FM1-43 in resting and activated human T cells
    • Fomina AF, Deerinck TJ, Ellisman MH, Cahalan MD. 2003. Regulation of membrane trafficking and subcellular organization of endocytic compartments revealed with FM1-43 in resting and activated human T cells. Exp. Cell Res. 291:150-66
    • (2003) Exp. Cell Res. , vol.291 , pp. 150-166
    • Fomina, A.F.1    Deerinck, T.J.2    Ellisman, M.H.3    Cahalan, M.D.4
  • 52
    • 0032438114 scopus 로고    scopus 로고
    • Altered thymic positive selection and intracellular signals in Cbl-deficient mice
    • Naramura M, Kole HK, Hu RJ, Gu H. 1998. Altered thymic positive selection and intracellular signals in Cbl-deficient mice. Proc. Natl. Acad. Sci. USA 95:15547-52
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15547-15552
    • Naramura, M.1    Kole, H.K.2    Hu, R.J.3    Gu, H.4
  • 53
    • 15744368010 scopus 로고    scopus 로고
    • T-cell activation is accompanied by an ubiquitination process occurring at the immunological synapse
    • Wiedemann A, Muller S, Favier B, Penna D, Guiraud M, et al. 2005. T-cell activation is accompanied by an ubiquitination process occurring at the immunological synapse. Immunol. Lett. 98:57-61
    • (2005) Immunol. Lett. , vol.98 , pp. 57-61
    • Wiedemann, A.1    Muller, S.2    Favier, B.3    Penna, D.4    Guiraud, M.5
  • 54
    • 0030461226 scopus 로고    scopus 로고
    • Control of EGF receptor signaling by clathrin-mediated endocytosis
    • Vieira AV, Lamaze C, Schmid SL. 1996. Control of EGF receptor signaling by clathrin-mediated endocytosis. Science 274:2086-89
    • (1996) Science , vol.274 , pp. 2086-2089
    • Vieira, A.V.1    Lamaze, C.2    Schmid, S.L.3
  • 55
    • 0033544953 scopus 로고    scopus 로고
    • Dynamin is required for the activation of mitogen-activated protein (MAP) kinase by MAP kinase kinase
    • Kranenburg O, Verlaan I, Moolenaar WH. 1999. Dynamin is required for the activation of mitogen-activated protein (MAP) kinase by MAP kinase kinase. J. Biol. Chem. 274:35301-4
    • (1999) J. Biol. Chem. , vol.274 , pp. 35301-35304
    • Kranenburg, O.1    Verlaan, I.2    Moolenaar, W.H.3
  • 56
    • 0031975838 scopus 로고    scopus 로고
    • Essential role for G protein-coupled receptor endocytosis in the activation of mitogen-activated protein kinase
    • Daaka Y, Luttrell LM, Ahn S, Della Rocca GJ, Ferguson SS. 1998. Essential role for G protein-coupled receptor endocytosis in the activation of mitogen-activated protein kinase. J. Biol. Chem. 273:685-88
    • (1998) J. Biol. Chem. , vol.273 , pp. 685-688
    • Daaka, Y.1    Luttrell, L.M.2    Ahn, S.3    Della Rocca, G.J.4    Ferguson, S.S.5
  • 57
    • 12544250585 scopus 로고    scopus 로고
    • Multivesicular bodies and multivesicular endosomes: The "ins and outs" of endosomal traffic
    • Stahl PD, Barbieri MA. 2002. Multivesicular bodies and multivesicular endosomes: the "ins and outs" of endosomal traffic. Science STKE 2002:PE32
    • (2002) Science STKE , vol.2002
    • Stahl, P.D.1    Barbieri, M.A.2
  • 58
    • 0035162703 scopus 로고    scopus 로고
    • Regulation of epidermal growth factor receptor signaling by endocytosis and intracellular trafficking
    • Burke P, Schooler K, Wiley HS. 2001. Regulation of epidermal growth factor receptor signaling by endocytosis and intracellular trafficking. Mol. Biol. Cell 12:1897-910
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1897-1910
    • Burke, P.1    Schooler, K.2    Wiley, H.S.3
  • 59
    • 0034597554 scopus 로고    scopus 로고
    • Interaction of EGF receptor and grb2 in living cells visualized by fluorescence resonance energy transfer (FRET) microscopy
    • Sorkin A, McClure M, Huang F, Carter R. 2000. Interaction of EGF receptor and grb2 in living cells visualized by fluorescence resonance energy transfer (FRET) microscopy. Curr. Biol. 10:1395-98
    • (2000) Curr. Biol. , vol.10 , pp. 1395-1398
    • Sorkin, A.1    McClure, M.2    Huang, F.3    Carter, R.4
  • 60
    • 0032567503 scopus 로고    scopus 로고
    • Endocytosis of functional epidermal growth factor receptor-green fluorescent protein chimera
    • Carter RE, Sorkin A. 1998. Endocytosis of functional epidermal growth factor receptor-green fluorescent protein chimera. J. Biol. Chem. 273:35000-7
    • (1998) J. Biol. Chem. , vol.273 , pp. 35000-35007
    • Carter, R.E.1    Sorkin, A.2
  • 61
    • 0033533709 scopus 로고    scopus 로고
    • Fluorescence lifetime imaging of receptor tyrosine kinase activity in cells
    • Wouters FS, Bastiaens PI. 1999. Fluorescence lifetime imaging of receptor tyrosine kinase activity in cells. Curr. Biol. 9:1127-30
    • (1999) Curr. Biol. , vol.9 , pp. 1127-1130
    • Wouters, F.S.1    Bastiaens, P.I.2
  • 62
    • 0035999983 scopus 로고    scopus 로고
    • Coordinated traffic of Grb2 and Ras during epidermal growth factor receptor endocytosis visualized in living cells
    • Jiang X, Sorkin A. 2002. Coordinated traffic of Grb2 and Ras during epidermal growth factor receptor endocytosis visualized in living cells. Mol. Biol. Cell 13:1522-35
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1522-1535
    • Jiang, X.1    Sorkin, A.2
  • 64
    • 0036341207 scopus 로고    scopus 로고
    • Signal transduction and endocytosis: Close encounters of many kinds
    • Sorkin A, Von Zastrow M. 2002. Signal transduction and endocytosis: close encounters of many kinds. Nat. Rev. Mol. Cell Biol. 3:600-14
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 600-614
    • Sorkin, A.1    Von Zastrow, M.2
  • 65
    • 0035031938 scopus 로고    scopus 로고
    • Re-localization of activated EGF receptor and its signal transducers to multivesicular compartments downstream of early endosomes in response to EGF
    • Oksvold MP, Skarpen E, Wierod L, Paulsen RE, Huitfeldt HS. 2001. Re-localization of activated EGF receptor and its signal transducers to multivesicular compartments downstream of early endosomes in response to EGF. Eur. J. Cell Biol. 80:285-94
    • (2001) Eur. J. Cell Biol. , vol.80 , pp. 285-294
    • Oksvold, M.P.1    Skarpen, E.2    Wierod, L.3    Paulsen, R.E.4    Huitfeldt, H.S.5
  • 66
    • 0035399162 scopus 로고    scopus 로고
    • EGF-dependent translocation of green fluorescent protein-tagged PLC-gamma1 to the plasma membrane and endosomes
    • Wang XJ, Liao HJ, Chattopadhyay A, Carpenter G. 2001. EGF-dependent translocation of green fluorescent protein-tagged PLC-gamma1 to the plasma membrane and endosomes. Exp. Cell Res. 267:28-36
    • (2001) Exp. Cell Res. , vol.267 , pp. 28-36
    • Wang, X.J.1    Liao, H.J.2    Chattopadhyay, A.3    Carpenter, G.4
  • 67
    • 0035972164 scopus 로고    scopus 로고
    • Real time fluorescence imaging of PLC gamma translocation and its interaction with the epidermal growth factor receptor
    • Matsuda M, Paterson HF, Rodriguez R, Fensome AC, Ellis MV, et al. 2001. Real time fluorescence imaging of PLC gamma translocation and its interaction with the epidermal growth factor receptor. J. Cell Biol. 153:599-612
    • (2001) J. Cell Biol. , vol.153 , pp. 599-612
    • Matsuda, M.1    Paterson, H.F.2    Rodriguez, R.3    Fensome, A.C.4    Ellis, M.V.5
  • 68
    • 0032436774 scopus 로고    scopus 로고
    • Isolated endosomes from quiescent rat liver contain the signal transduction machinery. Differential distribution of activated Raf-1 and Mek in the endocytic compartment
    • Pol A, Calvo M, Enrich C. 1998. Isolated endosomes from quiescent rat liver contain the signal transduction machinery. Differential distribution of activated Raf-1 and Mek in the endocytic compartment. FEBS Lett. 441:34-38
    • (1998) FEBS Lett. , vol.441 , pp. 34-38
    • Pol, A.1    Calvo, M.2    Enrich, C.3
  • 69
    • 0036293754 scopus 로고    scopus 로고
    • H-Ras signaling and K-Ras signaling are differentially dependent on endocytosis
    • Roy S, Wyse B, Hancock JF. 2002. H-Ras signaling and K-Ras signaling are differentially dependent on endocytosis. Mol. Cell. Biol. 22:5128-40
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5128-5140
    • Roy, S.1    Wyse, B.2    Hancock, J.F.3
  • 70
    • 0032553443 scopus 로고    scopus 로고
    • Intersectin, a novel adaptor protein with two Eps15 homology and five Src homology 3 domains
    • Yamabhai M, Hoffman NG, Hardison NL, McPherson PS, Castagnoli L, et al. 1998. Intersectin, a novel adaptor protein with two Eps15 homology and five Src homology 3 domains. J. Biol. Chem. 273:31401-7
    • (1998) J. Biol. Chem. , vol.273 , pp. 31401-31407
    • Yamabhai, M.1    Hoffman, N.G.2    Hardison, N.L.3    McPherson, P.S.4    Castagnoli, L.5
  • 71
    • 0033147449 scopus 로고    scopus 로고
    • SH3-domain-containing proteins function at distinct steps in clathrin-coated vesicle formation
    • Simpson F, Hussain NK, Qualmann B, Kelly RB, Kay BK, et al. 1999. SH3-domain-containing proteins function at distinct steps in clathrin-coated vesicle formation. Nat. Cell Biol. 1:119-24
    • (1999) Nat. Cell Biol. , vol.1 , pp. 119-124
    • Simpson, F.1    Hussain, N.K.2    Qualmann, B.3    Kelly, R.B.4    Kay, B.K.5
  • 72
    • 17544384658 scopus 로고    scopus 로고
    • The endocytic protein intersectin is a major binding partner for the Ras exchange factor mSos1 in rat brain
    • Tong XK, Hussain NK, Heuvel E, Kurakin A, Abi-Jaoude E, et al. 2000. The endocytic protein intersectin is a major binding partner for the Ras exchange factor mSos1 in rat brain. EMBO J. 19:1263-71
    • (2000) EMBO J. , vol.19 , pp. 1263-1271
    • Tong, X.K.1    Hussain, N.K.2    Heuvel, E.3    Kurakin, A.4    Abi-Jaoude, E.5
  • 73
    • 0344875509 scopus 로고    scopus 로고
    • Intersectin activates Ras but stimulates transcription through an independent pathway involving JNK
    • Mohney RP, Das M, Bivona TG, Hanes R, Adams AG, et al. 2003. Intersectin activates Ras but stimulates transcription through an independent pathway involving JNK. J. Biol. Chem. 278:47038-45
    • (2003) J. Biol. Chem. , vol.278 , pp. 47038-47045
    • Mohney, R.P.1    Das, M.2    Bivona, T.G.3    Hanes, R.4    Adams, A.G.5
  • 74
    • 0033106167 scopus 로고    scopus 로고
    • The EH and SH3 domain Ese proteins regulate endocytosis by linking to dynamin and Eps175
    • Sengar AS, Wang W, Bishay J, Cohen S, Egan SE. 1999. The EH and SH3 domain Ese proteins regulate endocytosis by linking to dynamin and Eps175. EMBO J. 18:1159-71
    • (1999) EMBO J. , vol.18 , pp. 1159-1171
    • Sengar, A.S.1    Wang, W.2    Bishay, J.3    Cohen, S.4    Egan, S.E.5
  • 75
    • 0034282927 scopus 로고    scopus 로고
    • Intersectin, an adaptor protein involved in clathrin-mediated endocytosis, activates mitogenic signaling pathways
    • Adams A, Thorn JM, Yamabhai M, Kay BK, O'Bryan JP. 2000. Intersectin, an adaptor protein involved in clathrin-mediated endocytosis, activates mitogenic signaling pathways. J. Biol. Chem. 275:27414-20
    • (2000) J. Biol. Chem. , vol.275 , pp. 27414-27420
    • Adams, A.1    Thorn, J.M.2    Yamabhai, M.3    Kay, B.K.4    O'Bryan, J.P.5
  • 76
    • 0242351936 scopus 로고    scopus 로고
    • The odd couple: Signal transduction and endocytosis
    • Teis D, Huber LA. 2003. The odd couple: signal transduction and endocytosis. Cell. Mol. Life Sci. 60:2020-33
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 2020-2033
    • Teis, D.1    Huber, L.A.2
  • 77
    • 0036787904 scopus 로고    scopus 로고
    • Endosomal signaling of epidermal growth factor receptor stimulates signal transduction pathways leading to cell survival
    • Wang Y, Pennock S, Chen X, Wang Z. 2002. Endosomal signaling of epidermal growth factor receptor stimulates signal transduction pathways leading to cell survival. Mol. Cell. Biol. 22:7279-90
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7279-7290
    • Wang, Y.1    Pennock, S.2    Chen, X.3    Wang, Z.4
  • 80
    • 0032401757 scopus 로고    scopus 로고
    • All in the family? New insights and questions regarding interconnectivity of Ras, Rap1 and Ral
    • Bos JL. 1998. All in the family? New insights and questions regarding interconnectivity of Ras, Rap1 and Ral. EMBO J. 17:6776-82
    • (1998) EMBO J. , vol.17 , pp. 6776-6782
    • Bos, J.L.1
  • 81
    • 13944263579 scopus 로고    scopus 로고
    • Ras-independent activation of ERK signaling via the torso receptor tyrosine kinase is mediated by Rap1
    • Mishra S, Smolik SM, Forte MA, Stork PJ. 2005. Ras-independent activation of ERK signaling via the torso receptor tyrosine kinase is mediated by Rap1. Curr. Biol. 15:366-70
    • (2005) Curr. Biol. , vol.15 , pp. 366-370
    • Mishra, S.1    Smolik, S.M.2    Forte, M.A.3    Stork, P.J.4
  • 82
    • 27644475483 scopus 로고    scopus 로고
    • Multiple roles of Rap1 in hematopoietic cells: Complementary versus antagonistic functions
    • Stork PJ, Dillon TJ. 2005. Multiple roles of Rap1 in hematopoietic cells: complementary versus antagonistic functions. Blood 106:2952-61
    • (2005) Blood , vol.106 , pp. 2952-2961
    • Stork, P.J.1    Dillon, T.J.2
  • 84
    • 0042490495 scopus 로고    scopus 로고
    • RAPL, a Rap1 -binding molecule that mediates Rap1-induced adhesion through spatial regulation of LFA-1
    • Katagiri K, Maeda A, Shimonaka M, Kinashi T. 2003. RAPL, a Rap1 -binding molecule that mediates Rap1-induced adhesion through spatial regulation of LFA-1. Nat. Immunol. 4:741-48
    • (2003) Nat. Immunol. , vol.4 , pp. 741-748
    • Katagiri, K.1    Maeda, A.2    Shimonaka, M.3    Kinashi, T.4
  • 85
    • 4344691642 scopus 로고    scopus 로고
    • Membranes as messengers in T cell adhesion signaling
    • Dustin ML, Bivona TG, Philips MR. 2004. Membranes as messengers in T cell adhesion signaling. Nat. Immunol. 5:363-72
    • (2004) Nat. Immunol. , vol.5 , pp. 363-372
    • Dustin, M.L.1    Bivona, T.G.2    Philips, M.R.3
  • 86
    • 0035963331 scopus 로고    scopus 로고
    • Spatio-temporal images of growth-factor-induced activation of Ras and Rap1
    • Mochizuki N, Yamashita S, Kurokawa K, Ohba Y, Nagai T, et al. 2001. Spatio-temporal images of growth-factor-induced activation of Ras and Rap1. Nature 411:1065-68
    • (2001) Nature , vol.411 , pp. 1065-1068
    • Mochizuki, N.1    Yamashita, S.2    Kurokawa, K.3    Ohba, Y.4    Nagai, T.5
  • 87
    • 23844509495 scopus 로고    scopus 로고
    • Protein kinase D1 and the β1 integrin cytoplasmic domain control β1 integrin function via regulation of Rap1 activation
    • Medeiros RB, Dickey DM, Chung H, Quale AC, Nagarajan LR, et al. 2005. Protein kinase D1 and the β1 integrin cytoplasmic domain control β1 integrin function via regulation of Rap1 activation. Immunity 23:213-26
    • (2005) Immunity , vol.23 , pp. 213-226
    • Medeiros, R.B.1    Dickey, D.M.2    Chung, H.3    Quale, A.C.4    Nagarajan, L.R.5
  • 88
    • 0035426219 scopus 로고    scopus 로고
    • Nerve growth factor activates persistent Rap1 signaling in endosomes
    • Wu C, Lai CF, Mobley WC. 2001. Nerve growth factor activates persistent Rap1 signaling in endosomes. J. Neurosci. 21:5406-16
    • (2001) J. Neurosci. , vol.21 , pp. 5406-5416
    • Wu, C.1    Lai, C.F.2    Mobley, W.C.3
  • 89
    • 0842333853 scopus 로고    scopus 로고
    • Signaling endosome hypothesis: A cellular mechanism for long distance communication
    • Howe CL, Mobley WC. 2004. Signaling endosome hypothesis: a cellular mechanism for long distance communication. J. Neurobiol. 58:207-16
    • (2004) J. Neurobiol. , vol.58 , pp. 207-216
    • Howe, C.L.1    Mobley, W.C.2
  • 90
    • 10544248585 scopus 로고    scopus 로고
    • Endocytosis of activated TrkA: Evidence that nerve growth factor induces formation of signaling endosomes
    • Grimes ML, Zhou J, Beattie EC, Yuen EC, Hall DE, et al. 1996. Endocytosis of activated TrkA: evidence that nerve growth factor induces formation of signaling endosomes. J. Neurosci. 16:7950-64
    • (1996) J. Neurosci. , vol.16 , pp. 7950-7964
    • Grimes, M.L.1    Zhou, J.2    Beattie, E.C.3    Yuen, E.C.4    Hall, D.E.5
  • 91
    • 0035819073 scopus 로고    scopus 로고
    • NGF signaling from clathrin-coated vesicles: Evidence that signaling endosomes serve as a platform for the Ras-MAPK pathway
    • Howe CL, Valletta JS, Rusnak AS, Mobley WC. 2001. NGF signaling from clathrin-coated vesicles: evidence that signaling endosomes serve as a platform for the Ras-MAPK pathway. Neuron 32:801-14
    • (2001) Neuron , vol.32 , pp. 801-814
    • Howe, C.L.1    Valletta, J.S.2    Rusnak, A.S.3    Mobley, W.C.4
  • 92
    • 13844275312 scopus 로고    scopus 로고
    • Long-distance retrograde neurotrophic signaling
    • Howe CL, Mobley WC. 2005. Long-distance retrograde neurotrophic signaling. Curr. Opin. Neurobiol. 15:40-48
    • (2005) Curr. Opin. Neurobiol. , vol.15 , pp. 40-48
    • Howe, C.L.1    Mobley, W.C.2
  • 94
    • 0034044227 scopus 로고    scopus 로고
    • Neurotrophin signal transduction in the nervous system
    • Kaplan DR, Miller FD. 2000. Neurotrophin signal transduction in the nervous system. Curr. Opin. Neurobiol. 10:381-91
    • (2000) Curr. Opin. Neurobiol. , vol.10 , pp. 381-391
    • Kaplan, D.R.1    Miller, F.D.2
  • 95
    • 0028872649 scopus 로고
    • Specificity of receptor tyrosine kinase signaling: Transient versus sustained extracellular signal-regulated kinase activation
    • Marshall CJ. 1995. Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation. Cell 80:179-85
    • (1995) Cell , vol.80 , pp. 179-185
    • Marshall, C.J.1
  • 96
    • 0034255428 scopus 로고    scopus 로고
    • Cell surface Trk receptors mediate NGF-induced survival while internalized receptors regulate NGF-induced differentiation
    • Zhang Y, Moheban DB, Conway BR, Bhattacharyya A, Segal RA. 2000. Cell surface Trk receptors mediate NGF-induced survival while internalized receptors regulate NGF-induced differentiation. J. Neurosci. 20:5671-78
    • (2000) J. Neurosci. , vol.20 , pp. 5671-5678
    • Zhang, Y.1    Moheban, D.B.2    Conway, B.R.3    Bhattacharyya, A.4    Segal, R.A.5
  • 97
    • 0033776498 scopus 로고    scopus 로고
    • Role of phosphoinositide 3-kinase and endocytosis in nerve growth factor-induced extracellular signal-regulated kinase activation via Ras and Rap1
    • York RD, Molliver DC, Grewal SS, Stenberg PE, McCleskey EW, Stork PJ. 2000. Role of phosphoinositide 3-kinase and endocytosis in nerve growth factor-induced extracellular signal-regulated kinase activation via Ras and Rap1. Mol. Cell. Biol. 20:8069-83
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8069-8083
    • York, R.D.1    Molliver, D.C.2    Grewal, S.S.3    Stenberg, P.E.4    McCleskey, E.W.5    Stork, P.J.6
  • 98
    • 3242698182 scopus 로고    scopus 로고
    • A neurotrophin signaling cascade coordinates sympathetic neuron development through differential control of TrkA trafficking and retrograde signaling
    • Kuruvilla R, Zweifel LS, Glebova NO, Lonze BE, Valdez G, et al. 2004. A neurotrophin signaling cascade coordinates sympathetic neuron development through differential control of TrkA trafficking and retrograde signaling. Cell 118:243-55
    • (2004) Cell , vol.118 , pp. 243-255
    • Kuruvilla, R.1    Zweifel, L.S.2    Glebova, N.O.3    Lonze, B.E.4    Valdez, G.5
  • 99
    • 0034689003 scopus 로고    scopus 로고
    • β-arrestin-dependent endocytosis of proteinase-activated receptor 2 is required for intracellular targeting of activated ERK1/2
    • DeFea KA, Zalevsky J, Thoma MS, Dery O, Mullins RD, Bunnett NW. 2000. β-arrestin-dependent endocytosis of proteinase-activated receptor 2 is required for intracellular targeting of activated ERK1/2. J. Cell Biol. 148:1267-81
    • (2000) J. Cell Biol. , vol.148 , pp. 1267-1281
    • DeFea, K.A.1    Zalevsky, J.2    Thoma, M.S.3    Dery, O.4    Mullins, R.D.5    Bunnett, N.W.6
  • 100
    • 0742289969 scopus 로고    scopus 로고
    • Signal transduction pathways mediated by the interaction of CpG DNA with Toll-like receptor 9
    • Takeshita F, Gursel I, Ishii KJ, Suzuki K, Gursel M, Klinman DM. 2004. Signal transduction pathways mediated by the interaction of CpG DNA with Toll-like receptor 9. Semin. Immunol. 16:17-22
    • (2004) Semin. Immunol. , vol.16 , pp. 17-22
    • Takeshita, F.1    Gursel, I.2    Ishii, K.J.3    Suzuki, K.4    Gursel, M.5    Klinman, D.M.6
  • 101
    • 0036318851 scopus 로고    scopus 로고
    • Bacterial CpG-DNA and lipopolysaccharides activate Toll-like receptors at distinct cellular compartments
    • Ahmad-Nejad P, Hacker H, Rutz M, Bauer S, Vabulas RM, Wagner H. 2002. Bacterial CpG-DNA and lipopolysaccharides activate Toll-like receptors at distinct cellular compartments. Eur. J. Immunol. 32:1958-68
    • (2002) Eur. J. Immunol. , vol.32 , pp. 1958-1968
    • Ahmad-Nejad, P.1    Hacker, H.2    Rutz, M.3    Bauer, S.4    Vabulas, R.M.5    Wagner, H.6
  • 102
    • 17844380477 scopus 로고    scopus 로고
    • Spatiotemporal regulation of MyD88-IRF-7 signalling for robust type-I interferon induction
    • Honda K, Ohba Y, Yanai H, Negishi H, Mizutani T, et al. 2005. Spatiotemporal regulation of MyD88-IRF-7 signalling for robust type-I interferon induction. Nature 434:1035-40
    • (2005) Nature , vol.434 , pp. 1035-1040
    • Honda, K.1    Ohba, Y.2    Yanai, H.3    Negishi, H.4    Mizutani, T.5
  • 103
    • 0031685620 scopus 로고    scopus 로고
    • TGF-β signal transduction
    • Massague J. 1998. TGF-β signal transduction. Annu. Rev. Biochem. 67:753-91
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 753-791
    • Massague, J.1
  • 104
    • 0037144841 scopus 로고    scopus 로고
    • TGF β receptor internalization into EEA1-enriched early endosomes: Role in signaling to Smad2
    • Hayes S, Chawla A, Corvera S. 2002. TGF β receptor internalization into EEA1-enriched early endosomes: role in signaling to Smad2. J. Cell Biol. 158:1239-49
    • (2002) J. Cell Biol. , vol.158 , pp. 1239-1249
    • Hayes, S.1    Chawla, A.2    Corvera, S.3
  • 105
  • 106
    • 0034051852 scopus 로고    scopus 로고
    • Ligand endocytosis drives receptor dissociation and activation in the Notch pathway
    • Parks AL, Klueg KM, Stout JR, Muskavitch MA. 2000. Ligand endocytosis drives receptor dissociation and activation in the Notch pathway. Development 127:1373-85
    • (2000) Development , vol.127 , pp. 1373-1385
    • Parks, A.L.1    Klueg, K.M.2    Stout, J.R.3    Muskavitch, M.A.4
  • 107
    • 3142704315 scopus 로고    scopus 로고
    • Monoubiquitination and endocytosis direct gamma-secretase cleavage of activated Notch receptor
    • Gupta-Rossi N, Six E, LeBail O, Logeat F, Chastagner P, et al. 2004. Monoubiquitination and endocytosis direct gamma-secretase cleavage of activated Notch receptor. J. Cell Biol. 166:73-83
    • (2004) J. Cell Biol. , vol.166 , pp. 73-83
    • Gupta-Rossi, N.1    Six, E.2    LeBail, O.3    Logeat, F.4    Chastagner, P.5
  • 108
    • 0033458831 scopus 로고    scopus 로고
    • Scaffolding and protein interactions in MAP kinase modules
    • Karandikar M, Cobb MH. 1999. Scaffolding and protein interactions in MAP kinase modules. Cell Calcium 26:219-26
    • (1999) Cell Calcium , vol.26 , pp. 219-226
    • Karandikar, M.1    Cobb, M.H.2
  • 109
    • 0037436155 scopus 로고    scopus 로고
    • Rewiring MAP kinase pathways using alternative scaffold assembly mechanisms
    • Park SH, Zarrinpar A, Lim WA. 2003. Rewiring MAP kinase pathways using alternative scaffold assembly mechanisms. Science 299:1061-64
    • (2003) Science , vol.299 , pp. 1061-1064
    • Park, S.H.1    Zarrinpar, A.2    Lim, W.A.3
  • 111
    • 0029559183 scopus 로고
    • The C. elegans ksr-1 gene encodes a novel Raf-related kinase involved in Ras-mediated signal transduction
    • Sundaram M, Han M. 1995. The C. elegans ksr-1 gene encodes a novel Raf-related kinase involved in Ras-mediated signal transduction. Cell 83:889-901
    • (1995) Cell , vol.83 , pp. 889-901
    • Sundaram, M.1    Han, M.2
  • 112
    • 0029588204 scopus 로고
    • The ksr-1 gene encodes a novel protein kinase involved in Ras-mediated signaling in C. elegans
    • Kornfeld K, Horn DB, Horvitz HR. 1995. The ksr-1 gene encodes a novel protein kinase involved in Ras-mediated signaling in C. elegans. Cell 83:903-13
    • (1995) Cell , vol.83 , pp. 903-913
    • Kornfeld, K.1    Horn, D.B.2    Horvitz, H.R.3
  • 113
    • 0032959886 scopus 로고    scopus 로고
    • Identification of constitutive and ras-inducible phosphorylation sites of KSR: Implications for 14-3-3 binding, mitogen-activated protein kinase binding, and KSR overexpression
    • Cacace AM, Michaud NR, Therrien M, Mathes K, Copeland T, et al. 1999. Identification of constitutive and ras-inducible phosphorylation sites of KSR: implications for 14-3-3 binding, mitogen-activated protein kinase binding, and KSR overexpression. Mol. Cell. Biol. 19:229-40
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 229-240
    • Cacace, A.M.1    Michaud, N.R.2    Therrien, M.3    Mathes, K.4    Copeland, T.5
  • 114
    • 0035930343 scopus 로고    scopus 로고
    • C-TAK1 regulates Ras signaling by phosphorylating the MAPK scaffold, KSR1
    • Muller J, Ory S, Copeland T, Piwnica-Worms H, Morrison DK. 2001. C-TAK1 regulates Ras signaling by phosphorylating the MAPK scaffold, KSR1. Mol. Cell 8:983-93
    • (2001) Mol. Cell , vol.8 , pp. 983-993
    • Muller, J.1    Ory, S.2    Copeland, T.3    Piwnica-Worms, H.4    Morrison, D.K.5
  • 115
    • 0036301210 scopus 로고    scopus 로고
    • Solution structure and functional analysis of the cysteine-rich C1 domain of kinase suppressor of Ras (KSR)
    • Zhou M, Horita DA, Waugh DS, Byrd RA, Morrison DK. 2002. Solution structure and functional analysis of the cysteine-rich C1 domain of kinase suppressor of Ras (KSR). J. Mol. Biol. 315:435-46
    • (2002) J. Mol. Biol. , vol.315 , pp. 435-446
    • Zhou, M.1    Horita, D.A.2    Waugh, D.S.3    Byrd, R.A.4    Morrison, D.K.5
  • 116
    • 0036239642 scopus 로고    scopus 로고
    • Kinase suppressor of Ras (KSR) is a scaffold which facilitates mitogen-activated protein kinase activation in vivo
    • Nguyen A, Burack WR, Stock JL, Kortum R, Chaika OV, et al. 2002. Kinase suppressor of Ras (KSR) is a scaffold which facilitates mitogen-activated protein kinase activation in vivo. Mol. Cell. Biol. 22:3035-45
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 3035-3045
    • Nguyen, A.1    Burack, W.R.2    Stock, J.L.3    Kortum, R.4    Chaika, O.V.5
  • 117
    • 0032508538 scopus 로고    scopus 로고
    • MP1: A MEK binding partner that enhances enzymatic activation of the MAP kinase cascade
    • Schaeffer HJ, Catling AD, Eblen ST, Collier LS, Krauss A, Weber MJ. 1998. MP1: a MEK binding partner that enhances enzymatic activation of the MAP kinase cascade. Science 281:1668-71
    • (1998) Science , vol.281 , pp. 1668-1671
    • Schaeffer, H.J.1    Catling, A.D.2    Eblen, S.T.3    Collier, L.S.4    Krauss, A.5    Weber, M.J.6
  • 118
    • 0036899420 scopus 로고    scopus 로고
    • Localization of the MP1-MAPK scaffold complex to endosomes is mediated by p14 and required for signal transduction
    • Teis D, Wunderlich W, Huber LA. 2002. Localization of the MP1-MAPK scaffold complex to endosomes is mediated by p14 and required for signal transduction. Dev. Cell 3:803-14
    • (2002) Dev. Cell , vol.3 , pp. 803-814
    • Teis, D.1    Wunderlich, W.2    Huber, L.A.3
  • 119
    • 0036473397 scopus 로고    scopus 로고
    • The role of β-arrestins in the termination and transduction of G-protein-coupled receptor signals
    • Luttrell LM, Lefkowitz RJ. 2002. The role of β-arrestins in the termination and transduction of G-protein-coupled receptor signals. J. Cell Sci. 115:455-65
    • (2002) J. Cell Sci. , vol.115 , pp. 455-465
    • Luttrell, L.M.1    Lefkowitz, R.J.2
  • 120
    • 0033616494 scopus 로고    scopus 로고
    • The β2-adrenergic receptor/βarrestin complex recruits the clathrin adaptor AP-2 during endocytosis
    • Laporte SA, Oakley RH, Zhang J, Holt JA, Ferguson SS, et al. 1999. The β2-adrenergic receptor/βarrestin complex recruits the clathrin adaptor AP-2 during endocytosis. Proc. Natl. Acad. Sci. USA 96:3712-17
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3712-3717
    • Laporte, S.A.1    Oakley, R.H.2    Zhang, J.3    Holt, J.A.4    Ferguson, S.S.5
  • 121
    • 0029770657 scopus 로고    scopus 로고
    • β-arrestin acts as a clathrin adaptor in endocytosis of the β2-adrenergic receptor
    • Goodman OB Jr, Krupnick JG, Santini F, Gurevich W, Penn RB, et al. 1996. β-arrestin acts as a clathrin adaptor in endocytosis of the β2-adrenergic receptor. Nature 383:447-50
    • (1996) Nature , vol.383 , pp. 447-450
    • Goodman Jr., O.B.1    Krupnick, J.G.2    Santini, F.3    Gurevich, W.4    Penn, R.B.5
  • 123
    • 0034711397 scopus 로고    scopus 로고
    • β-arrestin 2: A receptor-regulated MAPK scaffold for the activation of JNK3
    • McDonald PH, Chow CW, Miller WE, Laporte SA, Field ME, et al. 2000. β-arrestin 2: a receptor-regulated MAPK scaffold for the activation of JNK3. Science 290:1574-77
    • (2000) Science , vol.290 , pp. 1574-1577
    • McDonald, P.H.1    Chow, C.W.2    Miller, W.E.3    Laporte, S.A.4    Field, M.E.5
  • 124
    • 0036173032 scopus 로고    scopus 로고
    • Sef is a feedback-induced antagonist of Ras/MAPK-mediated FGF signalling
    • Furthauer M, Lin W, Ang SL, Thisse B, Thisse C. 2002. Sef is a feedback-induced antagonist of Ras/MAPK-mediated FGF signalling. Nat. Cell Biol. 4:170-74
    • (2002) Nat. Cell Biol. , vol.4 , pp. 170-174
    • Furthauer, M.1    Lin, W.2    Ang, S.L.3    Thisse, B.4    Thisse, C.5
  • 125
    • 0036170142 scopus 로고    scopus 로고
    • Identification of Sef, a novel modulator of FGF signalling
    • Tsang M, Friesel R, Kudoh T, Dawid IB. 2002. Identification of Sef, a novel modulator of FGF signalling. Nat. Cell Biol. 4:165-69
    • (2002) Nat. Cell Biol. , vol.4 , pp. 165-169
    • Tsang, M.1    Friesel, R.2    Kudoh, T.3    Dawid, I.B.4
  • 127
    • 3242701513 scopus 로고    scopus 로고
    • Sef: A MEK/ERK catcher on the Golgi
    • Philips MR. 2004. Sef: a MEK/ERK catcher on the Golgi. Mol. Cell 15:168-69
    • (2004) Mol. Cell , vol.15 , pp. 168-169
    • Philips, M.R.1
  • 128
  • 129
    • 0032538927 scopus 로고    scopus 로고
    • Direct pathway from early/recycling endosomes to the Golgi apparatus revealed through the study of shiga toxin B-fragment transport
    • Mallard F, Antony C, Tenza D, Salamero J, Goud B, Johannes L. 1998. Direct pathway from early/recycling endosomes to the Golgi apparatus revealed through the study of shiga toxin B-fragment transport. J. Cell Biol. 143:973-90
    • (1998) J. Cell Biol. , vol.143 , pp. 973-990
    • Mallard, F.1    Antony, C.2    Tenza, D.3    Salamero, J.4    Goud, B.5    Johannes, L.6
  • 130
    • 0041488671 scopus 로고    scopus 로고
    • Phospholipase C gamma activates Ras on the Golgi apparatus by means of RasGRP1
    • Bivona TG, Pérez de Castro I, Ahearn IM, Grana TM, Chiu VK, et al. 2003. Phospholipase C gamma activates Ras on the Golgi apparatus by means of RasGRP1. Nature 424:694-98
    • (2003) Nature , vol.424 , pp. 694-698
    • Bivona, T.G.1    Pérez De Castro, I.2    Ahearn, I.M.3    Grana, T.M.4    Chiu, V.K.5
  • 132
    • 1842609782 scopus 로고    scopus 로고
    • Ras activation in Jurkat T cells following low-grade stimulation of the T-cell receptor is specific to N-Ras and occurs only on the Golgi
    • Pérez de Castro I, Bivona T, Philips M, Pellicer A. 2004. Ras activation in Jurkat T cells following low-grade stimulation of the T-cell receptor is specific to N-Ras and occurs only on the Golgi. Mol. Cell. Biol. 24:3485-96
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 3485-3496
    • Pérez De Castro, I.1    Bivona, T.2    Philips, M.3    Pellicer, A.4
  • 133
    • 0042858184 scopus 로고    scopus 로고
    • Exchange factors of the RasGRP family mediate Ras activation in the Golgi
    • Caloca MJ, Zugaza JL, Bustelo XR. 2003. Exchange factors of the RasGRP family mediate Ras activation in the Golgi. J. Biol. Chem. 278:33465-73
    • (2003) J. Biol. Chem. , vol.278 , pp. 33465-33473
    • Caloca, M.J.1    Zugaza, J.L.2    Bustelo, X.R.3
  • 134
    • 2542444383 scopus 로고    scopus 로고
    • Diacylglycerol-dependent binding recruits PKCtheta and RasGRP1 C1 domains to specific subcellular localizations in living T lymphocytes
    • Carrasco S, Merida I. 2004. Diacylglycerol-dependent binding recruits PKCtheta and RasGRP1 C1 domains to specific subcellular localizations in living T lymphocytes. Mol. Biol. Cell 15:2932-42
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2932-2942
    • Carrasco, S.1    Merida, I.2
  • 135
    • 0842304220 scopus 로고    scopus 로고
    • Activation of H-Ras in the endoplasmic reticulum by the RasGRF family guanine nucleotide exchange factors
    • 134a. Arozarena I, Matallanas D, Berciano MT, Sanz-Moreno V, Calvo F, et al. 2004. Activation of H-Ras in the endoplasmic reticulum by the RasGRF family guanine nucleotide exchange factors. Mol. Cell. Biol. 24(4):1516-30
    • (2004) Mol. Cell. Biol. , vol.24 , Issue.4 , pp. 1516-1530
    • Arozarena, I.1    Matallanas, D.2    Berciano, M.T.3    Sanz-Moreno, V.4    Calvo, F.5
  • 136
    • 0038111847 scopus 로고    scopus 로고
    • A novel Ras inhibitor, Eri1, engages yeast Ras at the endoplasmic reticulum
    • Sobering AK, Romeo MJ, Vay HA, Levin DE. 2003. A novel Ras inhibitor, Eri1, engages yeast Ras at the endoplasmic reticulum. Mol. Cell. Biol. 23:4983-90
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 4983-4990
    • Sobering, A.K.1    Romeo, M.J.2    Vay, H.A.3    Levin, D.E.4
  • 137
    • 2542423740 scopus 로고    scopus 로고
    • Yeast Ras regulates the complex that catalyzes the first step in GPI-anchor biosynthesis at the ER
    • Sobering AK, Watanabe R, Romeo MJ, Yan BC, Specht CA, et al. 2004. Yeast Ras regulates the complex that catalyzes the first step in GPI-anchor biosynthesis at the ER. Cell 117:637-48
    • (2004) Cell , vol.117 , pp. 637-648
    • Sobering, A.K.1    Watanabe, R.2    Romeo, M.J.3    Yan, B.C.4    Specht, C.A.5
  • 138
    • 0037416134 scopus 로고    scopus 로고
    • Regulation of cytochrome c oxidase activity by c-Src in osteoclasts
    • Miyazaki T, Neff L, Tanaka S, Home WC, Baron R. 2003. Regulation of cytochrome c oxidase activity by c-Src in osteoclasts. J. Cell Biol. 160:709-18
    • (2003) J. Cell Biol. , vol.160 , pp. 709-718
    • Miyazaki, T.1    Neff, L.2    Tanaka, S.3    Home, W.C.4    Baron, R.5
  • 139
    • 3543025709 scopus 로고    scopus 로고
    • Phosphorylation of Y845 on the epidermal growth factor receptor mediates binding to the mitochondrial protein cytochrome c oxidase subunit II
    • Boerner JL, Demory ML, Silva C, Parsons SJ. 2004. Phosphorylation of Y845 on the epidermal growth factor receptor mediates binding to the mitochondrial protein cytochrome c oxidase subunit II. Mol. Cell. Biol. 24:7059-71
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 7059-7071
    • Boerner, J.L.1    Demory, M.L.2    Silva, C.3    Parsons, S.J.4
  • 140
    • 22544454482 scopus 로고    scopus 로고
    • Involvement of a mitochondrial phosphatase in the regulation of ATP production and insulin secretion in pancreatic beta cells
    • Pagliarini DJ, Wiley SE, Kimple ME, Dixon JR, Kelly P, et al. 2005. Involvement of a mitochondrial phosphatase in the regulation of ATP production and insulin secretion in pancreatic beta cells. Mol. Cell 19:197-207
    • (2005) Mol. Cell , vol.19 , pp. 197-207
    • Pagliarini, D.J.1    Wiley, S.E.2    Kimple, M.E.3    Dixon, J.R.4    Kelly, P.5
  • 141
    • 0008573656 scopus 로고    scopus 로고
    • Bcl-2 differentially targets K-, N-, and H-Ras to mitochondria in IL-2 supplemented or deprived cells: Implications in prevention of apoptosis
    • Rebollo A, Perez-Sala D, Martinez AC. 1999. Bcl-2 differentially targets K-, N-, and H-Ras to mitochondria in IL-2 supplemented or deprived cells: implications in prevention of apoptosis. Oncogene 18:4930-39
    • (1999) Oncogene , vol.18 , pp. 4930-4939
    • Rebollo, A.1    Perez-Sala, D.2    Martinez, A.C.3
  • 142
    • 0345498292 scopus 로고    scopus 로고
    • Bcl-2 targets the protein kinase Raf-1 to mitochondria
    • Wang HG, Rapp UR, Reed JC. 1996. Bcl-2 targets the protein kinase Raf-1 to mitochondria. Cell 87:629-38
    • (1996) Cell , vol.87 , pp. 629-638
    • Wang, H.G.1    Rapp, U.R.2    Reed, J.C.3
  • 143
    • 33646189552 scopus 로고    scopus 로고
    • Phosphorylation of K-Ras by PKC regulates a farnesyl-electrostatic switch that promotes association with Bcl-XI on mitochondria and induces apoptosis
    • In press
    • 141a. Bivona TG, Quatela SE, Bodemann BO, Ahearn IM, Soskis MJ, et al. 2006. Phosphorylation of K-Ras by PKC regulates a farnesyl-electrostatic switch that promotes association with Bcl-XI on mitochondria and induces apoptosis. Mol. Cell. In press
    • (2006) Mol. Cell.
    • Bivona, T.G.1    Quatela, S.E.2    Bodemann, B.O.3    Ahearn, I.M.4    Soskis, M.J.5
  • 144
    • 0036273905 scopus 로고    scopus 로고
    • Two ras pathways in fission yeast are differentially regulated by two ras guanine nucleotide exchange factors
    • Papadaki P, Pizon V, Onken B, Chang EC. 2002. Two ras pathways in fission yeast are differentially regulated by two ras guanine nucleotide exchange factors. Mol. Cell. Biol. 22:4598-606
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4598-4606
    • Papadaki, P.1    Pizon, V.2    Onken, B.3    Chang, E.C.4
  • 145
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K, Ikonen E. 1997. Functional rafts in cell membranes. Nature 387:569-72
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 146
    • 0031692336 scopus 로고    scopus 로고
    • The caveolae membrane system
    • Anderson RG. 1998. The caveolae membrane system. Annu. Rev. Biochem. 67:199-225
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 199-225
    • Anderson, R.G.1
  • 148
    • 0344585437 scopus 로고    scopus 로고
    • Lipid rafts: Elusive or illusive?
    • Munro S. 2003. Lipid rafts: elusive or illusive? Cell 115:377-88
    • (2003) Cell , vol.115 , pp. 377-388
    • Munro, S.1
  • 149
    • 0032696038 scopus 로고    scopus 로고
    • Regulated migration of epidermal growth factor receptor from caveolae
    • Mineo C, Gill GN, Anderson RG. 1999. Regulated migration of epidermal growth factor receptor from caveolae. J. Biol. Chem. 274:30636-43
    • (1999) J. Biol. Chem. , vol.274 , pp. 30636-30643
    • Mineo, C.1    Gill, G.N.2    Anderson, R.G.3
  • 150
    • 0037427329 scopus 로고    scopus 로고
    • Membrane insertion of a lipidated ras peptide studied by FTIR, solid-state NMR, and neutron diffraction spectroscopy
    • Huster D, Vogel A, Katzka C, Scheidt HA, Binder H, et al. 2003. Membrane insertion of a lipidated ras peptide studied by FTIR, solid-state NMR, and neutron diffraction spectroscopy. J. Am. Chem. Soc. 125:4070-79
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 4070-4079
    • Huster, D.1    Vogel, A.2    Katzka, C.3    Scheidt, H.A.4    Binder, H.5
  • 151
    • 0033525077 scopus 로고    scopus 로고
    • Role of lipid modifications in targeting proteins to detergent-resistant membrane rafts. Many raft proteins are acylated, while few are prenylated
    • Melkonian KA, Ostermeyer AG, Chen JZ, Roth MG, Brown DA. 1999. Role of lipid modifications in targeting proteins to detergent-resistant membrane rafts. Many raft proteins are acylated, while few are prenylated. J. Biol. Chem. 274:3910-17
    • (1999) J. Biol. Chem. , vol.274 , pp. 3910-3917
    • Melkonian, K.A.1    Ostermeyer, A.G.2    Chen, J.Z.3    Roth, M.G.4    Brown, D.A.5
  • 152
    • 0032516835 scopus 로고    scopus 로고
    • Cholesterol depletion of caveolae causes hyperactivation of extracellular signal-related kinase (ERK)
    • Furuchi T, Anderson RG. 1998. Cholesterol depletion of caveolae causes hyperactivation of extracellular signal-related kinase (ERK). J. Biol. Chem. 273:21099-104
    • (1998) J. Biol. Chem. , vol.273 , pp. 21099-21104
    • Furuchi, T.1    Anderson, R.G.2
  • 153
    • 0029912981 scopus 로고    scopus 로고
    • Co-purification and direct interaction of Ras with caveolin, an integral membrane protein of caveolae microdomains. Detergent-free purification of caveolae microdomains
    • Song KS, Li S, Okamoto T, Quilliam LA, Sargiacomo M, Lisanti MP. 1996. Co-purification and direct interaction of Ras with caveolin, an integral membrane protein of caveolae microdomains. Detergent-free purification of caveolae microdomains. J. Biol. Chem. 271:9690-97
    • (1996) J. Biol. Chem. , vol.271 , pp. 9690-9697
    • Song, K.S.1    Li, S.2    Okamoto, T.3    Quilliam, L.A.4    Sargiacomo, M.5    Lisanti, M.P.6
  • 155
    • 0037455589 scopus 로고    scopus 로고
    • Direct visualization of Ras proteins in spatially distinct cell surface microdomains
    • Prior IA, Muncke C, Parton RG, Hancock JF. 2003. Direct visualization of Ras proteins in spatially distinct cell surface microdomains. J. Cell Biol. 160:165-70
    • (2003) J. Cell Biol. , vol.160 , pp. 165-170
    • Prior, I.A.1    Muncke, C.2    Parton, R.G.3    Hancock, J.F.4
  • 156
    • 3242657115 scopus 로고    scopus 로고
    • Three separable domains regulate GTP-dependent association of H-ras with the plasma membrane
    • Rotblat B, Prior IA, Muncke C, Parton RG, Kloog Y, et al. 2004. Three separable domains regulate GTP-dependent association of H-ras with the plasma membrane. Mol. Cell. Biol. 24:6799-810
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 6799-6810
    • Rotblat, B.1    Prior, I.A.2    Muncke, C.3    Parton, R.G.4    Kloog, Y.5
  • 158
  • 159
    • 22144479017 scopus 로고    scopus 로고
    • Ras plasma membrane signalling platforms
    • Hancock JF, Parton RG. 2005. Ras plasma membrane signalling platforms. Biochem. J. 389:1-11
    • (2005) Biochem. J. , vol.389 , pp. 1-11
    • Hancock, J.F.1    Parton, R.G.2
  • 160
    • 0033998793 scopus 로고    scopus 로고
    • The role of lipid rafts in T cell antigen receptor (TCR) signalling
    • Janes PW, Ley SC, Magee AI, Kabouridis PS. 2000. The role of lipid rafts in T cell antigen receptor (TCR) signalling. Semin. Immunol. 12:23-34
    • (2000) Semin. Immunol. , vol.12 , pp. 23-34
    • Janes, P.W.1    Ley, S.C.2    Magee, A.I.3    Kabouridis, P.S.4
  • 161
    • 0034051162 scopus 로고    scopus 로고
    • Membrane rafts and signaling by the multichain immune recognition receptors
    • Langlet C, Bernard AM, Drevot P, He HT. 2000. Membrane rafts and signaling by the multichain immune recognition receptors. Curr. Opin. Immunol. 12:250-55
    • (2000) Curr. Opin. Immunol. , vol.12 , pp. 250-255
    • Langlet, C.1    Bernard, A.M.2    Drevot, P.3    He, H.T.4
  • 162
    • 0032101348 scopus 로고    scopus 로고
    • Membrane compartmentation is required for efficient T cell activation
    • Xavier R, Brennan T, Li Q, McCormack C, Seed B. 1998. Membrane compartmentation is required for efficient T cell activation. Immunity 8:723-32
    • (1998) Immunity , vol.8 , pp. 723-732
    • Xavier, R.1    Brennan, T.2    Li, Q.3    McCormack, C.4    Seed, B.5
  • 163
    • 0032727709 scopus 로고    scopus 로고
    • Aggregation of lipid rafts accompanies signaling via the T cell antigen receptor
    • Janes PW, Ley SC, Magee AI. 1999. Aggregation of lipid rafts accompanies signaling via the T cell antigen receptor. J. Cell Biol. 147:447-61
    • (1999) J. Cell Biol. , vol.147 , pp. 447-461
    • Janes, P.W.1    Ley, S.C.2    Magee, A.I.3
  • 164
    • 0032498231 scopus 로고    scopus 로고
    • LAT: The ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation
    • Zhang W, Sloan-Lancaster J, Kitchen J, Trible RP, Samelson LE. 1998. LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation. Cell 92:83-92
    • (1998) Cell , vol.92 , pp. 83-92
    • Zhang, W.1    Sloan-Lancaster, J.2    Kitchen, J.3    Trible, R.P.4    Samelson, L.E.5
  • 165
    • 0032142953 scopus 로고    scopus 로고
    • LAT palmitoylation: Its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation
    • Zhang W, Trible RP, Samelson LE. 1998. LAT palmitoylation: its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation. Immunity 9:239-46
    • (1998) Immunity , vol.9 , pp. 239-246
    • Zhang, W.1    Trible, R.P.2    Samelson, L.E.3
  • 166
    • 0033613826 scopus 로고    scopus 로고
    • T lymphocyte costimulation mediated by reorganization of membrane microdomains
    • Viola A, Schroeder S, Sakakibara Y, Lanzavecchia A. 1999. T lymphocyte costimulation mediated by reorganization of membrane microdomains. Science 283:680-82
    • (1999) Science , vol.283 , pp. 680-682
    • Viola, A.1    Schroeder, S.2    Sakakibara, Y.3    Lanzavecchia, A.4
  • 167
    • 0032438178 scopus 로고    scopus 로고
    • Engagement of GPI-linked CD48 contributes to TCR signals and cytoskeletal reorganization: A role for lipid rafts in T cell activation
    • Moran M, Miceli MC. 1998. Engagement of GPI-linked CD48 contributes to TCR signals and cytoskeletal reorganization: a role for lipid rafts in T cell activation. Immunity 9:787-96
    • (1998) Immunity , vol.9 , pp. 787-796
    • Moran, M.1    Miceli, M.C.2
  • 168
    • 20444404267 scopus 로고    scopus 로고
    • Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in T cells
    • Douglass AD, Vale RD. 2005. Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in T cells. Cell 121:937-50
    • (2005) Cell , vol.121 , pp. 937-950
    • Douglass, A.D.1    Vale, R.D.2
  • 169


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.