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Volumn 5, Issue 243, 2012, Pages

Where EGF receptors transmit their signals

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CLATHRIN; DYNAMIN I; DYNAMIN II; EARLY GROWTH RESPONSE FACTOR 1; EPIDERMAL GROWTH FACTOR RECEPTOR; ESCRT PROTEIN; GROWTH FACTOR RECEPTOR BOUND PROTEIN 2; GUANOSINE TRIPHOSPHATASE; HOMODIMER; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LIGAND; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOLIPASE C GAMMA; PROTEIN FOS; PROTEIN KINASE B; PROTEIN SHC; PROTEIN TYROSINE KINASE; SMALL INTERFERING RNA; TUMOR SUSCEPTIBILITY GENE 101 PROTEIN; UBIQUITIN PROTEIN LIGASE E3;

EID: 84866861514     PISSN: 19450877     EISSN: 19379145     Source Type: Journal    
DOI: 10.1126/scisignal.2003341     Document Type: Review
Times cited : (26)

References (42)
  • 2
    • 84858665104 scopus 로고    scopus 로고
    • Suppression of EGFR endocytosis by dynamin depletion reveals that EGFR signaling occurs primarily at the plasma membrane
    • L. P. Sousa, I. Lax, H. Shen, S. M. Ferguson, P. De Camilli, J. Schlessinger, Suppression of EGFR endocytosis by dynamin depletion reveals that EGFR signaling occurs primarily at the plasma membrane. Proc. Natl. Acad. Sci. U.S.A. 109, 4419-4424 (2012).
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 4419-4424
    • Sousa, L.P.1    Lax, I.2    Shen, H.3    Ferguson, S.M.4    De Camilli, P.5    Schlessinger, J.6
  • 3
    • 0028969961 scopus 로고
    • Intracellular trafficking of epidermal growth factor family ligands is directly influenced by the pH sensitivity of the receptor/ligand interaction
    • A. R. French, D. K. Tadaki, S. K. Niyogi, D. A. Lauffenburger, Intracellular trafficking of epidermal growth factor family ligands is directly influenced by the pH sensitivity of the receptor/ligand interaction. J. Biol. Chem. 270, 4334-4340 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 4334-4340
    • French, A.R.1    Tadaki, D.K.2    Niyogi, S.K.3    Lauffenburger, D.A.4
  • 4
    • 0032128152 scopus 로고    scopus 로고
    • Comparative mitogenic potencies of EGF and TGF alpha and their dependence on receptor-limitation versus ligand-limitation
    • C. C. Reddy, A. Wells, D. A. Lauffenburger, Comparative mitogenic potencies of EGF and TGF alpha and their dependence on receptor-limitation versus ligand-limitation. Med. Biol. Eng. Comput. 36, 499-507 (1998).
    • (1998) Med. Biol. Eng. Comput. , vol.36 , pp. 499-507
    • Reddy, C.C.1    Wells, A.2    Lauffenburger, D.A.3
  • 5
    • 0032974814 scopus 로고    scopus 로고
    • Transforming growth factor-alpha short-circuits downregulation of the epidermal growth factor receptor
    • X. Ouyang, T. Gulliford, G. Huang, R. J. Epstein, Transforming growth factor-alpha short-circuits downregulation of the epidermal growth factor receptor. J. Cell. Physiol. 179, 52-57 (1999).
    • (1999) J. Cell. Physiol. , vol.179 , pp. 52-57
    • Ouyang, X.1    Gulliford, T.2    Huang, G.3    Epstein, R.J.4
  • 6
    • 41149086227 scopus 로고    scopus 로고
    • EGF and amphiregulin differentially regulate Cbl recruitment to endosomes and EGF receptor fate
    • K. A. Stern, T. L. Place, N. L. Lill, EGF and amphiregulin differentially regulate Cbl recruitment to endosomes and EGF receptor fate. Biochem. J. 410, 585-594 (2008).
    • (2008) Biochem. J. , vol.410 , pp. 585-594
    • Stern, K.A.1    Place, T.L.2    Lill, N.L.3
  • 8
    • 0025194462 scopus 로고
    • Intermolecular association of the p185neu protein and EGF receptor modulates EGF receptor function
    • T. Wada, X. L. Qian, M. I. Greene, Intermolecular association of the p185neu protein and EGF receptor modulates EGF receptor function. Cell 61, 1339-1347 (1990).
    • (1990) Cell , vol.61 , pp. 1339-1347
    • Wada, T.1    Qian, X.L.2    Greene, M.I.3
  • 9
    • 0025690737 scopus 로고
    • Heterodimerization of the erbB-1 and erbB-2 receptors in human breast carcinoma cells: A mechanism for receptor transregulation
    • R. Goldman, R. B. Levy, E. Peles, Y. Yarden, Heterodimerization of the erbB-1 and erbB-2 receptors in human breast carcinoma cells: A mechanism for receptor transregulation. Biochemistry 29, 11024-11028 (1990).
    • (1990) Biochemistry , vol.29 , pp. 11024-11028
    • Goldman, R.1    Levy, R.B.2    Peles, E.3    Yarden, Y.4
  • 10
    • 0030944455 scopus 로고    scopus 로고
    • ErbB-2, the preferred heterodimerization partner of all ErbB receptors, is a mediator of lateral signaling
    • D. Graus-Porta, R. R. Beerli, J. M. Daly, N. E. Hynes, ErbB-2, the preferred heterodimerization partner of all ErbB receptors, is a mediator of lateral signaling. EMBO J. 16, 1647-1655 (1997).
    • (1997) EMBO J. , vol.16 , pp. 1647-1655
    • Graus-Porta, D.1    Beerli, R.R.2    Daly, J.M.3    Hynes, N.E.4
  • 11
    • 0033564877 scopus 로고    scopus 로고
    • The C-terminus of the kinase-defective neuregulin receptor ErbB-3 confers mitogenic superiority and dictates endocytic routing
    • H. Waterman, I. Alroy, S. Strano, R. Seger, Y. Yarden, The C-terminus of the kinase-defective neuregulin receptor ErbB-3 confers mitogenic superiority and dictates endocytic routing. EMBO J. 18, 3348-3358 (1999).
    • (1999) EMBO J. , vol.18 , pp. 3348-3358
    • Waterman, H.1    Alroy, I.2    Strano, S.3    Seger, R.4    Yarden, Y.5
  • 13
    • 0027179703 scopus 로고
    • Eps8, a substrate for the epidermal growth factor receptor kinase, enhances EGF-dependent mitogenic signals
    • F. Fazioli, L. Minichiello, V. Matoska, P. Castagnino, T. Miki, W. T. Wong, P. P. Di Fiore, Eps8, a substrate for the epidermal growth factor receptor kinase, enhances EGF-dependent mitogenic signals. EMBO J. 12, 3799-3808 (1993).
    • (1993) EMBO J. , vol.12 , pp. 3799-3808
    • Fazioli, F.1    Minichiello, L.2    Matoska, V.3    Castagnino, P.4    Miki, T.5    Wong, W.T.6    Di Fiore, P.P.7
  • 15
    • 0025681492 scopus 로고
    • Binding of SH2 domains of phospholipase C gamma 1, GAP, and Src to activated growth factor receptors
    • D. Anderson, C. A. Koch, L. Grey, C. Ellis, M. F. Moran, T. Pawson, Binding of SH2 domains of phospholipase C gamma 1, GAP, and Src to activated growth factor receptors. Science 250, 979-982 (1990).
    • (1990) Science , vol.250 , pp. 979-982
    • Anderson, D.1    Koch, C.A.2    Grey, L.3    Ellis, C.4    Moran, M.F.5    Pawson, T.6
  • 16
    • 0031011155 scopus 로고    scopus 로고
    • EGF receptor binding and transformation by v-cbl is ablated by the introduction of a loss-of-function mutation from the Caenorhabditis elegans sli-1 gene
    • C. B. Thien, W. Y. Langdon, EGF receptor binding and transformation by v-cbl is ablated by the introduction of a loss-of-function mutation from the Caenorhabditis elegans sli-1 gene. Oncogene 14, 2239-2249 (1997).
    • (1997) Oncogene , vol.14 , pp. 2239-2249
    • Thien, C.B.1    Langdon, W.Y.2
  • 19
    • 0032860819 scopus 로고    scopus 로고
    • Controlled dimerization of ErbB receptors provides evidence for differential signaling by homo- And heterodimers
    • S. K. Muthuswamy, M. Gilman, J. S. Brugge, Controlled dimerization of ErbB receptors provides evidence for differential signaling by homo- and heterodimers. Mol. Cell. Biol. 19, 6845-6857 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6845-6857
    • Muthuswamy, S.K.1    Gilman, M.2    Brugge, J.S.3
  • 20
    • 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
    • N. L. Lill, P. Douillard, R. A. Awwad, S. Ota, M. L. Lupher Jr., S. Miyake, N. Meissner-Lula, V. W. Hsu, H. Band, The evolutionarily conserved N-terminal region of Cbl is sufficient to enhance down-regulation of the epidermal growth factor receptor. J. Biol. Chem. 275, 367-377 (2000).
    • (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
  • 21
    • 0020657322 scopus 로고
    • Tyrosine phosphorylation of specific proteins after mitogen stimulation of chicken embryo fibroblasts
    • K. D. Nakamura, R. Martinez, M. J. Weber, Tyrosine phosphorylation of specific proteins after mitogen stimulation of chicken embryo fibroblasts. Mol. Cell. Biol. 3, 380-390 (1983).
    • (1983) Mol. Cell. Biol. , vol.3 , pp. 380-390
    • Nakamura, K.D.1    Martinez, R.2    Weber, M.J.3
  • 22
    • 0021312740 scopus 로고
    • Diverse mitogenic agents induce the phosphorylation of two related 42,000-dalton proteins on tyrosine in quiescent chick cells
    • J. A. Cooper, B. M. Sefton, T. Hunter, Diverse mitogenic agents induce the phosphorylation of two related 42,000-dalton proteins on tyrosine in quiescent chick cells. Mol. Cell. Biol. 4, 30-37 (1984).
    • (1984) Mol. Cell. Biol. , vol.4 , pp. 30-37
    • Cooper, J.A.1    Sefton, B.M.2    Hunter, T.3
  • 23
    • 0025316902 scopus 로고
    • Activated type i phosphatidylinositol kinase is associated with the epidermal growth factor (EGF) receptor following EGF stimulation
    • J. D. Bjorge, T. O. Chan, M. Antczak, H. J. Kung, D. J. Fujita, Activated type I phosphatidylinositol kinase is associated with the epidermal growth factor (EGF) receptor following EGF stimulation. Proc. Natl. Acad. Sci. U.S.A. 87, 3816-3820 (1990).
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 3816-3820
    • Bjorge, J.D.1    Chan, T.O.2    Antczak, M.3    Kung, H.J.4    Fujita, D.J.5
  • 24
    • 0024380391 scopus 로고
    • Phospholipase C-gamma is a substrate for the PDGF and EGF receptor protein-tyrosine kinases in vivo and in vitro
    • J. Meisenhelder, P. G. Suh, S. G. Rhee, T. Hunter, Phospholipase C-gamma is a substrate for the PDGF and EGF receptor protein-tyrosine kinases in vivo and in vitro. Cell 57, 1109-1122 (1989).
    • (1989) Cell , vol.57 , pp. 1109-1122
    • Meisenhelder, J.1    Suh, P.G.2    Rhee, S.G.3    Hunter, T.4
  • 25
    • 0033607542 scopus 로고    scopus 로고
    • Internalized epidermal growth factor receptors participate in the activation of p21(ras) in fibroblasts
    • J. M. Haugh, A. C. Huang, H. S. Wiley, A. Wells, D. A. Lauffenburger, Internalized epidermal growth factor receptors participate in the activation of p21(ras) in fibroblasts. J. Biol. Chem. 274, 34350-34360 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 34350-34360
    • Haugh, J.M.1    Huang, A.C.2    Wiley, H.S.3    Wells, A.4    Lauffenburger, D.A.5
  • 26
    • 0035162703 scopus 로고    scopus 로고
    • Regulation of epidermal growth factor receptor signaling by endocytosis and intracellular trafficking
    • P. Burke, K. Schooler, H. S. Wiley, Regulation of epidermal growth factor receptor signaling by endocytosis and intracellular trafficking. Mol. Biol. Cell 12, 1897-1910 (2001).
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1897-1910
    • Burke, P.1    Schooler, K.2    Wiley, H.S.3
  • 27
    • 0034859108 scopus 로고    scopus 로고
    • Internalization of the epidermal growth factor receptor: Role in signalling
    • A. Sorkin, Internalization of the epidermal growth factor receptor: role in signalling. Biochem. Soc. Trans. 29, 480-484 (2001).
    • (2001) Biochem. Soc. Trans. , vol.29 , pp. 480-484
    • Sorkin, A.1
  • 28
    • 0028036513 scopus 로고
    • Induction of mutant dynamin specifically blocks endocytic coated vesicle formation
    • H. Damke, T. Baba, D. E. Warnock, S. L. Schmid, Induction of mutant dynamin specifically blocks endocytic coated vesicle formation. J. Cell Biol. 127, 915-934 (1994).
    • (1994) J. Cell Biol. , vol.127 , pp. 915-934
    • Damke, H.1    Baba, T.2    Warnock, D.E.3    Schmid, S.L.4
  • 29
    • 0034949705 scopus 로고    scopus 로고
    • c-Cbl ubiquitinates the EGF receptor at the plasma membrane and remains receptor associated throughout the endocytic route
    • A. A. de Melker, G. van der Horst, J. Calafat, H. Jansen, J. Borst, c-Cbl ubiquitinates the EGF receptor at the plasma membrane and remains receptor associated throughout the endocytic route. J. Cell Sci. 114, 2167-2178 (2001).
    • (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
  • 30
    • 4344602943 scopus 로고    scopus 로고
    • c-Cbl-mediated ubiquitinylation is required for epidermal growth factor receptor exit from the early endosomes
    • T. Ravid, J. M. Heidinger, P. Gee, E. M. Khan, T. Goldkorn, c-Cbl-mediated ubiquitinylation is required for epidermal growth factor receptor exit from the early endosomes. J. Biol. Chem. 279, 37153-37162 (2004).
    • (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
  • 33
    • 0038825173 scopus 로고    scopus 로고
    • Hrs regulates early endosome fusion by inhibiting formation of an endosomal SNARE complex
    • W. Sun, Q. Yan, T. A. Vida, A. J. Bean, Hrs regulates early endosome fusion by inhibiting formation of an endosomal SNARE complex. J. Cell Biol. 162, 125-137 (2003).
    • (2003) J. Cell Biol. , vol.162 , pp. 125-137
    • Sun, W.1    Yan, Q.2    Vida, T.A.3    Bean, A.J.4
  • 34
    • 0034157875 scopus 로고    scopus 로고
    • Mammalian tumor susceptibility gene 101 (TSG101) and the yeast homologue, Vps23p, both function in late endosomal trafficking
    • M. Babst, G. Odorizzi, E. J. Estepa, S. D. Emr, Mammalian tumor susceptibility gene 101 (TSG101) and the yeast homologue, Vps23p, both function in late endosomal trafficking. Traffic 1, 248-258 (2000).
    • (2000) Traffic , vol.1 , pp. 248-258
    • Babst, M.1    Odorizzi, G.2    Estepa, E.J.3    Emr, S.D.4
  • 35
    • 58149280810 scopus 로고    scopus 로고
    • In vitro budding of intralumenal vesicles into late endosomes is regulated by Alix and Tsg101
    • T. Falguières, P. P. Luyet, C. Bissig, C. C. Scott, M. C. Velluz, J. Gruenberg, In vitro budding of intralumenal vesicles into late endosomes is regulated by Alix and Tsg101. Mol. Biol. Cell 19, 4942-4955 (2008).
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4942-4955
    • Falguières, T.1    Luyet, P.P.2    Bissig, C.3    Scott, C.C.4    Velluz, M.C.5    Gruenberg, J.6
  • 36
    • 2342423251 scopus 로고    scopus 로고
    • ATPase-deficient hVPS4 impairs formation of internal endosomal vesicles and stabilizes bilayered clathrin coats on endosomal vacuoles
    • M. Sachse, G. J. Strous, J. Klumperman, ATPase-deficient hVPS4 impairs formation of internal endosomal vesicles and stabilizes bilayered clathrin coats on endosomal vacuoles. J. Cell Sci. 117, 1699-1708 (2004).
    • (2004) J. Cell Sci. , vol.117 , pp. 1699-1708
    • Sachse, M.1    Strous, G.J.2    Klumperman, J.3
  • 37
    • 77953379422 scopus 로고    scopus 로고
    • Cell-free reconstitution of multivesicular body formation and receptor sorting
    • W. Sun, T. A. Vida, N. Sirisaengtaksin, S. A. Merrill, P. I. Hanson, A. J. Bean, Cell-free reconstitution of multivesicular body formation and receptor sorting. Traffic 11, 867-876 (2010).
    • (2010) Traffic , vol.11 , pp. 867-876
    • Sun, W.1    Vida, T.A.2    Sirisaengtaksin, N.3    Merrill, S.A.4    Hanson, P.I.5    Bean, A.J.6
  • 40
    • 33746092492 scopus 로고    scopus 로고
    • Flat clathrin coats on endosomes mediate degradative protein sorting by scaffolding Hrs in dynamic microdomains
    • C. Raiborg, J. Wesche, L. Malerød, H. Stenmark, Flat clathrin coats on endosomes mediate degradative protein sorting by scaffolding Hrs in dynamic microdomains. J. Cell Sci. 119, 2414-2424 (2006).
    • (2006) J. Cell Sci. , vol.119 , pp. 2414-2424
    • Raiborg, C.1    Wesche, J.2    Malerød, L.3    Stenmark, H.4
  • 41
    • 77956880594 scopus 로고    scopus 로고
    • A Dyn2-CIN85 complex mediates degradative traffic of the EGFR by regulation of late endosomal budding
    • B. Schroeder, S. G. Weller, J. Chen, D. Billadeau, M. A. McNiven, A Dyn2-CIN85 complex mediates degradative traffic of the EGFR by regulation of late endosomal budding. EMBO J. 29, 3039-3053 (2010).
    • (2010) EMBO J. , vol.29 , pp. 3039-3053
    • Schroeder, B.1    Weller, S.G.2    Chen, J.3    Billadeau, D.4    McNiven, M.A.5


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