메뉴 건너뛰기




Volumn 297, Issue 2, 2004, Pages 380-391

A role for Hrs in endosomal sorting of ligand-stimulated and unstimulated epidermal growth factor receptor

Author keywords

Early endosome; EGF receptor; Endosomal sorting; FYVE domain; Hrs

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR; HEPATOCYTE GROWTH FACTOR REGULATED TYROSINE KINASE SUBSTRATE; PROTEIN TYROSINE KINASE; UNCLASSIFIED DRUG;

EID: 2942736876     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2004.03.038     Document Type: Article
Times cited : (34)

References (43)
  • 1
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinase
    • Schlessinger J. Cell signaling by receptor tyrosine kinase. Cell. 103:2000;211-225
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 2
    • 2142713199 scopus 로고    scopus 로고
    • Endocytosis and intracellular sorting of receptor tyrosine kinases
    • Sorkin A. Endocytosis and intracellular sorting of receptor tyrosine kinases. Front. Biosci. 3:1998;729-738
    • (1998) Front. Biosci. , vol.3 , pp. 729-738
    • Sorkin, A.1
  • 3
    • 0030846562 scopus 로고    scopus 로고
    • Hrs, a tyrosine kinase substrate with a conserved double zinc finger domain, is localized to the cytoplasmic surface of early endosomes
    • Komada M., Masaki R., Yamamoto A., Kitamura N. Hrs, a tyrosine kinase substrate with a conserved double zinc finger domain, is localized to the cytoplasmic surface of early endosomes. J. Biol. Chem. 272:1997;20538-20544
    • (1997) J. Biol. Chem. , vol.272 , pp. 20538-20544
    • Komada, M.1    Masaki, R.2    Yamamoto, A.3    Kitamura, N.4
  • 4
    • 0034805184 scopus 로고    scopus 로고
    • Hrs and Hbp: Possible regulators of endocytosis and exocytosis
    • Komada M., Kitamura N. Hrs and Hbp: possible regulators of endocytosis and exocytosis. Biochem. Biophys. Res. Commun. 281:2001;1065-1069
    • (2001) Biochem. Biophys. Res. Commun. , vol.281 , pp. 1065-1069
    • Komada, M.1    Kitamura, N.2
  • 5
    • 0028849793 scopus 로고
    • Growth factor-induced tyrosine phosphorylation of Hrs, a novel 115-kilodalton protein with a structurally conserved putative zinc finger domain
    • Komada M., Kitamura N. Growth factor-induced tyrosine phosphorylation of Hrs, a novel 115-kilodalton protein with a structurally conserved putative zinc finger domain. Mol. Cell. Biol. 15:1995;6213-6221
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6213-6221
    • Komada, M.1    Kitamura, N.2
  • 6
    • 0035831517 scopus 로고    scopus 로고
    • Hrs interacts with sorting nexin 1 and regulates degradation of epidermal growth factor receptor
    • Chin L.-S., Raynor M.C., Wei X., Chen H.-Q., Li L. Hrs interacts with sorting nexin 1 and regulates degradation of epidermal growth factor receptor. J. Biol. Chem. 276:2001;7069-7078
    • (2001) J. Biol. Chem. , vol.276 , pp. 7069-7078
    • Chin, L.-S.1    Raynor, M.C.2    Wei, X.3    Chen, H.-Q.4    Li, L.5
  • 8
    • 0036544559 scopus 로고    scopus 로고
    • Mammalian class e vps proteins recognize ubiquitin and act in the removal of endosomal protein-ubiquitin conjugates
    • Bishop N., Horman A., Woodman P. Mammalian class E vps proteins recognize ubiquitin and act in the removal of endosomal protein-ubiquitin conjugates. J. Cell Biol. 157:2002;91-101
    • (2002) J. Cell Biol. , vol.157 , pp. 91-101
    • Bishop, N.1    Horman, A.2    Woodman, P.3
  • 9
    • 0033982368 scopus 로고    scopus 로고
    • A Hrs binding protein having a Src homology 3 domain is involved in intracellular degradation of growth factors and their receptors
    • Takata H., Kato M., Denda K., Kitamura N. A Hrs binding protein having a Src homology 3 domain is involved in intracellular degradation of growth factors and their receptors. Genes Cells. 5:2000;57-69
    • (2000) Genes Cells , vol.5 , pp. 57-69
    • Takata, H.1    Kato, M.2    Denda, K.3    Kitamura, N.4
  • 11
    • 0029762883 scopus 로고    scopus 로고
    • Enhanced degradation of EGF receptors by a sorting nexin, SNX1
    • Kurten R.C., Cadena D.L., Gill G.L. Enhanced degradation of EGF receptors by a sorting nexin, SNX1. Science. 272:1996;1008-1010
    • (1996) Science , vol.272 , pp. 1008-1010
    • Kurten, R.C.1    Cadena, D.L.2    Gill, G.L.3
  • 13
    • 0037169336 scopus 로고    scopus 로고
    • Hrs regulates endosome membrane invagination and tyrosine kinase receptor signaling in Drosophila
    • Lloyd T.E., Atkinson R., Wu M.N., Zhou Y., Pennetta G., Bellen H. Hrs regulates endosome membrane invagination and tyrosine kinase receptor signaling in Drosophila. Cell. 108:2002;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.6
  • 14
    • 0038323973 scopus 로고    scopus 로고
    • STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes
    • Bache K.G., Raiborg C., Mehlum A., Stenmark H. STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes. J. Biol. Chem. 278:2003;12513-12521
    • (2003) J. Biol. Chem. , vol.278 , pp. 12513-12521
    • Bache, K.G.1    Raiborg, C.2    Mehlum, A.3    Stenmark, H.4
  • 17
    • 0029024442 scopus 로고
    • Novel PI(4)P 5-kinase homologue, Fab1p, essential for normal vacuole function and morphology in yeast
    • Yamamoto A., DeWald D.B., Boronenkov I.V., Anderson R.V., Emr S.D., Koshland D. Novel PI(4)P 5-kinase homologue, Fab1p, essential for normal vacuole function and morphology in yeast. Mol. Biol. Cell. 6:1995;525-539
    • (1995) Mol. Biol. Cell , vol.6 , pp. 525-539
    • Yamamoto, A.1    Dewald, D.B.2    Boronenkov, I.V.3    Anderson, R.V.4    Emr, S.D.5    Koshland, D.6
  • 18
    • 0028800173 scopus 로고
    • VPS27 controls vacuolar and endocytic traffic through a prevacuolar compartment in Saccharomyces cerevisiae
    • Piper R.C., Cooper A.A., Yang H., Stevens T.H. VPS27 controls vacuolar and endocytic traffic through a prevacuolar compartment in Saccharomyces cerevisiae. J. Cell Biol. 131:1995;603-617
    • (1995) J. Cell Biol. , vol.131 , pp. 603-617
    • Piper, R.C.1    Cooper, A.A.2    Yang, H.3    Stevens, T.H.4
  • 19
    • 0026544213 scopus 로고
    • Molecular characterization of VAC1, a gene required for vacuole inheritance and vacuole protein sorting
    • Weisman L.S., Wickner W. Molecular characterization of VAC1, a gene required for vacuole inheritance and vacuole protein sorting. J. Biol. Chem. 267:1992;618-623
    • (1992) J. Biol. Chem. , vol.267 , pp. 618-623
    • Weisman, L.S.1    Wickner, W.2
  • 20
    • 0030918921 scopus 로고    scopus 로고
    • Pep7p provides a novel protein that functions in vesicle-mediated transport between the yeast Golgi and endosome
    • Webb G.C., Zhang J., Garlow S.J., Wesp A., Riezman H., Jones E.W. Pep7p provides a novel protein that functions in vesicle-mediated transport between the yeast Golgi and endosome. Mol. Biol. Cell. 8:1997;871-895
    • (1997) Mol. Biol. Cell , vol.8 , pp. 871-895
    • Webb, G.C.1    Zhang, J.2    Garlow, S.J.3    Wesp, A.4    Riezman, H.5    Jones, E.W.6
  • 21
    • 0032111444 scopus 로고    scopus 로고
    • Phosphatidylinositol(3)-phosphate signaling mediated by specific binding to RING FYVE domains
    • Burd C.G., Emr S.D. Phosphatidylinositol(3)-phosphate signaling mediated by specific binding to RING FYVE domains. Mol. Cell. 2:1998;157-162
    • (1998) Mol. Cell , vol.2 , pp. 157-162
    • Burd, C.G.1    Emr, S.D.2
  • 25
    • 0034703046 scopus 로고    scopus 로고
    • Early endosomal localization of Hrs requires a sequence within the proline- and glutamine-rich region but not the FYVE finger
    • Hayakawa A., Kitamura N. Early endosomal localization of Hrs requires a sequence within the proline- and glutamine-rich region but not the FYVE finger. J. Biol. Chem. 275:2000;29636-29642
    • (2000) J. Biol. Chem. , vol.275 , pp. 29636-29642
    • Hayakawa, A.1    Kitamura, N.2
  • 26
    • 0027264590 scopus 로고
    • The cell dissociation and motility triggered by scatter factor/hepatocyte growth factor are mediated through the cytoplasmic domain of the c-Met receptor
    • Komada M., Kitamura N. The cell dissociation and motility triggered by scatter factor/hepatocyte growth factor are mediated through the cytoplasmic domain of the c-Met receptor. Oncogene. 8:1993;2381-2390
    • (1993) Oncogene , vol.8 , pp. 2381-2390
    • Komada, M.1    Kitamura, N.2
  • 27
    • 0141744750 scopus 로고    scopus 로고
    • STAM proteins bind ubiquitinated proteins on the early endosome via the VHS domain and ubiquitin-interacting motif
    • Mizuno E., Kawahata K., Kato M., Kitamura N., Komada M. STAM proteins bind ubiquitinated proteins on the early endosome via the VHS domain and ubiquitin-interacting motif. Mol. Biol. Cell. 14:2003;3675-3689
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3675-3689
    • Mizuno, E.1    Kawahata, K.2    Kato, M.3    Kitamura, N.4    Komada, M.5
  • 28
    • 0034097137 scopus 로고    scopus 로고
    • Syntaxin 7 mediates endocytic trafficking to late endosomes
    • Nakamura N., Yamamoto A., Wada Y., Futai M. Syntaxin 7 mediates endocytic trafficking to late endosomes. J. Biol. Chem. 275:2000;6523-6529
    • (2000) J. Biol. Chem. , vol.275 , pp. 6523-6529
    • Nakamura, N.1    Yamamoto, A.2    Wada, Y.3    Futai, M.4
  • 30
    • 0032516818 scopus 로고    scopus 로고
    • EAST, an epidermal growth factor receptor- and Eps15-associated protein with Src homology 3 and tyrosine-based activation motif domains
    • Lohi O., Poussu A., Meriläinen J., Kellokumpu S., Wasenius V.-M., Lehto V.-P. EAST, an epidermal growth factor receptor- and Eps15-associated protein with Src homology 3 and tyrosine-based activation motif domains. J. Biol. Chem. 273:1998;21408-21415
    • (1998) J. Biol. Chem. , vol.273 , pp. 21408-21415
    • Lohi, O.1    Poussu, A.2    Meriläinen, J.3    Kellokumpu, S.4    Wasenius, V.-M.5    Lehto, V.-P.6
  • 31
    • 18544383164 scopus 로고    scopus 로고
    • Ligand-independent degradation of epidermal growth factor receptor involves receptor ubiquitylation and Hgs, an adaptor whose ubiquitin-interacting motif targets ubiquitylation by Nedd4
    • Katz M., Shtiegman K., Tal-Or P., Yakir L., Mosesson Y., Harari D., Machluf Y., Asao H., Jovin T., Sugamura K., Yarden Y. Ligand-independent degradation of epidermal growth factor receptor involves receptor ubiquitylation and Hgs, an adaptor whose ubiquitin-interacting motif targets ubiquitylation by Nedd4. Traffic. 3:2002;740-751
    • (2002) Traffic , vol.3 , pp. 740-751
    • Katz, M.1    Shtiegman, K.2    Tal-Or, P.3    Yakir, L.4    Mosesson, Y.5    Harari, D.6    MacHluf, Y.7    Asao, H.8    Jovin, T.9    Sugamura, K.10    Yarden, Y.11
  • 32
    • 0035316576 scopus 로고    scopus 로고
    • Cb1: Many adaptations to regulate protein tyrosine kinases
    • Thien C.B., Langdon W.Y. Cb1: many adaptations to regulate protein tyrosine kinases. Nat. Rev., Mol. Cell Biol. 2:2001;294-307
    • (2001) Nat. Rev., Mol. Cell Biol. , vol.2 , pp. 294-307
    • Thien, C.B.1    Langdon, W.Y.2
  • 33
    • 0035856472 scopus 로고    scopus 로고
    • Membrane transport: Ubiquitylation in endosomal sorting
    • Dupre S., Volland C., Haguenauer-Tsapis R. Membrane transport: ubiquitylation in endosomal sorting. Curr. Biol. 11:2001;R932-R934
    • (2001) Curr. Biol. , vol.11
    • Dupre, S.1    Volland, C.2    Haguenauer-Tsapis, R.3
  • 35
    • 0037187597 scopus 로고    scopus 로고
    • Fiore, a single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins
    • Polo S., Sigismund S., Faretta M., Guidi M., Capua M.R., Bossi G., Chen H., Camilli P.D., Di P.P. Fiore, A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins. Nature. 416:2002;451-455
    • (2002) Nature , vol.416 , pp. 451-455
    • Polo, S.1    Sigismund, S.2    Faretta, M.3    Guidi, M.4    Capua, M.R.5    Bossi, G.6    Chen, H.7    Camilli, P.D.8    Di, P.P.9
  • 36
    • 0035958546 scopus 로고    scopus 로고
    • Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I
    • Katzmann D.J., Babst M., Emr S.D. Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I. Cell. 106:2001;145-155
    • (2001) Cell , vol.106 , pp. 145-155
    • Katzmann, D.J.1    Babst, M.2    Emr, S.D.3
  • 37
    • 0034157875 scopus 로고    scopus 로고
    • Mammalian tumor susceptibility gene 101 (TSG101) and the yeast homologue, Vps23p, both function in late endosomal trafficking
    • Babst M., Odorizzi G., Estepa E.J., Emr S.D. Mammalian tumor susceptibility gene 101 (TSG101) and the yeast homologue, Vps23p, both function in late endosomal trafficking. Traffic. 1:2000;248-258
    • (2000) Traffic , vol.1 , pp. 248-258
    • Babst, M.1    Odorizzi, G.2    Estepa, E.J.3    Emr, S.D.4
  • 38
    • 0037008677 scopus 로고    scopus 로고
    • Huntingtin-associated protein 1 interacts with hepatocyte growth factor-regulated tyrosine kinase substrate and functions in endosomal trafficking
    • Li Y., Chin L.-S., Levey A.I., Li L. Huntingtin-associated protein 1 interacts with hepatocyte growth factor-regulated tyrosine kinase substrate and functions in endosomal trafficking. J. Biol. Chem. 277:2002;28212-28221
    • (2002) J. Biol. Chem. , vol.277 , pp. 28212-28221
    • Li, Y.1    Chin, L.-S.2    Levey, A.I.3    Li, L.4
  • 42
    • 0035369692 scopus 로고    scopus 로고
    • Binding of GGA2 to the lysosomal enzyme sorting motif of the mannose 6-phosphate receptor
    • Zhu Y., Doray B., Poussu A., Lehto V.-P., Kornfeld S. Binding of GGA2 to the lysosomal enzyme sorting motif of the mannose 6-phosphate receptor. Science. 292:2001;1716-17108
    • (2001) Science , vol.292 , pp. 1716-17108
    • Zhu, Y.1    Doray, B.2    Poussu, A.3    Lehto, V.-P.4    Kornfeld, S.5
  • 43
    • 0035958856 scopus 로고    scopus 로고
    • Golgi-localizing, γ-adaptin ear homology domain, ADP-ribosylation factor-binding (GGA) proteins interact with acidic dileucine sequences within the cytoplasmic domains of sorting receptors through their Vps27p/Hrs/STAM (VHS) domains
    • Takatsu H., Katoh Y., Shiba Y., Nakayama K. Golgi-localizing, γ-adaptin ear homology domain, ADP-ribosylation factor-binding (GGA) proteins interact with acidic dileucine sequences within the cytoplasmic domains of sorting receptors through their Vps27p/Hrs/STAM (VHS) domains. J. Biol. Chem. 276:2001;28541-28545
    • (2001) J. Biol. Chem. , vol.276 , pp. 28541-28545
    • Takatsu, H.1    Katoh, Y.2    Shiba, Y.3    Nakayama, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.