메뉴 건너뛰기




Volumn 5, Issue 5, 2013, Pages

Endocytosis of receptor tyrosine kinases

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN TYROSINE KINASE;

EID: 84877103013     PISSN: None     EISSN: 19430264     Source Type: Journal    
DOI: 10.1101/cshperspect.a017459     Document Type: Article
Times cited : (358)

References (156)
  • 1
    • 67349237981 scopus 로고    scopus 로고
    • Ubiquitin in trafficking: The network at work
    • Acconcia F., Sigismund S, Polo S. 2009. Ubiquitin in trafficking: The network at work. Exp Cell Res 315: 1610-1618.
    • (2009) Exp Cell Res , vol.315 , pp. 1610-1618
    • Acconcia, F.1    Sigismund, S.2    Polo, S.3
  • 2
    • 64549154396 scopus 로고    scopus 로고
    • Diversity of polyubiquitin chains
    • Adhikari A., Chen ZJ. 2009. Diversity of polyubiquitin chains. Dev Cell 16: 485-486.
    • (2009) Dev Cell , vol.16 , pp. 485-486
    • Adhikari, A.1    Chen, Z.J.2
  • 3
    • 33646396185 scopus 로고    scopus 로고
    • Cell survival through Trk neurotrophin receptors is differentially regulated by ubiquitination
    • Arevalo J.C., Waite J, Rajagopal R, Beyna M, Chen ZY, Lee FS, Chao MV. 2006. Cell survival through Trk neurotrophin receptors is differentially regulated by ubiquitination. Neuron 50: 549-559.
    • (2006) Neuron , vol.50 , pp. 549-559
    • Arevalo, J.C.1    Waite, J.2    Rajagopal, R.3    Beyna, M.4    Chen, Z.Y.5    Lee, F.S.6    Chao, M.V.7
  • 4
    • 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. 2003. STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes. J Biol Chem 278: 12513-12521.
    • (2003) J Biol Chem , vol.278 , pp. 12513-12521
    • Bache, K.G.1    Raiborg, C.2    Mehlum, A.3    Stenmark, H.4
  • 5
    • 0026343342 scopus 로고
    • Insulin receptors internalize by a rapid, saturable pathway requiring receptor autophosphorylation and an intact juxtamembrane region
    • Backer J.M., Shoelson SE, Haring E, White MF. 1991. Insulin receptors internalize by a rapid, saturable pathway requiring receptor autophosphorylation and an intact juxtamembrane region. J Cell Biol 115: 1535-1545.
    • (1991) J Cell Biol , vol.115 , pp. 1535-1545
    • Backer, J.M.1    Shoelson, S.E.2    Haring, E.3    White, M.F.4
  • 7
    • 0034714277 scopus 로고    scopus 로고
    • Threonine phosphorylation diverts internalized epidermal growth factor receptors from a degradative pathway to the recycling endosome
    • Bao J., Alroy I, Waterman H, Schejter ED, Brodie C, Gruenberg J., Yarden Y. 2000. Threonine phosphorylation diverts internalized epidermal growth factor receptors from a degradative pathway to the recycling endosome. J Biol Chem 275: 26178-26186.
    • (2000) J Biol Chem , vol.275 , pp. 26178-26186
    • Bao, J.1    Alroy, I.2    Waterman, H.3    Schejter, E.D.4    Brodie, C.5    Gruenberg, J.6    Yarden, Y.7
  • 8
    • 0037418192 scopus 로고    scopus 로고
    • Src promotes destruction of c-Cbl: Implications for oncogenic synergy between Src and growth factor receptors
    • Bao J., Gur G, Yarden Y. 2003. Src promotes destruction of c-Cbl: Implications for oncogenic synergy between Src and growth factor receptors. Proc Natl Acad Sci 100: 2438-2443.
    • (2003) Proc Natl Acad Sci , vol.100 , pp. 2438-2443
    • Bao, J.1    Gur, G.2    Yarden, Y.3
  • 10
    • 0028040812 scopus 로고
    • Hierarchy of binding sites for Grb2 and Shc on the epidermal growth factor receptor
    • Batzer A.G., Rotin D, Urena JM, Skolnik EY, Schlessinger J. 1994. Hierarchy of binding sites for Grb2 and Shc on the epidermal growth factor receptor. Mol Cell Biol 14: 5192-5201.
    • (1994) Mol Cell Biol , vol.14 , pp. 5192-5201
    • Batzer, A.G.1    Rotin, D.2    Urena, J.M.3    Skolnik, E.Y.4    Schlessinger, J.5
  • 11
    • 0034307565 scopus 로고    scopus 로고
    • NGF signals through TrkA to increase clathrin at the plasma membrane and enhance clathrin-mediated membrane trafficking
    • Beattie E.C., Howe CL, Wilde A, Brodsky FM, Mobley WC. 2000. NGF signals through TrkA to increase clathrin at the plasma membrane and enhance clathrin-mediated membrane trafficking. J Neurosci 20: 7325-7333.
    • (2000) J Neurosci , vol.20 , pp. 7325-7333
    • Beattie, E.C.1    Howe, C.L.2    Wilde, A.3    Brodsky, F.M.4    Mobley, W.C.5
  • 12
    • 0041654309 scopus 로고
    • Down-regulation of the epidermal growth factor receptor in KB cells is due to receptor internalization and subsequent degradation in lysosomes
    • Beguinot L., Lyall RM, Willingham MC, Pastan I. 1984. Down-regulation of the epidermal growth factor receptor in KB cells is due to receptor internalization and subsequent degradation in lysosomes. Proc Natl Acad Sci 81: 2384-2388.
    • (1984) Proc Natl Acad Sci , vol.81 , pp. 2384-2388
    • Beguinot, L.1    Lyall, R.M.2    Willingham, M.C.3    Pastan, I.4
  • 13
    • 67349256390 scopus 로고    scopus 로고
    • Hrs regulates the endocytic sorting of the fibroblast growth factor receptor 2b
    • Belleudi F., Leone L, Maggio M, Torrisi MR. 2009. Hrs regulates the endocytic sorting of the fibroblast growth factor receptor 2b. Exp Cell Res 315: 2181-2191.
    • (2009) Exp Cell Res , vol.315 , pp. 2181-2191
    • Belleudi, F.1    Leone, L.2    Maggio, M.3    Torrisi, M.R.4
  • 14
    • 70349258220 scopus 로고    scopus 로고
    • Oligomerized Tie2 localizes to clathrin-coated pits in response to angiopoietin-1
    • Bogdanovic E., Coombs N, Dumont DJ. 2009. Oligomerized Tie2 localizes to clathrin-coated pits in response to angiopoietin-1. Histochem Cell Biol 132: 225-237.
    • (2009) Histochem Cell Biol , vol.132 , pp. 225-237
    • Bogdanovic, E.1    Coombs, N.2    Dumont, D.J.3
  • 16
    • 33646171781 scopus 로고    scopus 로고
    • Degradation of endocytosed epidermal growth factor and virally ubiquitinated major histocompatibility complex class I is independent of mammalian ESCRTII
    • Bowers K., Piper SC, Edeling MA, Gray SR, Owen DJ, Lehner P.J., Luzio JP. 2006. Degradation of endocytosed epidermal growth factor and virally ubiquitinated major histocompatibility complex class I is independent of mammalian ESCRTII. J Biol Chem 281: 5094-5105.
    • (2006) J Biol Chem , vol.281 , pp. 5094-5105
    • Bowers, K.1    Piper, S.C.2    Edeling, M.A.3    Gray, S.R.4    Owen, D.J.5    Lehner, P.J.6    Luzio, J.P.7
  • 18
    • 0032789613 scopus 로고    scopus 로고
    • Human mammary epithelial cells rapidly exchange empty EGFR between surface and intracellular pools
    • Burke P.M., Wiley HS. 1999. Human mammary epithelial cells rapidly exchange empty EGFR between surface and intracellular pools. J Cell Physiol 180: 448-460.
    • (1999) J Cell Physiol , vol.180 , pp. 448-460
    • Burke, P.M.1    Wiley, H.S.2
  • 19
    • 33947245587 scopus 로고    scopus 로고
    • Neuregulin-induced ErbB3 downregulation is mediated by a protein stability cascade involving the E3 ubiquitin ligase Nrdp1
    • Cao Z., Wu X, Yen L, Sweeney C, Carraway KL 3rd. 2007. Neuregulin-induced ErbB3 downregulation is mediated by a protein stability cascade involving the E3 ubiquitin ligase Nrdp1. Mol Cell Biol 27: 2180-2188.
    • (2007) Mol Cell Biol , vol.27 , pp. 2180-2188
    • Cao, Z.1    Wu, X.2    Yen, L.3    Sweeney, C.4    Carraway III, K.L.5
  • 21
    • 0020335070 scopus 로고
    • Co-localization of 125I-epidermal growth factor and ferritin-low density lipoprotein in coated pits: A quantitative electron microscopic study in normal and mutant human fibroblasts
    • Carpentier J.L., Gorden P, Anderson RG, Goldstein JL, Brown M.S., Cohen S, Orci L. 1982. Co-localization of 125I-epidermal growth factor and ferritin-low density lipoprotein in coated pits: A quantitative electron microscopic study in normal and mutant human fibroblasts. J Cell Biol 95: 73-77.
    • (1982) J Cell Biol , vol.95 , pp. 73-77
    • Carpentier, J.L.1    Gorden, P.2    Anderson, R.G.3    Goldstein, J.L.4    Brown, M.S.5    Cohen, S.6    Orci, L.7
  • 22
    • 0025250145 scopus 로고
    • NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor
    • Chen W.J., Goldstein JL, Brown MS. 1990. NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor. J Biol Chem 265: 3116-3123.
    • (1990) J Biol Chem , vol.265 , pp. 3116-3123
    • Chen, W.J.1    Goldstein, J.L.2    Brown, M.S.3
  • 23
    • 69549086892 scopus 로고    scopus 로고
    • Embryonic arrest at midgestation and disruption of Notch signaling produced by the absence of both epsin 1 and epsin 2 in mice
    • Chen H., Ko G, Zatti A, Di Giacomo G, Liu L, Raiteri E, Perucco E., Collesi C, Min W, Zeiss C, et al. 2009. Embryonic arrest at midgestation and disruption of Notch signaling produced by the absence of both epsin 1 and epsin 2 in mice. Proc Natl Acad Sci 106: 13838-13843.
    • (2009) Proc Natl Acad Sci , vol.106 , pp. 13838-13843
    • Chen, H.1    Ko, G.2    Zatti, A.3    Di Giacomo, G.4    Liu, L.5    Raiteri, E.6    Perucco, E.7    Collesi, C.8    Min, W.9    Zeiss, C.10
  • 26
    • 0034949705 scopus 로고    scopus 로고
    • c-Cbl ubiquitinates the EGF receptor at the plasma membrane and remains receptor associated throughout the endocytic route
    • de Melker AA, van der Horst G, Calafat J, Jansen H, Borst J. 2001. 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) 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
  • 27
    • 34547764975 scopus 로고    scopus 로고
    • Malfunctions within the Cbl interactome uncouple receptor tyrosine kinases from destructive transport
    • Dikic I., Schmidt MH. 2007. Malfunctions within the Cbl interactome uncouple receptor tyrosine kinases from destructive transport. Eur J Cell Biol 86: 505-512.
    • (2007) Eur J Cell Biol , vol.86 , pp. 505-512
    • Dikic, I.1    Schmidt, M.H.2
  • 28
    • 0038165451 scopus 로고    scopus 로고
    • Vascular endothelial growth factor-dependent down-regulation of Flk-1/KDR involves Cbl-mediated ubiquitination. Consequences on nitric oxide production from endothelial cells
    • Duval M., Bedard-Goulet S, Delisle C, Gratton JP. 2003. Vascular endothelial growth factor-dependent down-regulation of Flk-1/KDR involves Cbl-mediated ubiquitination. Consequences on nitric oxide production from endothelial cells. J Biol Chem 278: 20091-20097.
    • (2003) J Biol Chem , vol.278 , pp. 20091-20097
    • Duval, M.1    Bedard-Goulet, S.2    Delisle, C.3    Gratton, J.P.4
  • 29
    • 77649274212 scopus 로고    scopus 로고
    • Membrane contacts between endosomes and ER provide sites for PTP1B-epidermal growth factor receptor interaction
    • Eden E.R., White IJ, Tsapara A, Futter CE. 2010. Membrane contacts between endosomes and ER provide sites for PTP1B-epidermal growth factor receptor interaction. Nat Cell Biol 12: 267-272.
    • (2010) Nat Cell Biol , vol.12 , pp. 267-272
    • Eden, E.R.1    White, I.J.2    Tsapara, A.3    Futter, C.E.4
  • 30
    • 84855979997 scopus 로고    scopus 로고
    • The role of EGF receptor ubiquitination in regulating its intracellular traffic
    • Eden E.R., Huang F, Sorkin A, Futter CE. 2011. The role of EGF receptor ubiquitination in regulating its intracellular traffic. Traffic 13: 329-337.
    • (2011) Traffic , vol.13 , pp. 329-337
    • Eden, E.R.1    Huang, F.2    Sorkin, A.3    Futter, C.E.4
  • 31
    • 33746936677 scopus 로고    scopus 로고
    • Intrinsic tyrosine kinase activity is required for vascular endothelial growth factor receptor 2 ubiquitination, sorting and degradation in endothelial cells
    • Ewan L.C., Jopling HM, Jia H, Mittar S, Bagherzadeh A, Howell G.J., Walker JH, Zachary IC, Ponnambalam S. 2006. Intrinsic tyrosine kinase activity is required for vascular endothelial growth factor receptor 2 ubiquitination, sorting and degradation in endothelial cells. Traffic 7: 1270-1282.
    • (2006) Traffic , vol.7 , pp. 1270-1282
    • Ewan, L.C.1    Jopling, H.M.2    Jia, H.3    Mittar, S.4    Bagherzadeh, A.5    Howell, G.J.6    Walker, J.H.7    Zachary, I.C.8    Ponnambalam, S.9
  • 32
    • 38149016260 scopus 로고    scopus 로고
    • Ligand binding induces Cbl-dependent EphB1 receptor degradation through the lysosomal pathway
    • Fasen K., Cerretti DP, Huynh-Do U. 2008. Ligand binding induces Cbl-dependent EphB1 receptor degradation through the lysosomal pathway. Traffic 9: 251-266.
    • (2008) Traffic , vol.9 , pp. 251-266
    • Fasen, K.1    Cerretti, D.P.2    Huynh-Do, U.3
  • 34
    • 0028224965 scopus 로고
    • Postendocytic trafficking of epidermal growth factor-receptor complexes is mediated through saturable and specific endosomal interactions
    • French A.R., Sudlow GP, Wiley HS, Lauffenburger DA. 1994. Postendocytic trafficking of epidermal growth factor-receptor complexes is mediated through saturable and specific endosomal interactions. J Biol Chem 269: 15749-15755.
    • (1994) J Biol Chem , vol.269 , pp. 15749-15755
    • French, A.R.1    Sudlow, G.P.2    Wiley, H.S.3    Lauffenburger, D.A.4
  • 35
    • 0028969961 scopus 로고
    • Intracellular trafficking of epidermal growth factor family ligands is directly influenced by the pH sensitivity of the receptor/ligand interaction
    • French A.R., Tadaki DK, Niyogi SK, Lauffenburger DA. 1995. 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) J Biol Chem , vol.270 , pp. 4334-4340
    • French, A.R.1    Tadaki, D.K.2    Niyogi, S.K.3    Lauffenburger, D.A.4
  • 37
    • 0029557613 scopus 로고
    • The epidermal growth factor receptor is covalently linked to ubiquitin
    • Galcheva-Gargova Z, Theroux SJ, Davis RJ. 1995. The epidermal growth factor receptor is covalently linked to ubiquitin. Oncogene 11: 2649-2655.
    • (1995) Oncogene , vol.11 , pp. 2649-2655
    • Galcheva-Gargova, Z.1    Theroux, S.J.2    Davis, R.J.3
  • 38
    • 26944484011 scopus 로고    scopus 로고
    • Lysine 63 polyubiquitination of the nerve growth factor receptor TrkA directs internalization and signaling
    • Geetha T., Jiang J, Wooten MW. 2005. Lysine 63 polyubiquitination of the nerve growth factor receptor TrkA directs internalization and signaling. Mol Cell 20: 301-312.
    • (2005) Mol Cell , vol.20 , pp. 301-312
    • Geetha, T.1    Jiang, J.2    Wooten, M.W.3
  • 39
    • 21644463635 scopus 로고    scopus 로고
    • β-Arrestin is crucial for ubiquitination and down-regulation of the insulin-like growth factor-1 receptor by acting as adaptor for the MDM2 E3 ligase
    • Girnita L., Shenoy SK, Sehat B, Vasilcanu R, Girnita A, Lefkowitz R.J., Larsson O. 2005. β-Arrestin is crucial for ubiquitination and down-regulation of the insulin-like growth factor-1 receptor by acting as adaptor for the MDM2 E3 ligase. J Biol Chem 280: 24412-24419.
    • (2005) J Biol Chem , vol.280 , pp. 24412-24419
    • Girnita, L.1    Shenoy, S.K.2    Sehat, B.3    Vasilcanu, R.4    Girnita, A.5    Lefkowitz, R.J.6    Larsson, O.7
  • 40
    • 77953167957 scopus 로고    scopus 로고
    • Multiple mechanisms collectively regulate clathrin-mediated endocytosis of the epidermal growth factor receptor
    • Goh L.K., Huang F, Kim W, Gygi S, Sorkin A. 2010. Multiple mechanisms collectively regulate clathrin-mediated endocytosis of the epidermal growth factor receptor. J Cell Biol 189: 871-883.
    • (2010) J Cell Biol , vol.189 , pp. 871-883
    • Goh, L.K.1    Huang, F.2    Kim, W.3    Gygi, S.4    Sorkin, A.5
  • 41
    • 0018166797 scopus 로고
    • Epidermal growth factor:Morphological demonstration of binding, internalization, and lysosomal association in human fibroblasts
    • Gorden P., Carpentier JL, Cohen S, Orci L. 1978. Epidermal growth factor:Morphological demonstration of binding, internalization, and lysosomal association in human fibroblasts. Proc Natl Acad Sci 75: 5025-5029.
    • (1978) Proc Natl Acad Sci , vol.75 , pp. 5025-5029
    • Gorden, P.1    Carpentier, J.L.2    Cohen, S.3    Orci, L.4
  • 42
    • 69249106881 scopus 로고    scopus 로고
    • Pathways and mechanisms of endocytic recycling
    • Grant B.D., Donaldson JG. 2009. Pathways and mechanisms of endocytic recycling. Nat Rev Mol Cell Biol 10: 597-608.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 597-608
    • Grant, B.D.1    Donaldson, J.G.2
  • 44
    • 0028079974 scopus 로고
    • Involvement of dileucine motifs in the internalization and degradation of the insulin receptor
    • Haft C.R., Klausner RD, Taylor SI. 1994. Involvement of dileucine motifs in the internalization and degradation of the insulin receptor. J Biol Chem 269: 26286-26294.
    • (1994) J Biol Chem , vol.269 , pp. 26286-26294
    • Haft, C.R.1    Klausner, R.D.2    Taylor, S.I.3
  • 45
    • 0018581544 scopus 로고
    • Rapid stimulation of pinocytosis in human carcinoma cells A-431 by epidermal growth factor
    • Haigler H.T., McKanna JA, Cohen S. 1979. Rapid stimulation of pinocytosis in human carcinoma cells A-431 by epidermal growth factor. J Cell Biol 83: 82-90.
    • (1979) J Cell Biol , vol.83 , pp. 82-90
    • Haigler, H.T.1    McKanna, J.A.2    Cohen, S.3
  • 48
    • 34047274090 scopus 로고    scopus 로고
    • A novel sorting sequence in the b2-adrenergic receptor switches recycling from default to the Hrs-dependent mechanism
    • Hanyaloglu A.C., von Zastrow M. 2007. A novel sorting sequence in the b2-adrenergic receptor switches recycling from default to the Hrs-dependent mechanism. J Biol Chem 282: 3095-3104.
    • (2007) J Biol Chem , vol.282 , pp. 3095-3104
    • Hanyaloglu, A.C.1    von Zastrow, M.2
  • 49
    • 54249152045 scopus 로고    scopus 로고
    • Ubiquitination of fibroblast growth factor receptor 1 is required for its intracellular sorting but not for its endocytosis
    • Haugsten E.M., Malecki J, Bjorklund SM, Olsnes S, Wesche J. 2008. Ubiquitination of fibroblast growth factor receptor 1 is required for its intracellular sorting but not for its endocytosis. Mol Biol Cell 19: 3390-3403.
    • (2008) Mol Biol Cell , vol.19 , pp. 3390-3403
    • Haugsten, E.M.1    Malecki, J.2    Bjorklund, S.M.3    Olsnes, S.4    Wesche, J.5
  • 52
    • 67449116833 scopus 로고    scopus 로고
    • Activation of protein kinase C a is necessary for sorting the PDGF β-receptor to Rab4a-dependent recycling
    • Hellberg C., Schmees C, Karlsson S, Ahgren A, Heldin CH. 2009. Activation of protein kinase C a is necessary for sorting the PDGF β-receptor to Rab4a-dependent recycling. Mol Biol Cell 20: 2856-2863.
    • (2009) Mol Biol Cell , vol.20 , pp. 2856-2863
    • Hellberg, C.1    Schmees, C.2    Karlsson, S.3    Ahgren, A.4    Heldin, C.H.5
  • 54
    • 1642422374 scopus 로고    scopus 로고
    • Association with membrane protrusions makes ErbB2 an internalization-resistant receptor
    • Hommelgaard A.M., Lerdrup M, van Deurs B. 2004. Association with membrane protrusions makes ErbB2 an internalization-resistant receptor. Mol Biol Cell 15: 1557-1567.
    • (2004) Mol Biol Cell , vol.15 , pp. 1557-1567
    • Hommelgaard, A.M.1    Lerdrup, M.2    van Deurs, B.3
  • 55
    • 0025281993 scopus 로고
    • Movement of internalized ligand-receptor complexes along a continuous endosomal reticulum
    • Hopkins C.R., Gibson A, Shipman M, Miller K. 1990. Movement of internalized ligand-receptor complexes along a continuous endosomal reticulum. Nature 346: 335-339.
    • (1990) Nature , vol.346 , pp. 335-339
    • Hopkins, C.R.1    Gibson, A.2    Shipman, M.3    Miller, K.4
  • 56
    • 14844334946 scopus 로고    scopus 로고
    • Grb2-mediated recruitment of the Cbl RING domain to the EGF receptor is essential and sufficient to support receptor endocytosis
    • Huang F., Sorkin A. 2005. Grb2-mediated recruitment of the Cbl RING domain to the EGF receptor is essential and sufficient to support receptor endocytosis. Mol Biol Cell 16: 1268-1281.
    • (2005) Mol Biol Cell , vol.16 , pp. 1268-1281
    • Huang, F.1    Sorkin, A.2
  • 57
    • 78650658024 scopus 로고    scopus 로고
    • Structural basis for the interaction between the growth factor-binding protein GRB10 and the E3 ubiquitin ligase NEDD4
    • Huang Q., Szebenyi DM. 2010. Structural basis for the interaction between the growth factor-binding protein GRB10 and the E3 ubiquitin ligase NEDD4. J Biol Chem 285: 42130-42139.
    • (2010) J Biol Chem , vol.285 , pp. 42130-42139
    • Huang, Q.1    Szebenyi, D.M.2
  • 58
    • 0242290315 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the b2 subunit of clathrin adaptor complex AP-2 reveals the role of a di-leucine motif in the epidermal growth factor receptor trafficking
    • Huang F., Jiang X, Sorkin A. 2003. Tyrosine phosphorylation of the b2 subunit of clathrin adaptor complex AP-2 reveals the role of a di-leucine motif in the epidermal growth factor receptor trafficking. J Biol Chem 278: 43411-43417.
    • (2003) J Biol Chem , vol.278 , pp. 43411-43417
    • Huang, F.1    Jiang, X.2    Sorkin, A.3
  • 59
    • 1942469322 scopus 로고    scopus 로고
    • Analysis of clathrin-mediated endocytosis of epidermal growth factor receptor by RNA interference
    • Huang F., Khvorova A, Marshall W, Sorkin A. 2004. Analysis of clathrin-mediated endocytosis of epidermal growth factor receptor by RNA interference. J Biol Chem 279: 16657-16661.
    • (2004) J Biol Chem , vol.279 , pp. 16657-16661
    • Huang, F.1    Khvorova, A.2    Marshall, W.3    Sorkin, A.4
  • 60
    • 33644852909 scopus 로고    scopus 로고
    • Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain
    • Huang F., Kirkpatrick D, Jiang X, Gygi S, Sorkin A. 2006. Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain. Mol Cell 21: 737-748.
    • (2006) Mol Cell , vol.21 , pp. 737-748
    • Huang, F.1    Kirkpatrick, D.2    Jiang, X.3    Gygi, S.4    Sorkin, A.5
  • 61
    • 0023035529 scopus 로고
    • Recycling of photoaffinity-labeled insulin receptors in rat adipocytes. Dissociation of insulin-receptor complexes is not required for receptor recycling
    • Huecksteadt T., Olefsky JM, Brandenberg D, Heidenreich KA. 1986. Recycling of photoaffinity-labeled insulin receptors in rat adipocytes. Dissociation of insulin-receptor complexes is not required for receptor recycling. J Biol Chem 261: 8655-8659.
    • (1986) J Biol Chem , vol.261 , pp. 8655-8659
    • Huecksteadt, T.1    Olefsky, J.M.2    Brandenberg, D.3    Heidenreich, K.A.4
  • 62
    • 0347093486 scopus 로고    scopus 로고
    • Hrs mediates downregulation of multiple signalling receptors in Drosophila
    • Jekely G., Rorth P. 2003. Hrs mediates downregulation of multiple signalling receptors in Drosophila. EMBO Rep 4: 1163-1168.
    • (2003) EMBO Rep , vol.4 , pp. 1163-1168
    • Jekely, G.1    Rorth, P.2
  • 63
    • 0042202634 scopus 로고    scopus 로고
    • Epidermal growth factor receptor internalization through clathrin-coated pits requires Cbl RING finger and proline-rich domains but not receptor polyubiquitylation
    • Jiang X., Sorkin A. 2003. Epidermal growth factor receptor internalization through clathrin-coated pits requires Cbl RING finger and proline-rich domains but not receptor polyubiquitylation. Traffic 4: 529-543.
    • (2003) Traffic , vol.4 , pp. 529-543
    • Jiang, X.1    Sorkin, A.2
  • 64
    • 0037339887 scopus 로고    scopus 로고
    • Grb2 regulates internalization of EGF receptors through clathrin-coated pits
    • Jiang X., Huang F, Marusyk A, Sorkin A. 2003. Grb2 regulates internalization of EGF receptors through clathrin-coated pits. Mol Biol Cell 14: 858-870.
    • (2003) Mol Biol Cell , vol.14 , pp. 858-870
    • Jiang, X.1    Huang, F.2    Marusyk, A.3    Sorkin, A.4
  • 65
    • 30644476941 scopus 로고    scopus 로고
    • Activation of the epidermal growth factor (EGF) receptor induces formation of EGF receptor-and Grb2-containing clathrin-coated pits
    • Johannessen L.E., Pedersen NM, Pedersen KW, Madshus IH, Stang E. 2006. Activation of the epidermal growth factor (EGF) receptor induces formation of EGF receptor-and Grb2-containing clathrin-coated pits. Mol Cell Biol 26: 389-401.
    • (2006) Mol Cell Biol , vol.26 , pp. 389-401
    • Johannessen, L.E.1    Pedersen, N.M.2    Pedersen, K.W.3    Madshus, I.H.4    Stang, E.5
  • 66
    • 79959720612 scopus 로고    scopus 로고
    • The VEGFR2 receptor tyrosine kinase undergoes constitutive endosome-to-plasma membrane recycling
    • Jopling H.M., Howell GJ, Gamper N, Ponnambalam S. 2011. The VEGFR2 receptor tyrosine kinase undergoes constitutive endosome-to-plasma membrane recycling. Biochem Biophys Res Commun 410: 170-176.
    • (2011) Biochem Biophys Res Commun , vol.410 , pp. 170-176
    • Jopling, H.M.1    Howell, G.J.2    Gamper, N.3    Ponnambalam, S.4
  • 69
    • 57749196168 scopus 로고    scopus 로고
    • A structural explanation for the binding of endocytic dileucine motifs by the AP2 complex
    • Kelly B.T., McCoy AJ, Spate K, Miller SE, Evans PR, Honing S, Owen DJ. 2008. A structural explanation for the binding of endocytic dileucine motifs by the AP2 complex. Nature 456: 976-979.
    • (2008) Nature , vol.456 , pp. 976-979
    • Kelly, B.T.1    McCoy, A.J.2    Spate, K.3    Miller, S.E.4    Evans, P.R.5    Honing, S.6    Owen, D.J.7
  • 71
    • 33747165872 scopus 로고    scopus 로고
    • Vascular endothelial cadherin controls VEGFR-2 internalization and signaling fromintracellular compartments
    • Lampugnani M.G., Orsenigo F, Gagliani MC, Tacchetti C, Dejana E. 2006. Vascular endothelial cadherin controls VEGFR-2 internalization and signaling fromintracellular compartments. J Cell Biol 174: 593-604.
    • (2006) J Cell Biol , vol.174 , pp. 593-604
    • Lampugnani, M.G.1    Orsenigo, F.2    Gagliani, M.C.3    Tacchetti, C.4    Dejana, E.5
  • 73
    • 9444280917 scopus 로고    scopus 로고
    • + exchanger regulatory factor stabilizes epidermal growth factor receptors at the cell surface
    • + exchanger regulatory factor stabilizes epidermal growth factor receptors at the cell surface. Mol Biol Cell 15: 5470-5480.
    • (2004) Mol Biol Cell , vol.15 , pp. 5470-5480
    • Lazar, C.S.1    Cresson, C.M.2    Lauffenburger, D.A.3    Gill, G.N.4
  • 74
    • 0033169024 scopus 로고    scopus 로고
    • The Cbl protooncoprotein stimulates CSF-1 receptor multiubiquitination and endocytosis, and attenuates macrophage proliferation
    • Lee P.S., Wang Y, Dominguez MG, Yeung YG, Murphy MA, Bowtell DD, Stanley ER. 1999. The Cbl protooncoprotein stimulates CSF-1 receptor multiubiquitination and endocytosis, and attenuates macrophage proliferation. EMBO J 18: 3616-3628.
    • (1999) EMBO J , vol.18 , pp. 3616-3628
    • Lee, P.S.1    Wang, Y.2    Dominguez, M.G.3    Yeung, Y.G.4    Murphy, M.A.5    Bowtell, D.D.6    Stanley, E.R.7
  • 76
    • 34447126344 scopus 로고    scopus 로고
    • Specific Grb2-mediated interactions regulate clathrin-dependent endocytosis of the cMet-tyrosine kinase
    • Li N., Lorinczi M, Ireton K, Elferink LA. 2007. Specific Grb2-mediated interactions regulate clathrin-dependent endocytosis of the cMet-tyrosine kinase. J Biol Chem 282: 16764-16775.
    • (2007) J Biol Chem , vol.282 , pp. 16764-16775
    • Li, N.1    Lorinczi, M.2    Ireton, K.3    Elferink, L.A.4
  • 77
    • 69249218913 scopus 로고    scopus 로고
    • WW domain containing E3 ubiquitin protein ligase 1 targets the fulllength ErbB4 for ubiquitin-mediated degradation in breast cancer
    • Li Y., Zhou Z, Alimandi M, Chen C. 2009. WW domain containing E3 ubiquitin protein ligase 1 targets the fulllength ErbB4 for ubiquitin-mediated degradation in breast cancer. Oncogene 28: 2948-2958.
    • (2009) Oncogene , vol.28 , pp. 2948-2958
    • Li, Y.1    Zhou, Z.2    Alimandi, M.3    Chen, C.4
  • 78
    • 70450225242 scopus 로고    scopus 로고
    • Participation of Tom1L1 in EGF-stimulated endocytosis of EGF receptor
    • Liu N.S., Loo LS, Loh E, Seet LF, Hong W. 2009. Participation of Tom1L1 in EGF-stimulated endocytosis of EGF receptor. EMBO J 28: 3485-3499.
    • (2009) EMBO J , vol.28 , pp. 3485-3499
    • Liu, N.S.1    Loo, L.S.2    Loh, E.3    Seet, L.F.4    Hong, W.5
  • 80
    • 82355171859 scopus 로고    scopus 로고
    • Poly-ubiquitination of the insulin-like growth factor I receptor (IGF-IR) activation loop promotes antibody-induced receptor internalization and down-regulation
    • Mao Y., Shang Y, Pham VC, Ernst JA, Lill JR, Scales SJ, Zha J. 2011. Poly-ubiquitination of the insulin-like growth factor I receptor (IGF-IR) activation loop promotes antibody-induced receptor internalization and down-regulation. J Biol Chem 286: 41852-41861.
    • (2011) J Biol Chem , vol.286 , pp. 41852-41861
    • Mao, Y.1    Shang, Y.2    Pham, V.C.3    Ernst, J.A.4    Lill, J.R.5    Scales, S.J.6    Zha, J.7
  • 81
    • 1842591231 scopus 로고    scopus 로고
    • Role of protein ubiquitylation in regulating endocytosis of receptor tyrosine kinases
    • Marmor MD, Yarden Y. 2004. Role of protein ubiquitylation in regulating endocytosis of receptor tyrosine kinases. Oncogene 23: 2057-2070.
    • (2004) Oncogene , vol.23 , pp. 2057-2070
    • Marmor, M.D.1    Yarden, Y.2
  • 82
    • 0027472437 scopus 로고
    • Consumption of EGF by A431 cells: Evidence for receptor recycling
    • Masui H., Castro L, Mendelsohn J. 1993. Consumption of EGF by A431 cells: Evidence for receptor recycling. J Cell Biol 120: 85-93.
    • (1993) J Cell Biol , vol.120 , pp. 85-93
    • Masui, H.1    Castro, L.2    Mendelsohn, J.3
  • 83
    • 0026744133 scopus 로고
    • Mechanism and role of insulin receptor endocytosis
    • McClain DA. 1992. Mechanism and role of insulin receptor endocytosis. Am J Med Sci 304: 192-201.
    • (1992) Am J Med Sci , vol.304 , pp. 192-201
    • McClain, D.A.1
  • 84
    • 4143080425 scopus 로고    scopus 로고
    • AMSH is an endosome-associated ubiquitin isopeptidase
    • McCullough J, Clague MJ, Urbe S. 2004. AMSH is an endosome-associated ubiquitin isopeptidase. J Cell Biol 166: 487-492.
    • (2004) J Cell Biol , vol.166 , pp. 487-492
    • McCullough, J.1    Clague, M.J.2    Urbe, S.3
  • 85
    • 30944464589 scopus 로고    scopus 로고
    • Activation of the endosomeassociated ubiquitin isopeptidase AMSH by STAM, a component of the multivesicular body-sorting machinery
    • McCullough J, Row PE, Lorenzo O, Doherty M, Beynon R, Clague M.J., Urbe S. 2006. Activation of the endosomeassociated ubiquitin isopeptidase AMSH by STAM, a component of the multivesicular body-sorting machinery. Curr Biol 16: 160-165.
    • (2006) Curr Biol , vol.16 , pp. 160-165
    • McCullough, J.1    Row, P.E.2    Lorenzo, O.3    Doherty, M.4    Beynon, R.5    Clague, M.J.6    Urbe, S.7
  • 86
    • 0022602283 scopus 로고
    • Localization of the epidermal growth factor (EGF) receptor within the endosome of EGF-stimulated epidermoid carcinoma (A431) cells
    • Miller K., Beardmore J, Kanety H, Schlessinger J, Hopkins CR. 1986. Localization of the epidermal growth factor (EGF) receptor within the endosome of EGF-stimulated epidermoid carcinoma (A431) cells. J Cell Biol 102: 500-509.
    • (1986) J Cell Biol , vol.102 , pp. 500-509
    • Miller, K.1    Beardmore, J.2    Kanety, H.3    Schlessinger, J.4    Hopkins, C.R.5
  • 87
    • 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: 30636-30643.
    • (1999) J Biol Chem , vol.274 , pp. 30636-30643
    • Mineo, C.1    Gill, G.N.2    Anderson, R.G.3
  • 88
    • 0033523010 scopus 로고    scopus 로고
    • Cbl-mediated negative regulation of platelet-derived growth factor receptor-dependent cell proliferation. A critical role for Cbl tyrosine kinase-binding domain
    • Miyake S., Mullane-Robinson KP, Lill NL, Douillard P, Band H. 1999. Cbl-mediated negative regulation of platelet-derived growth factor receptor-dependent cell proliferation. A critical role for Cbl tyrosine kinase-binding domain. J Biol Chem 274: 16619-16628.
    • (1999) J Biol Chem , vol.274 , pp. 16619-16628
    • Miyake, S.1    Mullane-Robinson, K.P.2    Lill, N.L.3    Douillard, P.4    Band, H.5
  • 89
    • 27644438783 scopus 로고    scopus 로고
    • Regulation of epidermal growth factor receptor down-regulation by UBPY-mediated deubiquitination at endosomes
    • Mizuno E., Iura T, Mukai A, Yoshimori T, Kitamura N, Komada M. 2005. Regulation of epidermal growth factor receptor down-regulation by UBPY-mediated deubiquitination at endosomes. Mol Biol Cell 16: 5163-5174.
    • (2005) Mol Biol Cell , vol.16 , pp. 5163-5174
    • Mizuno, E.1    Iura, T.2    Mukai, A.3    Yoshimori, T.4    Kitamura, N.5    Komada, M.6
  • 90
    • 33745754789 scopus 로고    scopus 로고
    • A deubiquitinating enzyme UBPY regulates the level of protein ubiquitination on endosomes
    • Mizuno E., Kobayashi K, Yamamoto A, Kitamura N, Komada M. 2006. A deubiquitinating enzyme UBPY regulates the level of protein ubiquitination on endosomes. Traffic 7: 1017-1031.
    • (2006) Traffic , vol.7 , pp. 1017-1031
    • Mizuno, E.1    Kobayashi, K.2    Yamamoto, A.3    Kitamura, N.4    Komada, M.5
  • 91
    • 46049089636 scopus 로고    scopus 로고
    • Grb10/Nedd4-mediated multiubiquitination of the insulin-like growth factor receptor regulates receptor internalization
    • Monami G., Emiliozzi V, Morrione A. 2008. Grb10/Nedd4-mediated multiubiquitination of the insulin-like growth factor receptor regulates receptor internalization. J Cell Physiol 216: 426-437.
    • (2008) J Cell Physiol , vol.216 , pp. 426-437
    • Monami, G.1    Emiliozzi, V.2    Morrione, A.3
  • 92
    • 0026664626 scopus 로고
    • Ligand-induced polyubiquitination of the platelet-derived growth factor β-receptor
    • Mori S., Heldin CH, Claesson-Welsh L. 1992. Ligand-induced polyubiquitination of the platelet-derived growth factor β-receptor. J Biol Chem 267: 6429-6434.
    • (1992) J Biol Chem , vol.267 , pp. 6429-6434
    • Mori, S.1    Heldin, C.H.2    Claesson-Welsh, L.3
  • 93
    • 0030462362 scopus 로고    scopus 로고
    • Mutation of Dileucine residues in the juxtamembrane region alters EGF receptor expression
    • Morrison P., Chung KC, Rosner MR. 1996. Mutation of Dileucine residues in the juxtamembrane region alters EGF receptor expression. Biochemistry 35: 14618-14624.
    • (1996) Biochemistry , vol.35 , pp. 14618-14624
    • Morrison, P.1    Chung, K.C.2    Rosner, M.R.3
  • 94
    • 0033522506 scopus 로고    scopus 로고
    • Inhibition of the receptor-binding function of clathrin adaptor protein AP-2 by dominant-negative mutant m2 subunit and its effects on endocytosis
    • Nesterov A., Carter RE, Sorkina T, Gill GN, Sorkin A. 1999. Inhibition of the receptor-binding function of clathrin adaptor protein AP-2 by dominant-negative mutant m2 subunit and its effects on endocytosis. EMBO J 18: 2489-2499.
    • (1999) EMBO J , vol.18 , pp. 2489-2499
    • Nesterov, A.1    Carter, R.E.2    Sorkina, T.3    Gill, G.N.4    Sorkin, A.5
  • 96
    • 33645741605 scopus 로고    scopus 로고
    • A novel endocytic mechanism of epidermal growth factor receptor sequestration and internalization
    • Orth J.D., Krueger EW, Weller SG, McNiven MA. 2006. A novel endocytic mechanism of epidermal growth factor receptor sequestration and internalization. Cancer Res 66: 3603-3610.
    • (2006) Cancer Res , vol.66 , pp. 3603-3610
    • Orth, J.D.1    Krueger, E.W.2    Weller, S.G.3    McNiven, M.A.4
  • 97
    • 79958214335 scopus 로고    scopus 로고
    • GGA3 functions as a switch to promote Met receptor recycling, essential for sustained ERK and cell migration
    • Parachoniak C.A., Luo Y, Abella JV, Keen JH, Park M. 2011. GGA3 functions as a switch to promote Met receptor recycling, essential for sustained ERK and cell migration. Dev Cell 20: 751-763.
    • (2011) Dev Cell , vol.20 , pp. 751-763
    • Parachoniak, C.A.1    Luo, Y.2    Abella, J.V.3    Keen, J.H.4    Park, M.5
  • 98
    • 0037534097 scopus 로고    scopus 로고
    • c-Cbl is a critical modulator of the Ron tyrosine kinase receptor
    • Penengo L., Rubin C, Yarden Y, Gaudino G. 2003. c-Cbl is a critical modulator of the Ron tyrosine kinase receptor. Oncogene 22: 3669-3679.
    • (2003) Oncogene , vol.22 , pp. 3669-3679
    • Penengo, L.1    Rubin, C.2    Yarden, Y.3    Gaudino, G.4
  • 100
    • 0035930341 scopus 로고    scopus 로고
    • Mutation of the c-Cbl TKB domain binding site on the Met receptor tyrosine kinase converts it into a transforming protein
    • Peschard P., Fournier TM, Lamorte L, Naujokas MA, Band H., Langdon WY, Park M. 2001. Mutation of the c-Cbl TKB domain binding site on the Met receptor tyrosine kinase converts it into a transforming protein. Mol Cell 8: 995-1004.
    • (2001) Mol Cell , vol.8 , pp. 995-1004
    • Peschard, P.1    Fournier, T.M.2    Lamorte, L.3    Naujokas, M.A.4    Band, H.5    Langdon, W.Y.6    Park, M.7
  • 102
    • 0842303313 scopus 로고    scopus 로고
    • Back to the future with ubiquitin
    • Pickart CM. 2004. Back to the future with ubiquitin. Cell 116: 181-190.
    • (2004) Cell , vol.116 , pp. 181-190
    • Pickart, C.M.1
  • 103
    • 78349252732 scopus 로고    scopus 로고
    • Eph/ephrin molecules-A hub for signaling and endocytosis
    • Pitulescu M.E., Adams RH. 2010. Eph/ephrin molecules-A hub for signaling and endocytosis. Genes Dev 24: 2480-2492.
    • (2010) Genes Dev , vol.24 , pp. 2480-2492
    • Pitulescu, M.E.1    Adams, R.H.2
  • 104
    • 0028263801 scopus 로고
    • Human insulin-like growth factor I receptor internalization. Role of the juxtamembrane domain
    • Prager D., Li HL, Yamasaki H, Melmed S. 1994. Human insulin-like growth factor I receptor internalization. Role of the juxtamembrane domain. J Biol Chem 269: 11934-11937.
    • (1994) J Biol Chem , vol.269 , pp. 11934-11937
    • Prager, D.1    Li, H.L.2    Yamasaki, H.3    Melmed, S.4
  • 105
    • 1542714469 scopus 로고    scopus 로고
    • Interactions of GGA3 with the ubiquitin sorting machinery
    • Puertollano R., Bonifacino JS. 2004. Interactions of GGA3 with the ubiquitin sorting machinery. Nat Cell Biol 6: 244-251.
    • (2004) Nat Cell Biol , vol.6 , pp. 244-251
    • Puertollano, R.1    Bonifacino, J.S.2
  • 107
    • 77949567362 scopus 로고    scopus 로고
    • VHS domains of ESCRT-0 cooperate in high-avidity binding to polyubiquitinated cargo
    • Ren X., Hurley JH. 2010. VHS domains of ESCRT-0 cooperate in high-avidity binding to polyubiquitinated cargo. EMBO J 29: 1045-1054.
    • (2010) EMBO J , vol.29 , pp. 1045-1054
    • Ren, X.1    Hurley, J.H.2
  • 108
    • 0041843750 scopus 로고    scopus 로고
    • An integrated model of epidermal growth factor receptor trafficking and signal transduction
    • Resat H., Ewald JA, Dixon DA, Wiley HS. 2003. An integrated model of epidermal growth factor receptor trafficking and signal transduction. Biophys J 85: 730-743.
    • (2003) Biophys J , vol.85 , pp. 730-743
    • Resat, H.1    Ewald, J.A.2    Dixon, D.A.3    Wiley, H.S.4
  • 110
    • 79959367966 scopus 로고    scopus 로고
    • CIN85 regulates ubiquitination and degradative endosomal sorting of the EGF receptor
    • Ronning S.B., Pedersen NM, Madshus IH, Stang E. 2011. CIN85 regulates ubiquitination and degradative endosomal sorting of the EGF receptor. Exp Cell Res 317: 1804-1816.
    • (2011) Exp Cell Res , vol.317 , pp. 1804-1816
    • Ronning, S.B.1    Pedersen, N.M.2    Madshus, I.H.3    Stang, E.4
  • 111
    • 67349132223 scopus 로고    scopus 로고
    • Physiological functions of the HECT family of ubiquitin ligases
    • Rotin D., Kumar S. 2009. Physiological functions of the HECT family of ubiquitin ligases. Nat Rev Mol Cell Biol 10: 398-409.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 398-409
    • Rotin, D.1    Kumar, S.2
  • 112
    • 33646788800 scopus 로고    scopus 로고
    • The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin dynamics and is essential for receptor downregulation
    • Row P.E., Prior IA, McCullough J, Clague MJ, Urbe S. 2006. The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin dynamics and is essential for receptor downregulation. J Biol Chem 281: 12618-12624.
    • (2006) J Biol Chem , vol.281 , pp. 12618-12624
    • Row, P.E.1    Prior, I.A.2    McCullough, J.3    Clague, M.J.4    Urbe, S.5
  • 114
    • 4744365071 scopus 로고    scopus 로고
    • Alix/AIP1 antagonizes epidermal growth factor receptor downregulation by the Cbl-SETA/CIN85 complex
    • Schmidt M.H., Hoeller D, Yu J, Furnari FB, Cavenee WK, Dikic I., Bogler O. 2004. Alix/AIP1 antagonizes epidermal growth factor receptor downregulation by the Cbl-SETA/CIN85 complex. Mol Cell Biol 24: 8981-8993.
    • (2004) Mol Cell Biol , vol.24 , pp. 8981-8993
    • Schmidt, M.H.1    Hoeller, D.2    Yu, J.3    Furnari, F.B.4    Cavenee, W.K.5    Dikic, I.6    Bogler, O.7
  • 115
    • 48649110734 scopus 로고    scopus 로고
    • Identification of c-Cbl as a new ligase for insulin-like growth factor-I receptor with distinct roles fromMdm2 in receptor ubiquitination and endocytosis
    • Sehat B., Andersson S, Girnita L, Larsson O. 2008. Identification of c-Cbl as a new ligase for insulin-like growth factor-I receptor with distinct roles fromMdm2 in receptor ubiquitination and endocytosis. Cancer Res 68: 5669-5677.
    • (2008) Cancer Res , vol.68 , pp. 5669-5677
    • Sehat, B.1    Andersson, S.2    Girnita, L.3    Larsson, O.4
  • 117
    • 0027249993 scopus 로고
    • Interaction of activated EGF receptors with coated pit adaptins
    • Sorkin A., Carpenter G. 1993. Interaction of activated EGF receptors with coated pit adaptins. Science 261: 612-615.
    • (1993) Science , vol.261 , pp. 612-615
    • Sorkin, A.1    Carpenter, G.2
  • 119
    • 0029889579 scopus 로고    scopus 로고
    • Epidermal growth factor receptor interaction with clathrin adaptors is mediated by the Tyr974-containing internalization motif
    • Sorkin A., Mazzotti M, Sorkina T, Scotto L, Beguinot L. 1996. Epidermal growth factor receptor interaction with clathrin adaptors is mediated by the Tyr974-containing internalization motif. J Biol Chem 271: 13377-13384.
    • (1996) J Biol Chem , vol.271 , pp. 13377-13384
    • Sorkin, A.1    Mazzotti, M.2    Sorkina, T.3    Scotto, L.4    Beguinot, L.5
  • 120
    • 0037075547 scopus 로고    scopus 로고
    • Cbl-CIN85-endophilin complex mediates ligand-induced downregulation of EGF receptors
    • Soubeyran P., Kowanetz K, Szymkiewicz I, Langdon WY, Dikic I. 2002. Cbl-CIN85-endophilin complex mediates ligand-induced downregulation of EGF receptors. Nature 416: 183-187.
    • (2002) Nature , vol.416 , pp. 183-187
    • Soubeyran, P.1    Kowanetz, K.2    Szymkiewicz, I.3    Langdon, W.Y.4    Dikic, I.5
  • 121
    • 0021219986 scopus 로고
    • Characterization of the metabolic turnover of epidermal growth factor receptor protein in A-431 cells
    • Stoscheck C.M., Carpenter G. 1984. Characterization of the metabolic turnover of epidermal growth factor receptor protein in A-431 cells. J Cell Physiol 120: 296-302.
    • (1984) J Cell Physiol , vol.120 , pp. 296-302
    • Stoscheck, C.M.1    Carpenter, G.2
  • 122
    • 18244372679 scopus 로고    scopus 로고
    • Ubiquitin-interacting motifs of Epsin are involved in the regulation of insulin-dependent endocytosis
    • Sugiyama S., Kishida S, Chayama K, Koyama S, Kikuchi A. 2005. Ubiquitin-interacting motifs of Epsin are involved in the regulation of insulin-dependent endocytosis. J Biochem 137: 355-364.
    • (2005) J Biochem , vol.137 , pp. 355-364
    • Sugiyama, S.1    Kishida, S.2    Chayama, K.3    Koyama, S.4    Kikuchi, A.5
  • 123
    • 35248849299 scopus 로고    scopus 로고
    • Grb2 mediates negative regulation of stem cell factor receptor/ c-Kit signaling by recruitment of Cbl
    • Sun J., Pedersen M, Bengtsson S, Ronnstrand L. 2007. Grb2 mediates negative regulation of stem cell factor receptor/ c-Kit signaling by recruitment of Cbl. Exp Cell Res 313: 3935-3942.
    • (2007) Exp Cell Res , vol.313 , pp. 3935-3942
    • Sun, J.1    Pedersen, M.2    Bengtsson, S.3    Ronnstrand, L.4
  • 127
    • 23044455604 scopus 로고    scopus 로고
    • Low density lipoprotein receptor-related protein 1 (LRP1) controls endocytosis and c-CBL-mediated ubiquitination of the platelet-derived growth factor receptor b (PDGFR b)
    • Takayama Y., May P, Anderson RG, Herz J. 2005. Low density lipoprotein receptor-related protein 1 (LRP1) controls endocytosis and c-CBL-mediated ubiquitination of the platelet-derived growth factor receptor b (PDGFR b). J Biol Chem 280: 18504-18510.
    • (2005) J Biol Chem , vol.280 , pp. 18504-18510
    • Takayama, Y.1    May, P.2    Anderson, R.G.3    Herz, J.4
  • 128
    • 0033516556 scopus 로고    scopus 로고
    • Possible involvement of a novel STAM-associated molecule "AMSH" in intracellular signal transduction mediated by cytokines
    • Tanaka N., Kaneko K, Asao H, Kasai H, Endo Y, Fujita T, Takeshita T., Sugamura K. 1999. Possible involvement of a novel STAM-associated molecule "AMSH" in intracellular signal transduction mediated by cytokines. J Biol Chem 274: 19129-19135.
    • (1999) J Biol Chem , vol.274 , pp. 19129-19135
    • Tanaka, N.1    Kaneko, K.2    Asao, H.3    Kasai, H.4    Endo, Y.5    Fujita, T.6    Takeshita, T.7    Sugamura, K.8
  • 129
    • 0029826531 scopus 로고    scopus 로고
    • Eps15 is a component of clathrin-coated pits and vesicles and is located at the rim of coated pits
    • Tebar F., Sorkina T, Sorkin A, Ericsson M, Kirchhausen T. 1996. Eps15 is a component of clathrin-coated pits and vesicles and is located at the rim of coated pits. J Biol Chem 271: 28727-28730.
    • (1996) J Biol Chem , vol.271 , pp. 28727-28730
    • Tebar, F.1    Sorkina, T.2    Sorkin, A.3    Ericsson, M.4    Kirchhausen, T.5
  • 130
    • 63049124957 scopus 로고    scopus 로고
    • SnapShot: The ESCRT machinery
    • Teis D., Saksena S, Emr SD. 2009. SnapShot: The ESCRT machinery. Cell 137: 182-182 e181.
    • (2009) Cell , vol.137
    • Teis, D.1    Saksena, S.2    Emr, S.D.3
  • 131
    • 24944538477 scopus 로고    scopus 로고
    • Negative regulation of PTK signalling by Cbl proteins
    • Thien C.B., Langdon WY. 2005. Negative regulation of PTK signalling by Cbl proteins. Growth Factors 23: 161-167.
    • (2005) Growth Factors , vol.23 , pp. 161-167
    • Thien, C.B.1    Langdon, W.Y.2
  • 132
    • 69249135065 scopus 로고    scopus 로고
    • Tickets to ride: Selecting cargo for clathrinregulated internalization
    • Traub LM. 2009. Tickets to ride: Selecting cargo for clathrinregulated internalization. Nat Rev Mol Cell Biol 10: 583-596.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 583-596
    • Traub, L.M.1
  • 135
    • 1342304089 scopus 로고    scopus 로고
    • Solution conformation of Lys63-linked di-ubiquitin chain provides clues to functional diversity of polyubiquitin signaling
    • Varadan R., Assfalg M, Haririnia A, Raasi S, Pickart C, Fushman D. 2004. Solution conformation of Lys63-linked di-ubiquitin chain provides clues to functional diversity of polyubiquitin signaling. J Biol Chem 279: 7055-7063.
    • (2004) J Biol Chem , vol.279 , pp. 7055-7063
    • Varadan, R.1    Assfalg, M.2    Haririnia, A.3    Raasi, S.4    Pickart, C.5    Fushman, D.6
  • 136
    • 0345381737 scopus 로고    scopus 로고
    • The Grb10/Nedd4 complex regulates ligand-induced ubiquitination and stability of the insulin-like growth factor I receptor
    • Vecchione A., Marchese A, Henry P, Rotin D, Morrione A. 2003. The Grb10/Nedd4 complex regulates ligand-induced ubiquitination and stability of the insulin-like growth factor I receptor. Mol Cell Biol 23: 3363-3372.
    • (2003) Mol Cell Biol , vol.23 , pp. 3363-3372
    • Vecchione, A.1    Marchese, A.2    Henry, P.3    Rotin, D.4    Morrione, A.5
  • 138
    • 79951933973 scopus 로고    scopus 로고
    • D-Cbl binding to Drk leads to dosedependent down-regulation of EGFR signaling and increases receptor-ligand endocytosis
    • Wang P.Y., Pai LM. 2011. D-Cbl binding to Drk leads to dosedependent down-regulation of EGFR signaling and increases receptor-ligand endocytosis. PloS ONE 6: e17097.
    • (2011) PloS ONE , vol.6
    • Wang, P.Y.1    Pai, L.M.2
  • 139
    • 0036469898 scopus 로고    scopus 로고
    • A mutant EGF-receptor defective in ubiquitylation and endocytosis unveils a role for Grb2 in negative signaling
    • Waterman H., Katz M, Rubin C, Shtiegman K, Lavi S, Elson A., Jovin T, Yarden Y. 2002. A mutant EGF-receptor defective in ubiquitylation and endocytosis unveils a role for Grb2 in negative signaling. EMBO J 21: 303-313.
    • (2002) EMBO J , vol.21 , pp. 303-313
    • Waterman, H.1    Katz, M.2    Rubin, C.3    Shtiegman, K.4    Lavi, S.5    Elson, A.6    Jovin, T.7    Yarden, Y.8
  • 140
    • 30444456831 scopus 로고    scopus 로고
    • EGF stimulates annexin 1-dependent inward vesiculation in a multivesicular endosome subpopulation
    • White I.J., Bailey LM, Aghakhani MR, Moss SE, Futter CE. 2006. EGF stimulates annexin 1-dependent inward vesiculation in a multivesicular endosome subpopulation. EMBO J 25: 1-12.
    • (2006) EMBO J , vol.25 , pp. 1-12
    • White, I.J.1    Bailey, L.M.2    Aghakhani, M.R.3    Moss, S.E.4    Futter, C.E.5
  • 141
    • 3242700634 scopus 로고    scopus 로고
    • Signaling, internalization, and intracellular activity of fibroblast growth factor
    • Wiedlocha A., Sorensen V. 2004. Signaling, internalization, and intracellular activity of fibroblast growth factor. Curr Top Microbiol Immunol 286: 45-79.
    • (2004) Curr Top Microbiol Immunol , vol.286 , pp. 45-79
    • Wiedlocha, A.1    Sorensen, V.2
  • 142
    • 0023677140 scopus 로고
    • Anomalous binding of epidermal growth factor to A431 cells is due to the effect of high receptor densities and a saturable endocytic system
    • Wiley HS. 1988. Anomalous binding of epidermal growth factor to A431 cells is due to the effect of high receptor densities and a saturable endocytic system. J Cell Biol 107: 801-810.
    • (1988) J Cell Biol , vol.107 , pp. 801-810
    • Wiley, H.S.1
  • 143
    • 0037034167 scopus 로고    scopus 로고
    • C-Cbl binds the CSF-1 receptor at tyrosine 973, a novel phosphorylation site in the receptor's carboxy-terminus
    • Wilhelmsen K., Burkhalter S, van der Geer P. 2002. C-Cbl binds the CSF-1 receptor at tyrosine 973, a novel phosphorylation site in the receptor's carboxy-terminus. Oncogene 21: 1079-1089.
    • (2002) Oncogene , vol.21 , pp. 1079-1089
    • Wilhelmsen, K.1    Burkhalter, S.2    van der Geer, P.3
  • 144
    • 0037119950 scopus 로고    scopus 로고
    • Sprouty2 attenuates epidermal growth factor receptor ubiquitylation and endocytosis, and consequently enhances Ras/ERK signalling
    • Wong E.S., Fong CW, Lim J, Yusoff P, Low BC, Langdon WY, Guy GR. 2002. Sprouty2 attenuates epidermal growth factor receptor ubiquitylation and endocytosis, and consequently enhances Ras/ERK signalling. EMBO J 21: 4796-4808.
    • (2002) EMBO J , vol.21 , pp. 4796-4808
    • Wong, E.S.1    Fong, C.W.2    Lim, J.3    Yusoff, P.4    Low, B.C.5    Langdon, W.Y.6    Guy, G.R.7
  • 145
    • 0142040128 scopus 로고    scopus 로고
    • YXXM motifs in the PDGF-b receptor serve dual roles as phosphoinositide 3-kinase binding motifs and tyrosine-based endocytic sorting signals
    • Wu H., Windmiller DA, Wang L, Backer JM. 2003a. YXXM motifs in the PDGF-b receptor serve dual roles as phosphoinositide 3-kinase binding motifs and tyrosine-based endocytic sorting signals. J Biol Chem 278: 40425-40428.
    • (2003) J Biol Chem , vol.278 , pp. 40425-40428
    • Wu, H.1    Windmiller, D.A.2    Wang, L.3    Backer, J.M.4
  • 146
    • 0141426629 scopus 로고    scopus 로고
    • Activated Cdc42 sequesters c-Cbl and prevents EGF receptor degradation
    • Wu W.J., Tu S, Cerione RA. 2003b. Activated Cdc42 sequesters c-Cbl and prevents EGF receptor degradation. Cell 114: 715-725.
    • (2003) Cell , vol.114 , pp. 715-725
    • Wu, W.J.1    Tu, S.2    Cerione, R.A.3
  • 147
    • 60649118104 scopus 로고    scopus 로고
    • The coming of age of axonal neurotrophin signaling endosomes
    • Wu C., Cui B, He L, Chen L, Mobley WC. 2009. The coming of age of axonal neurotrophin signaling endosomes. J Proteomics 72: 46-55.
    • (2009) J Proteomics , vol.72 , pp. 46-55
    • Wu, C.1    Cui, B.2    He, L.3    Chen, L.4    Mobley, W.C.5
  • 152
    • 0033748123 scopus 로고    scopus 로고
    • Requirements of multiple domains of SLI-1, a Caenorhabditis elegans homologue of c-Cbl, and an inhibitory tyrosine in LET-23 in regulating vulval differentiation
    • Yoon C.H., Chang C, Hopper NA, Lesa GM, Sternberg PW. 2000. Requirements of multiple domains of SLI-1, a Caenorhabditis elegans homologue of c-Cbl, and an inhibitory tyrosine in LET-23 in regulating vulval differentiation. Mol Biol Cell 11: 4019-4031.
    • (2000) Mol Biol Cell , vol.11 , pp. 4019-4031
    • Yoon, C.H.1    Chang, C.2    Hopper, N.A.3    Lesa, G.M.4    Sternberg, P.W.5
  • 153
    • 0031730287 scopus 로고    scopus 로고
    • Nerve growth factor processing and trafficking events following TrkA-mediated endocytosis
    • Zapf-Colby A, Olefsky JM. 1998. Nerve growth factor processing and trafficking events following TrkA-mediated endocytosis. Endocrinology 139: 3232-3240.
    • (1998) Endocrinology , vol.139 , pp. 3232-3240
    • Zapf-Colby, A.1    Olefsky, J.M.2
  • 154
    • 11144244315 scopus 로고    scopus 로고
    • Regulation of stem cell factor receptor signaling by Cbl family proteins (Cbl-b/c-Cbl)
    • Zeng S., Xu Z, Lipkowitz S, Longley JB. 2005. Regulation of stem cell factor receptor signaling by Cbl family proteins (Cbl-b/c-Cbl). Blood 105: 226-232.
    • (2005) Blood , vol.105 , pp. 226-232
    • Zeng, S.1    Xu, Z.2    Lipkowitz, S.3    Longley, J.B.4
  • 155
    • 67649311930 scopus 로고    scopus 로고
    • Nedd4 mediates ErbB4 JM-a/ CYT-1 ICD ubiquitination and degradation in MDCK II cells
    • Zeng F., Xu J, Harris RC. 2009. Nedd4 mediates ErbB4 JM-a/ CYT-1 ICD ubiquitination and degradation in MDCK II cells. FASEB J 23: 1935-1945.
    • (2009) FASEB J , vol.23 , pp. 1935-1945
    • Zeng, F.1    Xu, J.2    Harris, R.C.3
  • 156
    • 45149133324 scopus 로고    scopus 로고
    • Clathrin-dependent endocytosis is required for TrkB-dependent Aktmediated neuronal protection and dendritic growth
    • Zheng J., Shen WH, Lu TJ, Zhou Y, Chen Q, Wang Z, Xiang T, Zhu Y.C., Zhang C, Duan S, et al. 2008. Clathrin-dependent endocytosis is required for TrkB-dependent Aktmediated neuronal protection and dendritic growth. J Biol Chem 283: 13280-13288.
    • (2008) J Biol Chem , vol.283 , pp. 13280-13288
    • Zheng, J.1    Shen, W.H.2    Lu, T.J.3    Zhou, Y.4    Chen, Q.5    Wang, Z.6    Xiang, T.7    Zhu, Y.C.8    Zhang, C.9    Duan, S.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.