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Volumn 6, Issue 9, 2011, Pages

The von hippel-lindau tumor suppressor protein promotes c-Cbl-independent poly-ubiquitylation and degradation of the activated EGFR

Author keywords

[No Author keywords available]

Indexed keywords

CBL PROTEIN; EPIDERMAL GROWTH FACTOR RECEPTOR; HYPOXIA INDUCIBLE FACTOR 2ALPHA; PROTEASOME INHIBITOR; VON HIPPEL LINDAU PROTEIN; BASIC HELIX LOOP HELIX TRANSCRIPTION FACTOR; BENZYLOXYCARBONYLLEUCYL LEUCYL LEUCINE ALDEHYDE; BENZYLOXYCARBONYLLEUCYL-LEUCYL-LEUCINE ALDEHYDE; CBL PROTEIN, HUMAN; CHLOROQUINE; CYSTEINE PROTEINASE INHIBITOR; ENDOTHELIAL PAS DOMAIN CONTAINING PROTEIN 1; ENDOTHELIAL PAS DOMAIN-CONTAINING PROTEIN 1; LEUPEPTIN; VHL PROTEIN, HUMAN;

EID: 80052854931     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0023936     Document Type: Article
Times cited : (41)

References (43)
  • 2
    • 0036718539 scopus 로고    scopus 로고
    • Molecular basis of the VHL hereditary cancer syndrome
    • Kaelin WG Jr, (2002) Molecular basis of the VHL hereditary cancer syndrome. Nat Rev Cancer 2: 673-682.
    • (2002) Nat Rev Cancer , vol.2 , pp. 673-682
    • Kaelin Jr., W.G.1
  • 3
    • 0033597443 scopus 로고    scopus 로고
    • Rbx1, a component of the VHL tumor suppressor complex and SCF ubiquitin ligase
    • Kamura T, Koepp DM, Conrad MN, Skowyra D, Moreland RJ, et al. (1999) Rbx1, a component of the VHL tumor suppressor complex and SCF ubiquitin ligase. Science 284: 657-661.
    • (1999) Science , vol.284 , pp. 657-661
    • Kamura, T.1    Koepp, D.M.2    Conrad, M.N.3    Skowyra, D.4    Moreland, R.J.5
  • 4
    • 0033776536 scopus 로고    scopus 로고
    • Ubiquitination of hypoxia-inducible factor requires direct binding to the beta-domain of the von Hippel-Lindau protein
    • Ohh M, Park CW, Ivan M, Hoffman MA, Kim TY, et al. (2000) Ubiquitination of hypoxia-inducible factor requires direct binding to the beta-domain of the von Hippel-Lindau protein. Nat Cell Biol 2: 423-427.
    • (2000) Nat Cell Biol , vol.2 , pp. 423-427
    • Ohh, M.1    Park, C.W.2    Ivan, M.3    Hoffman, M.A.4    Kim, T.Y.5
  • 5
    • 34948883495 scopus 로고    scopus 로고
    • pVHL acts as an adaptor to promote the inhibitory phosphorylation of the NF-kappaB agonist Card9 by CK2
    • Yang H, Minamishima YA, Yan Q, Schlisio S, Ebert BL, et al. (2007) pVHL acts as an adaptor to promote the inhibitory phosphorylation of the NF-kappaB agonist Card9 by CK2. Mol Cell 28: 15-27.
    • (2007) Mol Cell , vol.28 , pp. 15-27
    • Yang, H.1    Minamishima, Y.A.2    Yan, Q.3    Schlisio, S.4    Ebert, B.L.5
  • 6
    • 68249112645 scopus 로고    scopus 로고
    • VHL loss causes spindle misorientation and chromosome instability
    • Thoma CR, Toso A, Gutbrodt KL, Reggi SP, Frew IJ, et al. (2009) VHL loss causes spindle misorientation and chromosome instability. Nat Cell Biol 11: 994-1001.
    • (2009) Nat Cell Biol , vol.11 , pp. 994-1001
    • Thoma, C.R.1    Toso, A.2    Gutbrodt, K.L.3    Reggi, S.P.4    Frew, I.J.5
  • 7
    • 58149159900 scopus 로고    scopus 로고
    • Sporadic clear cell renal cell carcinoma but not the papillary type is characterized by severely reduced frequency of primary cilia
    • Schraml P, Frew IJ, Thoma CR, Boysen G, Struckmann K, et al. (2009) Sporadic clear cell renal cell carcinoma but not the papillary type is characterized by severely reduced frequency of primary cilia. Mod Pathol 22: 31-36.
    • (2009) Mod Pathol , vol.22 , pp. 31-36
    • Schraml, P.1    Frew, I.J.2    Thoma, C.R.3    Boysen, G.4    Struckmann, K.5
  • 8
    • 42149089909 scopus 로고    scopus 로고
    • The von Hippel-Lindau tumor suppressor protein and Egl-9-Type proline hydroxylases regulate the large subunit of RNA polymerase II in response to oxidative stress
    • Mikhaylova O, Ignacak ML, Barankiewicz TJ, Harbaugh SV, Yi Y, et al. (2008) The von Hippel-Lindau tumor suppressor protein and Egl-9-Type proline hydroxylases regulate the large subunit of RNA polymerase II in response to oxidative stress. Mol Cell Biol 28: 2701-2717.
    • (2008) Mol Cell Biol , vol.28 , pp. 2701-2717
    • Mikhaylova, O.1    Ignacak, M.L.2    Barankiewicz, T.J.3    Harbaugh, S.V.4    Yi, Y.5
  • 9
    • 35148828429 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1 (HIF-1) pathway
    • Semenza GL, (2007) Hypoxia-inducible factor 1 (HIF-1) pathway. Sci STKE 2007: cm8.
    • (2007) Sci STKE , vol.2007
    • Semenza, G.L.1
  • 10
    • 0035917313 scopus 로고    scopus 로고
    • HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing
    • Ivan M, Kondo K, Yang H, Kim W, Valiando J, et al. (2001) HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing. Science 292: 464-468.
    • (2001) Science , vol.292 , pp. 464-468
    • Ivan, M.1    Kondo, K.2    Yang, H.3    Kim, W.4    Valiando, J.5
  • 11
    • 0035917808 scopus 로고    scopus 로고
    • Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation
    • Jaakkola P, Mole DR, Tian YM, Wilson MI, Gielbert J, et al. (2001) Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation. Science 292: 468-472.
    • (2001) Science , vol.292 , pp. 468-472
    • Jaakkola, P.1    Mole, D.R.2    Tian, Y.M.3    Wilson, M.I.4    Gielbert, J.5
  • 12
    • 17944375360 scopus 로고    scopus 로고
    • C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation
    • Epstein AC, Gleadle JM, McNeill LA, Hewitson KS, O'Rourke J, et al. (2001) C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell 107: 43-54.
    • (2001) Cell , vol.107 , pp. 43-54
    • Epstein, A.C.1    Gleadle, J.M.2    McNeill, L.A.3    Hewitson, K.S.4    O'Rourke, J.5
  • 13
    • 0037108807 scopus 로고    scopus 로고
    • Biochemical purification and pharmacological inhibition of a mammalian prolyl hydroxylase acting on hypoxia-inducible factor
    • Ivan M, Haberberger T, Gervasi DC, Michelson KS, Gunzler V, et al. (2002) Biochemical purification and pharmacological inhibition of a mammalian prolyl hydroxylase acting on hypoxia-inducible factor. Proc Natl Acad Sci U S A 99: 13459-13464.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 13459-13464
    • Ivan, M.1    Haberberger, T.2    Gervasi, D.C.3    Michelson, K.S.4    Gunzler, V.5
  • 14
    • 0142166332 scopus 로고    scopus 로고
    • Targeting HIF-1 for cancer therapy
    • Semenza GL, (2003) Targeting HIF-1 for cancer therapy. Nat Rev Cancer 3: 721-732.
    • (2003) Nat Rev Cancer , vol.3 , pp. 721-732
    • Semenza, G.L.1
  • 15
    • 0036528246 scopus 로고    scopus 로고
    • Inhibition of HIF is necessary for tumor suppression by the von Hippel-Lindau protein
    • Kondo K, Klco J, Nakamura E, Lechpammer M, Kaelin WG Jr, (2002) Inhibition of HIF is necessary for tumor suppression by the von Hippel-Lindau protein. Cancer Cell 1: 237-246.
    • (2002) Cancer Cell , vol.1 , pp. 237-246
    • Kondo, K.1    Klco, J.2    Nakamura, E.3    Lechpammer, M.4    Kaelin Jr., W.G.5
  • 16
    • 1342280515 scopus 로고    scopus 로고
    • Inhibition of hypoxia-inducible factor is sufficient for growth suppression of VHL-/- tumors
    • Zimmer M, Doucette D, Siddiqui N, Iliopoulos O, (2004) Inhibition of hypoxia-inducible factor is sufficient for growth suppression of VHL-/- tumors. Mol Cancer Res 2: 89-95.
    • (2004) Mol Cancer Res , vol.2 , pp. 89-95
    • Zimmer, M.1    Doucette, D.2    Siddiqui, N.3    Iliopoulos, O.4
  • 17
    • 2342597973 scopus 로고    scopus 로고
    • Inhibition of HIF2alpha is sufficient to suppress pVHL-defective tumor growth
    • Kondo K, Kim WY, Lechpammer M, Kaelin WG Jr, (2003) Inhibition of HIF2alpha is sufficient to suppress pVHL-defective tumor growth. PLoS Biol 1: E83.
    • (2003) PLoS Biol , vol.1
    • Kondo, K.1    Kim, W.Y.2    Lechpammer, M.3    Kaelin Jr., W.G.4
  • 18
    • 16244379522 scopus 로고    scopus 로고
    • VEGF-targeted therapy in metastatic renal cell carcinoma
    • Rini BI, (2005) VEGF-targeted therapy in metastatic renal cell carcinoma. Oncologist 10: 191-197.
    • (2005) Oncologist , vol.10 , pp. 191-197
    • Rini, B.I.1
  • 19
    • 0035852630 scopus 로고    scopus 로고
    • Role of transforming growth factor-alpha in von Hippel-Lindau (VHL)(-/-) clear cell renal carcinoma cell proliferation: a possible mechanism coupling VHL tumor suppressor inactivation and tumorigenesis
    • de Paulsen N, Brychzy A, Fournier MC, Klausner RD, Gnarra JR, et al. (2001) Role of transforming growth factor-alpha in von Hippel-Lindau (VHL)(-/-) clear cell renal carcinoma cell proliferation: a possible mechanism coupling VHL tumor suppressor inactivation and tumorigenesis. Proc Natl Acad Sci U S A 98: 1387-1392.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 1387-1392
    • de Paulsen, N.1    Brychzy, A.2    Fournier, M.C.3    Klausner, R.D.4    Gnarra, J.R.5
  • 20
    • 34548803430 scopus 로고    scopus 로고
    • Translational up-regulation of the EGFR by tumor hypoxia provides a nonmutational explanation for its overexpression in human cancer
    • Franovic A, Gunaratnam L, Smith K, Robert I, Patten D, et al. (2007) Translational up-regulation of the EGFR by tumor hypoxia provides a nonmutational explanation for its overexpression in human cancer. Proc Natl Acad Sci U S A 104: 13092-13097.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 13092-13097
    • Franovic, A.1    Gunaratnam, L.2    Smith, K.3    Robert, I.4    Patten, D.5
  • 21
    • 50849090006 scopus 로고    scopus 로고
    • Von Hippel-Lindau tumor suppressor gene loss in renal cell carcinoma promotes oncogenic epidermal growth factor receptor signaling via Akt-1 and MEK-1
    • Lee SJ, Lattouf JB, Xanthopoulos J, Linehan WM, Bottaro DP, et al. (2008) Von Hippel-Lindau tumor suppressor gene loss in renal cell carcinoma promotes oncogenic epidermal growth factor receptor signaling via Akt-1 and MEK-1. Eur Urol 54: 845-853.
    • (2008) Eur Urol , vol.54 , pp. 845-853
    • Lee, S.J.1    Lattouf, J.B.2    Xanthopoulos, J.3    Linehan, W.M.4    Bottaro, D.P.5
  • 22
    • 20444485232 scopus 로고    scopus 로고
    • Silencing of epidermal growth factor receptor suppresses hypoxia-inducible factor-2-driven VHL-/- renal cancer
    • Smith K, Gunaratnam L, Morley M, Franovic A, Mekhail K, et al. (2005) Silencing of epidermal growth factor receptor suppresses hypoxia-inducible factor-2-driven VHL-/- renal cancer. Cancer Res 65: 5221-5230.
    • (2005) Cancer Res , vol.65 , pp. 5221-5230
    • Smith, K.1    Gunaratnam, L.2    Morley, M.3    Franovic, A.4    Mekhail, K.5
  • 23
    • 34250216633 scopus 로고    scopus 로고
    • Mutational activation of ErbB family receptor tyrosine kinases: insights into mechanisms of signal transduction and tumorigenesis
    • Riese DJ 2nd, Gallo RM, Settleman J, (2007) Mutational activation of ErbB family receptor tyrosine kinases: insights into mechanisms of signal transduction and tumorigenesis. Bioessays 29: 558-565.
    • (2007) Bioessays , vol.29 , pp. 558-565
    • Riese 2nd, D.J.1    Gallo, R.M.2    Settleman, J.3
  • 25
    • 0037429737 scopus 로고    scopus 로고
    • Epidermal growth factor receptor: mechanisms of activation and signalling
    • Jorissen RN, Walker F, Pouliot N, Garrett TP, Ward CW, et al. (2003) Epidermal growth factor receptor: mechanisms of activation and signalling. Exp Cell Res 284: 31-53.
    • (2003) Exp Cell Res , vol.284 , pp. 31-53
    • Jorissen, R.N.1    Walker, F.2    Pouliot, N.3    Garrett, T.P.4    Ward, C.W.5
  • 26
    • 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: 3663-3674.
    • (1998) Genes Dev , vol.12 , pp. 3663-3674
    • Levkowitz, G.1    Waterman, H.2    Zamir, E.3    Kam, Z.4    Oved, S.5
  • 27
    • 0033392493 scopus 로고    scopus 로고
    • Ubiquitin ligase activity and tyrosine phosphorylation underlie suppression of growth factor signaling by c-Cbl/Sli-1
    • Levkowitz G, Waterman H, Ettenberg SA, Katz M, Tsygankov AY, et al. (1999) Ubiquitin ligase activity and tyrosine phosphorylation underlie suppression of growth factor signaling by c-Cbl/Sli-1. Mol Cell 4: 1029-1040.
    • (1999) Mol Cell , vol.4 , pp. 1029-1040
    • Levkowitz, G.1    Waterman, H.2    Ettenberg, S.A.3    Katz, M.4    Tsygankov, A.Y.5
  • 28
    • 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, et al. (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
  • 29
    • 0038394715 scopus 로고    scopus 로고
    • Multiple monoubiquitination of RTKs is sufficient for their endocytosis and degradation
    • Haglund K, Sigismund S, Polo S, Szymkiewicz I, Di Fiore PP, et al. (2003) Multiple monoubiquitination of RTKs is sufficient for their endocytosis and degradation. Nat Cell Biol 5: 461-466.
    • (2003) Nat Cell Biol , vol.5 , pp. 461-466
    • Haglund, K.1    Sigismund, S.2    Polo, S.3    Szymkiewicz, I.4    Di Fiore, P.P.5
  • 30
    • 36749036679 scopus 로고    scopus 로고
    • EGF receptor ubiquitination is not necessary for its internalization
    • Huang F, Goh LK, Sorkin A, (2007) EGF receptor ubiquitination is not necessary for its internalization. Proc Natl Acad Sci U S A 104: 16904-16909.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 16904-16909
    • Huang, F.1    Goh, L.K.2    Sorkin, A.3
  • 31
    • 77953167957 scopus 로고    scopus 로고
    • Multiple mechanisms collectively regulate clathrin-mediated endocytosis of the epidermal growth factor receptor
    • Goh LK, Huang F, Kim W, Gygi S, Sorkin A, Multiple mechanisms collectively regulate clathrin-mediated endocytosis of the epidermal growth factor receptor. J Cell Biol 189: 871-883.
    • J Cell Biol , vol.189 , pp. 871-883
    • Goh, L.K.1    Huang, F.2    Kim, W.3    Gygi, S.4    Sorkin, A.5
  • 32
    • 0036902646 scopus 로고    scopus 로고
    • Receptor downregulation and multivesicular-body sorting
    • Katzmann DJ, Odorizzi G, Emr SD, (2002) Receptor downregulation and multivesicular-body sorting. Nat Rev Mol Cell Biol 3: 893-905.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 893-905
    • Katzmann, D.J.1    Odorizzi, G.2    Emr, S.D.3
  • 33
    • 0037677208 scopus 로고    scopus 로고
    • Endocytosis of receptor tyrosine kinases is driven by monoubiquitylation, not polyubiquitylation
    • Mosesson Y, Shtiegman K, Katz M, Zwang Y, Vereb G, et al. (2003) Endocytosis of receptor tyrosine kinases is driven by monoubiquitylation, not polyubiquitylation. J Biol Chem 278: 21323-21326.
    • (2003) J Biol Chem , vol.278 , pp. 21323-21326
    • Mosesson, Y.1    Shtiegman, K.2    Katz, M.3    Zwang, Y.4    Vereb, G.5
  • 34
    • 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
  • 35
    • 54249151578 scopus 로고    scopus 로고
    • Ubc4/5 and c-Cbl continue to ubiquitinate EGF receptor after internalization to facilitate polyubiquitination and degradation
    • Umebayashi K, Stenmark H, Yoshimori T, (2008) Ubc4/5 and c-Cbl continue to ubiquitinate EGF receptor after internalization to facilitate polyubiquitination and degradation. Mol Biol Cell 19: 3454-3462.
    • (2008) Mol Biol Cell , vol.19 , pp. 3454-3462
    • Umebayashi, K.1    Stenmark, H.2    Yoshimori, T.3
  • 36
    • 61949090107 scopus 로고    scopus 로고
    • Regulation of endocytosis via the oxygen-sensing pathway
    • Wang Y, Roche O, Yan MS, Finak G, Evans AJ, et al. (2009) Regulation of endocytosis via the oxygen-sensing pathway. Nat Med 15: 319-324.
    • (2009) Nat Med , vol.15 , pp. 319-324
    • Wang, Y.1    Roche, O.2    Yan, M.S.3    Finak, G.4    Evans, A.J.5
  • 37
    • 0042206678 scopus 로고    scopus 로고
    • Cbl-mediated ubiquitinylation is required for lysosomal sorting of epidermal growth factor receptor but is dispensable for endocytosis
    • Duan L, Miura Y, Dimri M, Majumder B, Dodge IL, et al. (2003) Cbl-mediated ubiquitinylation is required for lysosomal sorting of epidermal growth factor receptor but is dispensable for endocytosis. J Biol Chem 278: 28950-28960.
    • (2003) J Biol Chem , vol.278 , pp. 28950-28960
    • Duan, L.1    Miura, Y.2    Dimri, M.3    Majumder, B.4    Dodge, I.L.5
  • 38
    • 0033587146 scopus 로고    scopus 로고
    • The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis
    • Maxwell PH, Wiesener MS, Chang GW, Clifford SC, Vaux EC, et al. (1999) The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis. Nature 399: 271-275.
    • (1999) Nature , vol.399 , pp. 271-275
    • Maxwell, P.H.1    Wiesener, M.S.2    Chang, G.W.3    Clifford, S.C.4    Vaux, E.C.5
  • 40
    • 54849372300 scopus 로고    scopus 로고
    • Endocytosis and intracellular trafficking of ErbBs
    • Sorkin A, Goh LK, (2008) Endocytosis and intracellular trafficking of ErbBs. Exp Cell Res 314: 3093-3106.
    • (2008) Exp Cell Res , vol.314 , pp. 3093-3106
    • Sorkin, A.1    Goh, L.K.2
  • 41
    • 0037018146 scopus 로고    scopus 로고
    • Ubiquitination and proteasomal activity is required for transport of the EGF receptor to inner membranes of multivesicular bodies
    • Longva KE, Blystad FD, Stang E, Larsen AM, Johannessen LE, et al. (2002) Ubiquitination and proteasomal activity is required for transport of the EGF receptor to inner membranes of multivesicular bodies. J Cell Biol 156: 843-854.
    • (2002) J Cell Biol , vol.156 , pp. 843-854
    • Longva, K.E.1    Blystad, F.D.2    Stang, E.3    Larsen, A.M.4    Johannessen, L.E.5
  • 42
    • 77954739712 scopus 로고    scopus 로고
    • Chloroquine-induced autophagic vacuole accumulation and cell death in glioma cells is p53 independent
    • Geng Y, Kohli L, Klocke BJ, Roth KA, Chloroquine-induced autophagic vacuole accumulation and cell death in glioma cells is p53 independent. Neuro Oncol 12: 473-481.
    • Neuro Oncol , vol.12 , pp. 473-481
    • Geng, Y.1    Kohli, L.2    Klocke, B.J.3    Roth, K.A.4
  • 43
    • 63049125531 scopus 로고    scopus 로고
    • Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation
    • Xu P, Duong DM, Seyfried NT, Cheng D, Xie Y, et al. (2009) Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation. Cell 137: 133-145.
    • (2009) Cell , vol.137 , pp. 133-145
    • Xu, P.1    Duong, D.M.2    Seyfried, N.T.3    Cheng, D.4    Xie, Y.5


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