메뉴 건너뛰기




Volumn 4, Issue 10, 2009, Pages

COMMD1 promotes pVHL and O2-independent proteolysis of HIF-1α via HSP90/70

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CHAPERONE; COPPER MUTABOLISM MURR1 DOMAIN CONTAINING 1 PROTEIN; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; HYPOXIA INDUCIBLE FACTOR 1ALPHA; TANESPIMYCIN; UNCLASSIFIED DRUG; VON HIPPEL LINDAU PROTEIN; 17-(ALLYLAMINO)-17-DEMETHOXYGELDANAMYCIN; BENZOQUINONE DERIVATIVE; CARRIER PROTEIN; COMMD1 PROTEIN, HUMAN; MACROCYCLIC LACTAM; OXYGEN; PROTEASOME; UBIQUITIN;

EID: 70350012306     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0007332     Document Type: Article
Times cited : (50)

References (35)
  • 1
    • 20444470299 scopus 로고    scopus 로고
    • COMMD proteins, a novel family of structural and functional homologs of MURR1
    • Burstein E, Hoberg JE, Wilkinson AS, Rumble JM, Csomos RA, et al. (2005) COMMD proteins, a novel family of structural and functional homologs of MURR1. J Biol Chem 280: 22222-22232.
    • (2005) J Biol Chem , vol.280 , pp. 22222-22232
    • Burstein, E.1    Hoberg, J.E.2    Wilkinson, A.S.3    Rumble, J.M.4    Csomos, R.A.5
  • 2
    • 34447623789 scopus 로고    scopus 로고
    • COMMD proteins: COMMing to the scene
    • Maine GN, Burstein E (2007) COMMD proteins: COMMing to the scene. Cell Mol Life Sci 64: 1997-2005.
    • (2007) Cell Mol Life Sci , vol.64 , pp. 1997-2005
    • Maine, G.N.1    Burstein, E.2
  • 3
    • 58249086099 scopus 로고    scopus 로고
    • COMMD1 expression is controlled by critical residues that determine XIAP binding
    • Maine GN, Mao X, Muller PA, Komarck CM, Klomp LW, et al. (2009) COMMD1 expression is controlled by critical residues that determine XIAP binding. Biochem J 417: 601-609.
    • (2009) Biochem J , vol.417 , pp. 601-609
    • Maine, G.N.1    Mao, X.2    Muller, P.A.3    Komarck, C.M.4    Klomp, L.W.5
  • 5
    • 33846475712 scopus 로고    scopus 로고
    • COMMD1 promotes the ubiquitination of NF-kappaB subunits through a cullin-containing ubiquitin ligase
    • Maine GN, Mao X, Komarck CM, Burstein E (2007) COMMD1 promotes the ubiquitination of NF-kappaB subunits through a cullin-containing ubiquitin ligase. Embo J 26: 436-447.
    • (2007) Embo J , vol.26 , pp. 436-447
    • Maine, G.N.1    Mao, X.2    Komarck, C.M.3    Burstein, E.4
  • 6
    • 0242690424 scopus 로고    scopus 로고
    • The ubiquitously expressed MURR1 protein is absent in canine copper toxicosis
    • Klomp AE, van de Sluis B, Klomp LW, Wijmenga C (2003) The ubiquitously expressed MURR1 protein is absent in canine copper toxicosis. J Hepatol 39: 703-709.
    • (2003) J Hepatol , vol.39 , pp. 703-709
    • Klomp, A.E.1    van de Sluis, B.2    Klomp, L.W.3    Wijmenga, C.4
  • 7
    • 0037081771 scopus 로고    scopus 로고
    • Identification of a new copper metabolism gene by positional cloning in a purebred dog population
    • van De Sluis B, Rothuizen J, Pearson PL, van Oost BA, Wijmenga C (2002) Identification of a new copper metabolism gene by positional cloning in a purebred dog population. Hum Mol Genet 11: 165-173.
    • (2002) Hum Mol Genet , vol.11 , pp. 165-173
    • van De Sluis, B.1    Rothuizen, J.2    Pearson, P.L.3    van Oost, B.A.4    Wijmenga, C.5
  • 8
    • 34548861803 scopus 로고    scopus 로고
    • Distinct Wilson's disease mutations in ATP7B are associated with enhanced binding to COMMD1 and reduced stability of ATP7B
    • de Bie P, van de Sluis B, Burstein E, van de Berghe PV, Muller P, et al. (2007) Distinct Wilson's disease mutations in ATP7B are associated with enhanced binding to COMMD1 and reduced stability of ATP7B. Gastroenterology 133: 1316-1326.
    • (2007) Gastroenterology , vol.133 , pp. 1316-1326
    • de Bie, P.1    van de Sluis, B.2    Burstein, E.3    van de Berghe, P.V.4    Muller, P.5
  • 9
    • 0142149219 scopus 로고    scopus 로고
    • The copper toxicosis gene product Murr1 directly interacts with the Wilson disease protein
    • Tao TY, Liu F, Klomp L, Wijmenga C, Gitlin JD (2003) The copper toxicosis gene product Murr1 directly interacts with the Wilson disease protein. J Biol Chem 278: 41593-41596.
    • (2003) J Biol Chem , vol.278 , pp. 41593-41596
    • Tao, T.Y.1    Liu, F.2    Klomp, L.3    Wijmenga, C.4    Gitlin, J.D.5
  • 10
    • 64349114240 scopus 로고    scopus 로고
    • GCN5 is a required cofactor for a ubiquitin ligase that targets NF-kappaB/RelA
    • Mao X, Gluck N, Li D, Maine GN, Li H, et al. (2009) GCN5 is a required cofactor for a ubiquitin ligase that targets NF-kappaB/RelA. Genes Dev 23: 849-861.
    • (2009) Genes Dev , vol.23 , pp. 849-861
    • Mao, X.1    Gluck, N.2    Li, D.3    Maine, G.N.4    Li, H.5
  • 11
    • 34347352142 scopus 로고    scopus 로고
    • Increased activity of hypoxia-inducible factor 1 is associated with early embryonic lethality in commd1 null mice
    • van de Sluis B, Muller P, Duran K, Chen A, Groot AJ, et al. (2007) Increased activity of hypoxia-inducible factor 1 is associated with early embryonic lethality in commd1 null mice. Mol Cell Biol 27: 4142-4156.
    • (2007) Mol Cell Biol , vol.27 , pp. 4142-4156
    • van de Sluis, B.1    Muller, P.2    Duran, K.3    Chen, A.4    Groot, A.J.5
  • 12
    • 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 2007
    • Semenza, G.L.1
  • 13
    • 0029051439 scopus 로고
    • Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension
    • Wang GL, Jiang BH, Rue EA, Semenza GL (1995) Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension. Proc Natl Acad Sci U S A 92: 5510-5514.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 5510-5514
    • Wang, G.L.1    Jiang, B.H.2    Rue, E.A.3    Semenza, G.L.4
  • 14
    • 0027427588 scopus 로고
    • Characterization of hypoxia-inducible factor 1 and regulation of DNA binding activity by hypoxia
    • Wang GL, Semenza GL (1993) Characterization of hypoxia-inducible factor 1 and regulation of DNA binding activity by hypoxia. J Biol Chem 268: 21513-21518.
    • (1993) J Biol Chem , vol.268 , pp. 21513-21518
    • Wang, G.L.1    Semenza, G.L.2
  • 15
    • 0035834409 scopus 로고    scopus 로고
    • A conserved family of prolyl-4-hydroxylases that modify HIF
    • Bruick RK, McKnight SL (2001) A conserved family of prolyl-4-hydroxylases that modify HIF. Science 294: 1337-1340.
    • (2001) Science , vol.294 , pp. 1337-1340
    • Bruick, R.K.1    McKnight, S.L.2
  • 16
    • 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
  • 17
    • 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
  • 18
    • 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
  • 19
    • 0025885693 scopus 로고
    • Functional analysis of an oxygen-regulated transcriptional enhancer lying 3′ to the mouse erythropoietin gene
    • Pugh CW, Tan CC, Jones RW, Ratcliffe PJ (1991) Functional analysis of an oxygen-regulated transcriptional enhancer lying 3′ to the mouse erythropoietin gene. Proc Natl Acad Sci U S A 88: 10553-10557.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 10553-10557
    • Pugh, C.W.1    Tan, C.C.2    Jones, R.W.3    Ratcliffe, P.J.4
  • 20
    • 34047215555 scopus 로고    scopus 로고
    • RACK1 vs. HSP90: Competition for HIF-1 alpha degradation vs. stabilization
    • Liu YV, Semenza GL (2007) RACK1 vs. HSP90: competition for HIF-1 alpha degradation vs. stabilization. Cell Cycle 6: 656-659.
    • (2007) Cell Cycle , vol.6 , pp. 656-659
    • Liu, Y.V.1    Semenza, G.L.2
  • 22
    • 0036810352 scopus 로고    scopus 로고
    • Heat-shock protein 90, a chaperone for folding and regulation
    • Picard D (2002) Heat-shock protein 90, a chaperone for folding and regulation. Cell Mol Life Sci 59: 1640-1648.
    • (2002) Cell Mol Life Sci , vol.59 , pp. 1640-1648
    • Picard, D.1
  • 23
    • 33744963443 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors repress the transactivation potential of hypoxia-inducible factors independently of direct acetylation of HIF-alpha
    • Fath DM, Kong X, Liang D, Lin Z, Chou A, et al. (2006) Histone deacetylase inhibitors repress the transactivation potential of hypoxia-inducible factors independently of direct acetylation of HIF-alpha. J Biol Chem 281: 13612-13619.
    • (2006) J Biol Chem , vol.281 , pp. 13612-13619
    • Fath, D.M.1    Kong, X.2    Liang, D.3    Lin, Z.4    Chou, A.5
  • 24
    • 0037119415 scopus 로고    scopus 로고
    • Hsp90 regulates a von Hippel Lindau-independent hypoxia-inducible factor-1 alpha-degradative pathway
    • Isaacs JS, Jung YJ, Mimnaugh EG, Martinez A, Cuttitta F, et al. (2002) Hsp90 regulates a von Hippel Lindau-independent hypoxia-inducible factor-1 alpha-degradative pathway. J Biol Chem 277: 29936-29944.
    • (2002) J Biol Chem , vol.277 , pp. 29936-29944
    • Isaacs, J.S.1    Jung, Y.J.2    Mimnaugh, E.G.3    Martinez, A.4    Cuttitta, F.5
  • 25
    • 33644780111 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors induce VHL and ubiquitin-independent proteasomal degradation of hypoxia-inducible factor 1alpha
    • Kong X, Lin Z, Liang D, Fath D, Sang N, et al. (2006) Histone deacetylase inhibitors induce VHL and ubiquitin-independent proteasomal degradation of hypoxia-inducible factor 1alpha. Mol Cell Biol 26: 2019-2028.
    • (2006) Mol Cell Biol , vol.26 , pp. 2019-2028
    • Kong, X.1    Lin, Z.2    Liang, D.3    Fath, D.4    Sang, N.5
  • 26
    • 33846254999 scopus 로고    scopus 로고
    • RACK1 competes with HSP90 for binding to HIF-1alpha and is required for O(2)-independent and HSP90 inhibitor-induced degradation of HIF-1alpha
    • Liu YV, Baek JH, Zhang H, Diez R, Cole RN, et al. (2007) RACK1 competes with HSP90 for binding to HIF-1alpha and is required for O(2)-independent and HSP90 inhibitor-induced degradation of HIF-1alpha. Mol Cell 25: 207-217.
    • (2007) Mol Cell , vol.25 , pp. 207-217
    • Liu, Y.V.1    Baek, J.H.2    Zhang, H.3    Diez, R.4    Cole, R.N.5
  • 27
    • 0036569704 scopus 로고    scopus 로고
    • Geldanamycin induces degradation of hypoxia-inducible factor 1alpha protein via the proteosome pathway in prostate cancer cells
    • Mabjeesh NJ, Post DE, Willard MT, Kaur B, Van Meir EG, et al. (2002) Geldanamycin induces degradation of hypoxia-inducible factor 1alpha protein via the proteosome pathway in prostate cancer cells. Cancer Res 62: 2478-2482.
    • (2002) Cancer Res , vol.62 , pp. 2478-2482
    • Mabjeesh, N.J.1    Post, D.E.2    Willard, M.T.3    Kaur, B.4    Van Meir, E.G.5
  • 28
    • 0032749463 scopus 로고    scopus 로고
    • Hypoxia-induced activation of HIF-1: Role of HIF-1alpha-Hsp90 interaction
    • Minet E, Mottet D, Michel G, Roland I, Raes M, et al. (1999) Hypoxia-induced activation of HIF-1: role of HIF-1alpha-Hsp90 interaction. FEBS Lett 460: 251-256.
    • (1999) FEBS Lett , vol.460 , pp. 251-256
    • Minet, E.1    Mottet, D.2    Michel, G.3    Roland, I.4    Raes, M.5
  • 29
    • 0023775756 scopus 로고
    • A Chinese hamster cell cycle mutant arrested at G2 phase has a temperature-sensitive ubiquitin-activating enzyme, E1
    • Kulka RG, Raboy B, Schuster R, Parag HA, Diamond G, et al. (1988) A Chinese hamster cell cycle mutant arrested at G2 phase has a temperature-sensitive ubiquitin-activating enzyme, E1. J Biol Chem 263: 15726-15731.
    • (1988) J Biol Chem , vol.263 , pp. 15726-15731
    • Kulka, R.G.1    Raboy, B.2    Schuster, R.3    Parag, H.A.4    Diamond, G.5
  • 30
    • 1842691021 scopus 로고    scopus 로고
    • PI3K/Akt is required for heat shock proteins to protect hypoxia-inducible factor 1alpha from pVHL-independent degradation
    • Zhou J, Schmid T, Frank R, Brune B (2004) PI3K/Akt is required for heat shock proteins to protect hypoxia-inducible factor 1alpha from pVHL-independent degradation. J Biol Chem 279: 13506-13513.
    • (2004) J Biol Chem , vol.279 , pp. 13506-13513
    • Zhou, J.1    Schmid, T.2    Frank, R.3    Brune, B.4
  • 31
    • 34447522124 scopus 로고    scopus 로고
    • Constitutive/hypoxic degradation of HIF-alpha proteins by the proteasome is independent of von Hippel Lindau protein ubiquitylation and the transactivation activity of the protein
    • Kong X, Alvarez-Castelao B, Lin Z, Castano JG, Caro J (2007) Constitutive/hypoxic degradation of HIF-alpha proteins by the proteasome is independent of von Hippel Lindau protein ubiquitylation and the transactivation activity of the protein. J Biol Chem 282: 15498-15505.
    • (2007) J Biol Chem , vol.282 , pp. 15498-15505
    • Kong, X.1    Alvarez-Castelao, B.2    Lin, Z.3    Castano, J.G.4    Caro, J.5
  • 32
    • 0035370123 scopus 로고    scopus 로고
    • Binding and regulation of HIF-1alpha by a subunit of the proteasome complex, PSMA7
    • Cho S, Choi YJ, Kim JM, Jeong ST, Kim JH, et al. (2001) Binding and regulation of HIF-1alpha by a subunit of the proteasome complex, PSMA7. FEBS Lett 498: 62-66.
    • (2001) FEBS Lett , vol.498 , pp. 62-66
    • Cho, S.1    Choi, Y.J.2    Kim, J.M.3    Jeong, S.T.4    Kim, J.H.5
  • 33
    • 0037443587 scopus 로고    scopus 로고
    • Levels of hypoxia-inducible factor-1alpha independently predict prognosis in patients with lymph node negative breast carcinoma
    • Bos R, van der Groep P, Greijer AE, Shvarts A, Meijer S, et al. (2003) Levels of hypoxia-inducible factor-1alpha independently predict prognosis in patients with lymph node negative breast carcinoma. Cancer 97: 1573-1581.
    • (2003) Cancer , vol.97 , pp. 1573-1581
    • Bos, R.1    van der Groep, P.2    Greijer, A.E.3    Shvarts, A.4    Meijer, S.5
  • 34
    • 33745303045 scopus 로고    scopus 로고
    • Hypoxia signalling in cancer and approaches to enforce tumour regression
    • Pouyssegur J, Dayan F, Mazure NM (2006) Hypoxia signalling in cancer and approaches to enforce tumour regression. Nature 441: 437-443.
    • (2006) Nature , vol.441 , pp. 437-443
    • Pouyssegur, J.1    Dayan, F.2    Mazure, N.M.3
  • 35
    • 35048875691 scopus 로고    scopus 로고
    • Evaluation of HIF-1 inhibitors as anticancer agents
    • Semenza GL (2007) Evaluation of HIF-1 inhibitors as anticancer agents. Drug Discov Today 12: 853-859.
    • (2007) Drug Discov Today , vol.12 , pp. 853-859
    • Semenza, G.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.