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Volumn 287, Issue 19, 2012, Pages 15996-16006

The chaperone-assisted E3 ligase C terminus of Hsc70-interacting protein (CHIP) targets PTEN for proteasomal degradation

Author keywords

[No Author keywords available]

Indexed keywords

C TERMINUS; CELLULAR PROCESS; COMPLEX MODES; DEGRADATION PATHWAYS; DOWN-REGULATION; E3 LIGASE; HUMAN PROSTATE CANCER; INVERSE CORRELATION; MOLECULAR CHAPERONES; N-TERMINAL DOMAINS; OVER-EXPRESSION; PROTEASOMAL DEGRADATION; TUMOR SUPPRESSORS; UBIQUITIN-PROTEASOME SYSTEM; UBIQUITINATION;

EID: 84860874770     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.321083     Document Type: Article
Times cited : (130)

References (57)
  • 7
    • 0142011466 scopus 로고    scopus 로고
    • PTEN: From pathology to biology
    • DOI 10.1016/S0962-8924(03)00175-2
    • Sulis, M. L., and Parsons, R. (2003) PTEN: from pathology to biology. Trends Cell Biol. 13, 478-483 (Pubitemid 37289398)
    • (2003) Trends in Cell Biology , vol.13 , Issue.9 , pp. 478-483
    • Sulis, M.L.1    Parsons, R.2
  • 8
    • 0034912744 scopus 로고    scopus 로고
    • PTEN and myotubularin: Novel phosphoinositide phosphatases
    • DOI 10.1146/annurev.biochem.70.1.247
    • Maehama, T., Taylor, G. S., and Dixon, J. E. (2001) PTEN and myotubularin: novel phosphoinositide phosphatases. Annu. Rev. Biochem. 70, 247-279 (Pubitemid 32662211)
    • (2001) Annual Review of Biochemistry , vol.70 , pp. 247-279
    • Maehama, T.1    Taylor, G.S.2    Dixon, J.E.3
  • 9
    • 40549118822 scopus 로고    scopus 로고
    • The nuclear affairs of PTEN
    • DOI 10.1242/jcs.022459
    • Planchon, S. M., Waite, K. A., and Eng, C. (2008) The nuclear affairs of PTEN. J. Cell Sci. 121, 249-253 (Pubitemid 351356695)
    • (2008) Journal of Cell Science , vol.121 , Issue.3 , pp. 249-253
    • Planchon, S.M.1    Waite, K.A.2    Eng, C.3
  • 10
    • 33845999615 scopus 로고    scopus 로고
    • Essential Role for Nuclear PTEN in Maintaining Chromosomal Integrity
    • DOI 10.1016/j.cell.2006.11.042, PII S0092867406015534
    • Shen, W. H., Balajee, A. S., Wang, J., Wu, H., Eng, C., Pandolfi, P. P., and Yin, Y. (2007) Essential role for nuclear PTEN in maintaining chromosomal integrity. Cell 128, 157-170 (Pubitemid 46048887)
    • (2007) Cell , vol.128 , Issue.1 , pp. 157-170
    • Shen, W.H.1    Balajee, A.S.2    Wang, J.3    Wu, H.4    Eng, C.5    Pandolfi, P.P.6    Yin, Y.7
  • 11
    • 33646376411 scopus 로고    scopus 로고
    • Pten dependence distinguishes haematopoietic stem cells from leukaemia-initiating cells
    • DOI 10.1038/nature04703, PII NATURE04703
    • Yilmaz, O. H., Valdez, R., Theisen, B. K., Guo, W., Ferguson, D. O., Wu, H., and Morrison, S. J. (2006) PTEN dependence distinguishes haematopoietic stem cells from leukaemia-initiating cells. Nature 441, 475-482 (Pubitemid 44050144)
    • (2006) Nature , vol.441 , Issue.7092 , pp. 475-482
    • Yilmaz, O.H.1    Valdez, R.2    Theisen, B.K.3    Guo, W.4    Ferguson, D.O.5    Wu, H.6    Morrison, S.J.7
  • 14
    • 38349030742 scopus 로고    scopus 로고
    • New insights into PTEN
    • Tamguney, T., and Stokoe, D. (2007) New insights into PTEN. J. Cell Sci. 120, 4071-4079
    • (2007) J. Cell Sci. , vol.120 , pp. 4071-4079
    • Tamguney, T.1    Stokoe, D.2
  • 15
    • 51849155581 scopus 로고    scopus 로고
    • Post-translational regulation of PTEN
    • Wang, X., and Jiang, X. (2008) Post-translational regulation of PTEN. Oncogene 27, 5454-5463
    • (2008) Oncogene , vol.27 , pp. 5454-5463
    • Wang, X.1    Jiang, X.2
  • 19
    • 68949121012 scopus 로고    scopus 로고
    • X-linked inhibitor of apoptosis protein (XIAP) regulates PTEN ubiquitination, content, and compartmentalization
    • Van Themsche, C., Leblanc, V., Parent, S., and Asselin, E. (2009) X-linked inhibitor of apoptosis protein (XIAP) regulates PTEN ubiquitination, content, and compartmentalization. J. Biol. Chem. 284, 20462-20466
    • (2009) J. Biol. Chem. , vol.284 , pp. 20462-20466
    • Van Themsche, C.1    Leblanc, V.2    Parent, S.3    Asselin, E.4
  • 21
    • 0030965946 scopus 로고    scopus 로고
    • Regulation of p53 stability by Mdm2
    • DOI 10.1038/387299a0
    • Kubbutat, M. H., Jones, S. N., and Vousden, K. H. (1997) Regulation of p53 stability by Mdm2. Nature 387, 299-303 (Pubitemid 27220767)
    • (1997) Nature , vol.387 , Issue.6630 , pp. 299-303
    • Kubbutat, M.H.G.1    Jones, S.N.2    Vousden, K.H.3
  • 22
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • DOI 10.1038/387296a0
    • Haupt, Y., Maya, R., Kazaz, A., and Oren, M. (1997) Mdm2 promotes the rapid degradation of p53. Nature 387, 296-299 (Pubitemid 27220766)
    • (1997) Nature , vol.387 , Issue.6630 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 24
    • 0037459377 scopus 로고    scopus 로고
    • Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53 degradation
    • DOI 10.1016/S0092-8674(03)00193-4
    • Leng, R. P., Lin, Y., Ma, W., Wu, H., Lemmers, B., Chung, S., Parant, J. M., Lozano, G., Hakem, R., and Benchimol, S. (2003) Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53 degradation. Cell 112, 779-791 (Pubitemid 36378882)
    • (2003) Cell , vol.112 , Issue.6 , pp. 779-791
    • Leng, R.P.1    Lin, Y.2    Ma, W.3    Wu, H.4    Lemmers, B.5    Chung, S.6    Parant, J.M.7    Lozano, G.8    Hakem, R.9    Benchimol, S.10
  • 26
    • 0033013126 scopus 로고    scopus 로고
    • Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions
    • Ballinger, C. A., Connell, P., Wu, Y., Hu, Z., Thompson, L. J., Yin, L. Y., and Patterson, C. (1999) Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. Mol. Cell. Biol. 19, 4535-4545 (Pubitemid 29242026)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.6 , pp. 4535-4545
    • Ballinger, C.A.1    Connell, P.2    Wu, Y.3    Hu, Z.4    Thompson, L.J.5    Yin, L.-Y.6    Patterson, C.7
  • 28
    • 0035900793 scopus 로고    scopus 로고
    • CHIP is a U-box-dependent E3 ubiquitin ligase: Identification of Hsc70 as a target for ubiquitylation
    • Jiang, J., Ballinger, C. A., Wu, Y., Dai, Q., Cyr, D. M., Höhfeld, J., and Patterson, C. (2001) CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation. J. Biol. Chem. 276, 42938-42944
    • (2001) J. Biol. Chem. , vol.276 , pp. 42938-42944
    • Jiang, J.1    Ballinger, C.A.2    Wu, Y.3    Dai, Q.4    Cyr, D.M.5    Höhfeld, J.6    Patterson, C.7
  • 29
    • 0035684430 scopus 로고    scopus 로고
    • CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein
    • DOI 10.1093/embo-reports/kve246
    • Murata, S., Minami, Y., Minami, M., Chiba, T., and Tanaka, K. (2001) CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein. EMBO Rep. 2, 1133-1138 (Pubitemid 34055961)
    • (2001) EMBO Reports , vol.2 , Issue.12 , pp. 1133-1138
    • Murata, S.1    Minami, Y.2    Minami, M.3    Chiba, T.4    Tanaka, K.5
  • 30
    • 0035899897 scopus 로고    scopus 로고
    • Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling
    • DOI 10.1016/S0960-9822(01)00487-0
    • Demand, J., Alberti, S., Patterson, C., and Höhfeld, J. (2001) Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling. Curr. Biol. 11, 1569-1577 (Pubitemid 32978521)
    • (2001) Current Biology , vol.11 , Issue.20 , pp. 1569-1577
    • Demand, J.1    Alberti, S.2    Patterson, C.3    Hohfeld, J.4
  • 31
    • 0035146685 scopus 로고    scopus 로고
    • The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins
    • DOI 10.1038/35050618
    • Connell, P., Ballinger, C. A., Jiang, J., Wu, Y., Thompson, L. J., Höhfeld, J., and Patterson, C. (2001) The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins. Nat. Cell Biol. 3, 93-96 (Pubitemid 32114838)
    • (2001) Nature Cell Biology , vol.3 , Issue.1 , pp. 93-96
    • Connell, P.1    Ballinger, C.A.2    Jiang, J.3    Wu, Y.4    Thompson, L.J.5    Hohfeld, J.6    Patterson, C.7
  • 32
    • 0035142877 scopus 로고    scopus 로고
    • The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
    • DOI 10.1038/35050509
    • Meacham, G. C., Patterson, C., Zhang, W., Younger, J. M., and Cyr, D. M. (2001) The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nat. Cell Biol. 3, 100-105 (Pubitemid 32114840)
    • (2001) Nature Cell Biology , vol.3 , Issue.1 , pp. 100-105
    • Meacham, G.C.1    Patterson, C.2    Zhang, W.3    Younger, J.M.4    Cyr, D.M.5
  • 33
    • 4344578534 scopus 로고    scopus 로고
    • The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator
    • DOI 10.1091/mbc.E04-04-0293
    • Alberti, S., Böhse, K., Arndt, V., Schmitz, A., and Höhfeld, J. (2004) The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator. Mol. Biol. Cell 15, 4003-4010 (Pubitemid 39122006)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.9 , pp. 4003-4010
    • Alberti, S.1    Bohse, K.2    Arndt, V.3    Schmitz, A.4    Hohfeld, J.5
  • 34
    • 1042266624 scopus 로고    scopus 로고
    • CHIP-Hsc70 Complex Ubiquitinates Phosphorylated Tau and Enhances Cell Survival
    • DOI 10.1074/jbc.M305838200
    • Shimura, H., Schwartz, D., Gygi, S. P., and Kosik, K. S. (2004) CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival. J. Biol. Chem. 279, 4869-4876 (Pubitemid 38199082)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.6 , pp. 4869-4876
    • Shimura, H.1    Schwartz, D.2    Gygi, S.P.3    Kosik, K.S.4
  • 36
    • 0036789884 scopus 로고    scopus 로고
    • Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu
    • Xu, W., Marcu, M., Yuan, X., Mimnaugh, E., Patterson, C., and Neckers, L. (2002) Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu. Proc. Natl. Acad. Sci. U.S.A. 99, 12847-12852
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 12847-12852
    • Xu, W.1    Marcu, M.2    Yuan, X.3    Mimnaugh, E.4    Patterson, C.5    Neckers, L.6
  • 37
    • 77950473770 scopus 로고    scopus 로고
    • Hsp70 and CHIP selectively mediate ubiquitination and degradation of hypoxia-inducible factor (HIF)-1α but Not HIF-2α
    • Luo, W., Zhong, J., Chang, R., Hu, H., Pandey, A., and Semenza, G. L. (2010) Hsp70 and CHIP selectively mediate ubiquitination and degradation of hypoxia-inducible factor (HIF)-1α but Not HIF-2α. J. Biol. Chem. 285, 3651-3663
    • (2010) J. Biol. Chem. , vol.285 , pp. 3651-3663
    • Luo, W.1    Zhong, J.2    Chang, R.3    Hu, H.4    Pandey, A.5    Semenza, G.L.6
  • 38
    • 28144439277 scopus 로고    scopus 로고
    • CHIP (carboxyl terminus of Hsc70-interacting protein) promotes basal and geldanamycin-induced degradation of estrogen receptor-α
    • DOI 10.1210/me.2005-0111
    • Fan, M., Park, A., and Nephew, K. P. (2005) CHIP (carboxyl terminus of Hsc70-interacting protein) promotes basal and geldanamycin-induced degradation of estrogen receptor-alpha. Mol. Endocrinol. 19, 2901-2914 (Pubitemid 41697710)
    • (2005) Molecular Endocrinology , vol.19 , Issue.12 , pp. 2901-2914
    • Fan, M.1    Park, A.2    Nephew, K.P.3
  • 39
    • 78650632231 scopus 로고    scopus 로고
    • CHIP promotes human telomerase reverse transcriptase degradation and negatively regulates telomerase activity
    • Lee, J. H., Khadka, P., Baek, S. H., and Chung, I. K. (2010) CHIP promotes human telomerase reverse transcriptase degradation and negatively regulates telomerase activity. J. Biol. Chem. 285, 42033-42045
    • (2010) J. Biol. Chem. , vol.285 , pp. 42033-42045
    • Lee, J.H.1    Khadka, P.2    Baek, S.H.3    Chung, I.K.4
  • 40
    • 22844447871 scopus 로고    scopus 로고
    • The chaperone-associated ubiquitin ligase CHIP is able to target p53 for proteasomal degradation
    • DOI 10.1074/jbc.M501574200
    • Esser, C., Scheffner, M., and Höhfeld, J. (2005) The chaperone-associated ubiquitin ligase CHIP is able to target p53 for proteasomal degradation. J. Biol. Chem. 280, 27443-27448 (Pubitemid 41040787)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.29 , pp. 27443-27448
    • Esser, C.1    Scheffner, M.2    Hohfeld, J.3
  • 42
    • 78650938218 scopus 로고    scopus 로고
    • Docking-dependent ubiquitination of the interferon regulatory factor-1 tumor suppressor protein by the ubiquitin ligase CHIP
    • Narayan, V., Pion, E., Landré, V., Müller, P., and Ball, K. L. (2011) Docking-dependent ubiquitination of the interferon regulatory factor-1 tumor suppressor protein by the ubiquitin ligase CHIP. J. Biol. Chem. 286, 607-619
    • (2011) J. Biol. Chem. , vol.286 , pp. 607-619
    • Narayan, V.1    Pion, E.2    Landré, V.3    Müller, P.4    Ball, K.L.5
  • 44
    • 1642576077 scopus 로고    scopus 로고
    • Dimerization of the Human E3 Ligase CHIP via a Coiled-coil Domain Is Essential for Its Activity
    • DOI 10.1074/jbc.M311112200
    • Nikolay, R., Wiederkehr, T., Rist, W., Kramer, G., Mayer, M. P., and Bukau, B. (2004) Dimerization of the human E3 ligase CHIP via a coiled-coil domain is essential for its activity. J. Biol. Chem. 279, 2673-2678 (Pubitemid 38114255)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.4 , pp. 2673-2678
    • Nikolay, R.1    Wiederkehr, T.2    Rist, W.3    Kramer, G.4    Mayer, M.P.5    Bukau, B.6
  • 45
    • 0042671234 scopus 로고    scopus 로고
    • 0 cells
    • DOI 10.1016/S1097-2765(03)00225-9
    • Ghosh, M. K., and Harter, M. L. (2003) A viral mechanism for remodeling chromatin structure in G0 cells. Mol. Cell 12, 255-260 (Pubitemid 36945049)
    • (2003) Molecular Cell , vol.12 , Issue.1 , pp. 255-260
    • Ghosh, M.K.1    Harter, M.L.2
  • 46
    • 28244469041 scopus 로고    scopus 로고
    • Redox regulation of the nutrient-sensitive raptor-mTOR pathway and complex
    • DOI 10.1074/jbc.M506096200
    • Sarbassov, D. D., and Sabatini, D. M. (2005) Redox regulation of the nutrient-sensitive raptor-mTOR pathway and complex. J. Biol. Chem. 280, 39505-39509 (Pubitemid 41713908)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.47 , pp. 39505-39509
    • Sarbassov, D.D.1    Sabatini, D.M.2
  • 47
    • 27744535984 scopus 로고    scopus 로고
    • PI3K-AKT pathway negatively controls EGFR-dependent DNA-binding activity of Stat3 in glioblastoma multiforme cells
    • DOI 10.1038/sj.onc.1208894, PII 1208894
    • Ghosh, M. K., Sharma, P., Harbor, P. C., Rahaman, S. O., and Haque, S. J. (2005) PI3K-AKT pathway negatively controls EGFR-dependent DNA binding activity of Stat3 in glioblastoma multiforme cells. Oncogene 24, 7290-7300 (Pubitemid 41622233)
    • (2005) Oncogene , vol.24 , Issue.49 , pp. 7290-7300
    • Ghosh, M.K.1    Sharma, P.2    Harbor, P.C.3    Rahaman, S.O.4    Haque, S.J.5
  • 48
    • 77950508409 scopus 로고    scopus 로고
    • E1A interacts with two opposing transcriptional pathways to induce quiescent cells into S phase
    • Sha, J., Ghosh, M. K., Zhang, K., and Harter, M. L. (2010) E1A interacts with two opposing transcriptional pathways to induce quiescent cells into S phase. J. Virol. 84, 4050-4059
    • (2010) J. Virol. , vol.84 , pp. 4050-4059
    • Sha, J.1    Ghosh, M.K.2    Zhang, K.3    Harter, M.L.4
  • 49
    • 0024514688 scopus 로고
    • A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
    • Chau, V., Tobias, J. W., Bachmair, A., Marriott, D., Ecker, D. J., Gonda, D. K., and Varshavsky, A. (1989) A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein. Science 243, 1576-1583 (Pubitemid 19090506)
    • (1989) Science , vol.243 , Issue.4898 , pp. 1576-1583
    • Chau, V.1    Tobias, J.W.2    Bachmair, A.3    Marriott, D.4    Ecker, D.J.5    Gonda, D.K.6    Varshavsky, A.7
  • 50
    • 59649086030 scopus 로고    scopus 로고
    • Nonproteolytic functions of ubiquitin in cell signaling
    • Chen, Z. J., and Sun, L. J. (2009) Nonproteolytic functions of ubiquitin in cell signaling. Mol. Cell 33, 275-286
    • (2009) Mol. Cell , vol.33 , pp. 275-286
    • Chen, Z.J.1    Sun, L.J.2
  • 52
    • 73449085831 scopus 로고    scopus 로고
    • PTEN-mediated G1 cell-cycle arrest in LNCaP prostate cancer cells is associated with altered expression of cell-cycle regulators
    • van Duijn, P. W., Ziel-van der Made, A. C., van der Korput, J. A., and Trapman, J. (2010) PTEN-mediated G1 cell-cycle arrest in LNCaP prostate cancer cells is associated with altered expression of cell-cycle regulators. Prostate 70, 135-146
    • (2010) Prostate , vol.70 , pp. 135-146
    • Van Duijn, P.W.1    Ziel-van Der Made, A.C.2    Van Der Korput, J.A.3    Trapman, J.4
  • 53
    • 77954374206 scopus 로고    scopus 로고
    • PTEN regulates angiogenesis and VEGF expression through phosphatase-dependent and -independent mechanisms in HepG2 cells
    • Tian, T., Nan, K. J., Wang, S. H., Liang, X., Lu, C. X., Guo, H., Wang, W. J., and Ruan, Z. P. (2010) PTEN regulates angiogenesis and VEGF expression through phosphatase-dependent and -independent mechanisms in HepG2 cells. Carcinogenesis 31, 1211-1219
    • (2010) Carcinogenesis , vol.31 , pp. 1211-1219
    • Tian, T.1    Nan, K.J.2    Wang, S.H.3    Liang, X.4    Lu, C.X.5    Guo, H.6    Wang, W.J.7    Ruan, Z.P.8
  • 56
    • 79954930813 scopus 로고    scopus 로고
    • Carboxyl terminus of Hsp70-interacting protein (CHIP) contributes to human glioma oncogenesis
    • Xu, T., Zhou, Q., Zhou, J., Huang, Y., Yan, Y., Li, W., Wang, C., Hu, G., Lu, Y., and Chen, J. (2011) Carboxyl terminus of Hsp70-interacting protein (CHIP) contributes to human glioma oncogenesis. Cancer Sci. 102, 959-966
    • (2011) Cancer Sci. , vol.102 , pp. 959-966
    • Xu, T.1    Zhou, Q.2    Zhou, J.3    Huang, Y.4    Yan, Y.5    Li, W.6    Wang, C.7    Hu, G.8    Lu, Y.9    Chen, J.10
  • 57
    • 67449164600 scopus 로고    scopus 로고
    • Endogenous tumor suppression mediated by PTEN involves survivin gene silencing
    • Guha, M., Plescia, J., Leav, I., Li, J., Languino, L. R., and Altieri, D. C. (2009) Endogenous tumor suppression mediated by PTEN involves survivin gene silencing. Cancer Res. 69, 4954-4958
    • (2009) Cancer Res. , vol.69 , pp. 4954-4958
    • Guha, M.1    Plescia, J.2    Leav, I.3    Li, J.4    Languino, L.R.5    Altieri, D.C.6


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