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Volumn 50, Issue 1, 2011, Pages 157-165

CHIP-dependent p53 regulation occurs specifically during cellular senescence

Author keywords

Aging; CHIP ligase; Degradation; Free radicals; p53; Replicative senescence; Ubiquitin proteasome system

Indexed keywords

CHAPERONE; PROTEIN CHIP; PROTEIN MDM2; PROTEIN P53; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 78650682540     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2010.10.701     Document Type: Article
Times cited : (26)

References (62)
  • 1
    • 0035059672 scopus 로고    scopus 로고
    • From cells to organisms: Can we learn about aging from cells in culture?
    • J. Campisi From cells to organisms: can we learn about aging from cells in culture? Exp. Gerontol. 36 2001 607 618
    • (2001) Exp. Gerontol. , vol.36 , pp. 607-618
    • Campisi, J.1
  • 2
    • 34447543913 scopus 로고    scopus 로고
    • Cellular senescence in cancer and aging
    • M. Collado, M.A. Blasco, and M. Serrano Cellular senescence in cancer and aging Cell 130 2007 223 233
    • (2007) Cell , vol.130 , pp. 223-233
    • Collado, M.1    Blasco, M.A.2    Serrano, M.3
  • 3
    • 0030944985 scopus 로고    scopus 로고
    • Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a
    • M. Serrano, A.W. Lin, M.E. McCurrach, D. Beach, and S.W. Lowe Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a Cell 88 1997 593 602
    • (1997) Cell , vol.88 , pp. 593-602
    • Serrano, M.1    Lin, A.W.2    McCurrach, M.E.3    Beach, D.4    Lowe, S.W.5
  • 5
    • 0042346327 scopus 로고    scopus 로고
    • Central role of the proteasome in senescence and survival of human fibroblasts: Induction of a senescence-like phenotype upon its inhibition and resistance to stress upon its activation
    • N. Chondrogianni, F.L. Stratford, I.P. Trougakos, B. Friguet, A.J. Rivett, and E.S. Gonos Central role of the proteasome in senescence and survival of human fibroblasts: induction of a senescence-like phenotype upon its inhibition and resistance to stress upon its activation J. Biol. Chem. 278 2003 28026 28037
    • (2003) J. Biol. Chem. , vol.278 , pp. 28026-28037
    • Chondrogianni, N.1    Stratford, F.L.2    Trougakos, I.P.3    Friguet, B.4    Rivett, A.J.5    Gonos, E.S.6
  • 6
    • 52449107748 scopus 로고    scopus 로고
    • Partial proteasome inhibition in human fibroblasts triggers accelerated M1 senescence or M2 crisis depending on p53 and Rb status
    • N. Chondrogianni, I.P. Trougakos, D. Kletsas, Q.M. Chen, and E.S. Gonos Partial proteasome inhibition in human fibroblasts triggers accelerated M1 senescence or M2 crisis depending on p53 and Rb status Aging Cell 7 2008 717 732
    • (2008) Aging Cell , vol.7 , pp. 717-732
    • Chondrogianni, N.1    Trougakos, I.P.2    Kletsas, D.3    Chen, Q.M.4    Gonos, E.S.5
  • 7
    • 0035370483 scopus 로고    scopus 로고
    • Regulation and function of the p53 tumor suppressor protein
    • K.M. Ryan, A.C. Phillips, and K.H. Vousden Regulation and function of the p53 tumor suppressor protein Curr. Opin. Cell Biol. 13 2001 332 337
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 332-337
    • Ryan, K.M.1    Phillips, A.C.2    Vousden, K.H.3
  • 9
    • 0030609861 scopus 로고    scopus 로고
    • Bypass of senescence after disruption of p21CIP1/WAF1 gene in normal diploid human fibroblasts
    • J.P. Brown, W. Wei, and J.M. Sedivy Bypass of senescence after disruption of p21CIP1/WAF1 gene in normal diploid human fibroblasts Science 277 1997 831 834
    • (1997) Science , vol.277 , pp. 831-834
    • Brown, J.P.1    Wei, W.2    Sedivy, J.M.3
  • 12
    • 43949107925 scopus 로고    scopus 로고
    • SnapShot: P53 posttranslational modifications
    • 930
    • Kruse J.P., and Gu W. SnapShot: p53 posttranslational modifications Cell 133 930-930 2008 e931
    • (2008) Cell , vol.133 , Issue.930
    • Kruse, J.P.1    Gu, W.2
  • 14
    • 0037329056 scopus 로고    scopus 로고
    • The p53-Mdm2 module and the ubiquitin system
    • D. Michael, and M. Oren The p53-Mdm2 module and the ubiquitin system Semin. Cancer Biol. 13 2003 49 58
    • (2003) Semin. Cancer Biol. , vol.13 , pp. 49-58
    • Michael, D.1    Oren, M.2
  • 19
    • 22844447871 scopus 로고    scopus 로고
    • The chaperone-associated ubiquitin ligase CHIP is able to target p53 for proteasomal degradation
    • C. Esser, M. Scheffner, and J. Hohfeld The chaperone-associated ubiquitin ligase CHIP is able to target p53 for proteasomal degradation J. Biol. Chem. 280 2005 27443 27448
    • (2005) J. Biol. Chem. , vol.280 , pp. 27443-27448
    • Esser, C.1    Scheffner, M.2    Hohfeld, J.3
  • 20
    • 35348941129 scopus 로고    scopus 로고
    • CHIP chaperones wild type p53 tumor suppressor protein
    • V. Tripathi, A. Ali, R. Bhat, and U. Pati CHIP chaperones wild type p53 tumor suppressor protein J. Biol. Chem. 282 2007 28441 28454
    • (2007) J. Biol. Chem. , vol.282 , pp. 28441-28454
    • Tripathi, V.1    Ali, A.2    Bhat, R.3    Pati, U.4
  • 21
    • 0037401714 scopus 로고    scopus 로고
    • CHIP: A quality-control E3 ligase collaborating with molecular chaperones
    • S. Murata, T. Chiba, and K. Tanaka CHIP: a quality-control E3 ligase collaborating with molecular chaperones Int. J. Biochem. Cell Biol. 35 2003 572 578
    • (2003) Int. J. Biochem. Cell Biol. , vol.35 , pp. 572-578
    • Murata, S.1    Chiba, T.2    Tanaka, K.3
  • 22
    • 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
    • C.A. Ballinger, P. Connell, Y. Wu, Z. Hu, L.J. Thompson, L.Y. Yin, and C. Patterson Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions Mol. Cell. Biol. 19 1999 4535 4545
    • (1999) Mol. Cell. Biol. , vol.19 , 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
  • 23
    • 4344578534 scopus 로고    scopus 로고
    • The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator
    • S. Alberti, K. Bohse, V. Arndt, A. Schmitz, and J. Hohfeld The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator Mol. Biol. Cell 15 2004 4003 4010
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4003-4010
    • Alberti, S.1    Bohse, K.2    Arndt, V.3    Schmitz, A.4    Hohfeld, J.5
  • 24
    • 23144443884 scopus 로고    scopus 로고
    • Protein quality control: Chaperones culling corrupt conformations
    • A.J. McClellan, S. Tam, D. Kaganovich, and J. Frydman Protein quality control: chaperones culling corrupt conformations Nat. Cell Biol. 7 2005 736 741
    • (2005) Nat. Cell Biol. , vol.7 , pp. 736-741
    • McClellan, A.J.1    Tam, S.2    Kaganovich, D.3    Frydman, J.4
  • 25
    • 33646255923 scopus 로고    scopus 로고
    • The triage of damaged proteins: Degradation by the ubiquitin-proteasome pathway or repair by molecular chaperones
    • C. Marques, W. Guo, P. Pereira, A. Taylor, C. Patterson, P.C. Evans, and F. Shang The triage of damaged proteins: degradation by the ubiquitin-proteasome pathway or repair by molecular chaperones FASEB J. 20 2006 741 743
    • (2006) FASEB J. , vol.20 , pp. 741-743
    • Marques, C.1    Guo, W.2    Pereira, P.3    Taylor, A.4    Patterson, C.5    Evans, P.C.6    Shang, F.7
  • 26
    • 0035900793 scopus 로고    scopus 로고
    • CHIP is a U-box-dependent E3 ubiquitin ligase: Identification of Hsc70 as a target for ubiquitylation
    • J. Jiang, C.A. Ballinger, Y. Wu, Q. Dai, D.M. Cyr, J. Hohfeld, and C. Patterson CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation J. Biol. Chem. 276 2001 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    Hohfeld, J.6    Patterson, C.7
  • 27
    • 1242291789 scopus 로고    scopus 로고
    • CHIP: A link between the chaperone and proteasome systems
    • H. McDonough, and C. Patterson CHIP: a link between the chaperone and proteasome systems Cell Stress Chaperones 8 2003 303 308
    • (2003) Cell Stress Chaperones , vol.8 , pp. 303-308
    • McDonough, H.1    Patterson, C.2
  • 29
    • 15744387323 scopus 로고    scopus 로고
    • Co-chaperone CHIP associates with expanded polyglutamine protein and promotes their degradation by proteasomes
    • N.R. Jana, P. Dikshit, A. Goswami, S. Kotliarova, S. Murata, K. Tanaka, and N. Nukina Co-chaperone CHIP associates with expanded polyglutamine protein and promotes their degradation by proteasomes J. Biol. Chem. 280 2005 11635 11640
    • (2005) J. Biol. Chem. , vol.280 , pp. 11635-11640
    • Jana, N.R.1    Dikshit, P.2    Goswami, A.3    Kotliarova, S.4    Murata, S.5    Tanaka, K.6    Nukina, N.7
  • 30
    • 0035142877 scopus 로고    scopus 로고
    • The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
    • G.C. Meacham, C. Patterson, W. Zhang, J.M. Younger, and D.M. Cyr The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation Nat. Cell Biol. 3 2001 100 105
    • (2001) Nat. Cell Biol. , vol.3 , pp. 100-105
    • Meacham, G.C.1    Patterson, C.2    Zhang, W.3    Younger, J.M.4    Cyr, D.M.5
  • 31
    • 58149465766 scopus 로고    scopus 로고
    • A critical role for CHIP in the aggresome pathway
    • Y. Sha, L. Pandit, S. Zeng, and N.T. Eissa A critical role for CHIP in the aggresome pathway Mol. Cell. Biol. 29 2009 116 128
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 116-128
    • Sha, Y.1    Pandit, L.2    Zeng, S.3    Eissa, N.T.4
  • 33
    • 0038701745 scopus 로고    scopus 로고
    • Regulation of aging and age-related disease by DAF-16 and heat-shock factor
    • A.L. Hsu, C.T. Murphy, and C. Kenyon Regulation of aging and age-related disease by DAF-16 and heat-shock factor Science 300 2003 1142 1145
    • (2003) Science , vol.300 , pp. 1142-1145
    • Hsu, A.L.1    Murphy, C.T.2    Kenyon, C.3
  • 35
    • 44949127204 scopus 로고    scopus 로고
    • CHIP deficiency decreases longevity, with accelerated aging phenotypes accompanied by altered protein quality control
    • J.N. Min, R.A. Whaley, N.E. Sharpless, P. Lockyer, A.L. Portbury, and C. Patterson CHIP deficiency decreases longevity, with accelerated aging phenotypes accompanied by altered protein quality control Mol. Cell. Biol. 28 2008 4018 4025
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 4018-4025
    • Min, J.N.1    Whaley, R.A.2    Sharpless, N.E.3    Lockyer, P.4    Portbury, A.L.5    Patterson, C.6
  • 36
    • 27944510125 scopus 로고    scopus 로고
    • Proteasome dysfunction in mammalian aging: Steps and factors involved
    • N. Chondrogianni, and E.S. Gonos Proteasome dysfunction in mammalian aging: steps and factors involved Exp. Gerontol. 40 2005 931 938
    • (2005) Exp. Gerontol. , vol.40 , pp. 931-938
    • Chondrogianni, N.1    Gonos, E.S.2
  • 37
    • 64949135819 scopus 로고    scopus 로고
    • Does damage to DNA and other macromolecules play a role in aging? if so, how?
    • J. Campisi, and J. Vijg Does damage to DNA and other macromolecules play a role in aging? If so, how? J. Gerontol. A Biol. Sci. Med. Sci. 64 2009 175 178
    • (2009) J. Gerontol. A Biol. Sci. Med. Sci. , vol.64 , pp. 175-178
    • Campisi, J.1    Vijg, J.2
  • 38
    • 64949099855 scopus 로고    scopus 로고
    • Protein homeostasis and aging: Taking care of proteins from the cradle to the grave
    • R.I. Morimoto, and A.M. Cuervo Protein homeostasis and aging: taking care of proteins from the cradle to the grave J. Gerontol. A Biol. Sci. Med. Sci. 64 2009 167 170
    • (2009) J. Gerontol. A Biol. Sci. Med. Sci. , vol.64 , pp. 167-170
    • Morimoto, R.I.1    Cuervo, A.M.2
  • 39
    • 64949116972 scopus 로고    scopus 로고
    • Cell stress and aging: New emphasis on multiplex resistance mechanisms
    • Miller R.A. Cell stress and aging: new emphasis on multiplex resistance mechanisms J. Gerontol. A Biol. Sci. Med. Sci. 64 2009 179 182
    • (2009) J. Gerontol. A Biol. Sci. Med. Sci. , vol.64 , pp. 179-182
    • Miller, R.A.1
  • 40
    • 0025827637 scopus 로고
    • Regulation of extracellular matrix production by chemically synthesized subfragments of type i collagen carboxy propeptide
    • K. Katayama, J.M. Seyer, R. Raghow, and A.H. Kang Regulation of extracellular matrix production by chemically synthesized subfragments of type I collagen carboxy propeptide Biochemistry 30 1991 7097 7104
    • (1991) Biochemistry , vol.30 , pp. 7097-7104
    • Katayama, K.1    Seyer, J.M.2    Raghow, R.3    Kang, A.H.4
  • 43
    • 0035857092 scopus 로고    scopus 로고
    • Role of cyclin-dependent kinase inhibitors in the growth arrest at senescence in human prostate epithelial and uroepithelial cells
    • S.R. Schwarze, Y. Shi, V.X. Fu, P.A. Watson, and D.F. Jarrard Role of cyclin-dependent kinase inhibitors in the growth arrest at senescence in human prostate epithelial and uroepithelial cells Oncogene 20 2001 8184 8192
    • (2001) Oncogene , vol.20 , pp. 8184-8192
    • Schwarze, S.R.1    Shi, Y.2    Fu, V.X.3    Watson, P.A.4    Jarrard, D.F.5
  • 44
    • 10344260912 scopus 로고    scopus 로고
    • Loss of proliferative capacity and induction of senescence in oxidatively stressed human fibroblasts
    • J.H. Chen, K. Stoeber, S. Kingsbury, S.E. Ozanne, G.H. Williams, and C.N. Hales Loss of proliferative capacity and induction of senescence in oxidatively stressed human fibroblasts J. Biol. Chem. 279 2004 49439 49446
    • (2004) J. Biol. Chem. , vol.279 , pp. 49439-49446
    • Chen, J.H.1    Stoeber, K.2    Kingsbury, S.3    Ozanne, S.E.4    Williams, G.H.5    Hales, C.N.6
  • 45
    • 1842789948 scopus 로고    scopus 로고
    • Proteasome inhibition induces a senescence-like phenotype in primary human fibroblasts cultures
    • N. Chondrogianni, and E.S. Gonos Proteasome inhibition induces a senescence-like phenotype in primary human fibroblasts cultures Biogerontology 5 2004 55 61
    • (2004) Biogerontology , vol.5 , pp. 55-61
    • Chondrogianni, N.1    Gonos, E.S.2
  • 47
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
    • C.E. Stebbins, A.A. Russo, C. Schneider, N. Rosen, F.U. Hartl, and N.P. Pavletich Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent Cell 89 1997 239 250
    • (1997) Cell , vol.89 , pp. 239-250
    • Stebbins, C.E.1    Russo, A.A.2    Schneider, C.3    Rosen, N.4    Hartl, F.U.5    Pavletich, N.P.6
  • 48
    • 0028697474 scopus 로고
    • Multiple p53 protein isoforms and formation of oligomeric complexes with heat shock proteins Hsp70 and Hsp90 in the human mammary tumor, T47D, cell line
    • J.K. Selkirk, B.A. Merrick, B.L. Stackhouse, and C. He Multiple p53 protein isoforms and formation of oligomeric complexes with heat shock proteins Hsp70 and Hsp90 in the human mammary tumor, T47D, cell line Appl. Theor. Electrophor. 4 1994 11 18
    • (1994) Appl. Theor. Electrophor. , vol.4 , pp. 11-18
    • Selkirk, J.K.1    Merrick, B.A.2    Stackhouse, B.L.3    He, C.4
  • 49
    • 0035684430 scopus 로고    scopus 로고
    • CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein
    • S. Murata, Y. Minami, M. Minami, T. Chiba, and K. Tanaka CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein EMBO Rep. 2 2001 1133 1138
    • (2001) EMBO Rep. , vol.2 , pp. 1133-1138
    • Murata, S.1    Minami, Y.2    Minami, M.3    Chiba, T.4    Tanaka, K.5
  • 51
    • 33846921755 scopus 로고    scopus 로고
    • The impact of altered p53 dosage on hematopoietic stem cell dynamics during aging
    • DOI 10.1182/blood-2006-03-010413
    • M. Dumble, L. Moore, S.M. Chambers, H. Geiger, G. Van Zant, M.A. Goodell, and L.A. Donehower The impact of altered p53 dosage on hematopoietic stem cell dynamics during aging Blood 109 2007 1736 1742 (Pubitemid 46239609)
    • (2007) Blood , vol.109 , Issue.4 , pp. 1736-1742
    • Dumble, M.1    Moore, L.2    Chambers, S.M.3    Geiger, H.4    Van Zant, G.5    Goodell, M.A.6    Donehower, L.A.7
  • 55
    • 51049098347 scopus 로고    scopus 로고
    • The Arf/p53 pathway in cancer and aging
    • A. Matheu, A. Maraver, and M. Serrano The Arf/p53 pathway in cancer and aging Cancer Res. 68 2008 6031 6034
    • (2008) Cancer Res. , vol.68 , pp. 6031-6034
    • Matheu, A.1    Maraver, A.2    Serrano, M.3
  • 56
    • 0034069237 scopus 로고    scopus 로고
    • Cancer, aging and cellular senescence
    • Campisi J. Cancer, aging and cellular senescence In Vivo 14 2000 183 188
    • (2000) In Vivo , vol.14 , pp. 183-188
    • Campisi, J.1
  • 57
    • 0030941458 scopus 로고    scopus 로고
    • P53, the cellular gatekeeper for growth and division
    • A.J. Levine p53, the cellular gatekeeper for growth and division Cell 88 1997 323 331
    • (1997) Cell , vol.88 , pp. 323-331
    • Levine, A.J.1
  • 59
    • 44149124776 scopus 로고    scopus 로고
    • Chaperone-dependent stabilization and degradation of p53 mutants
    • P. Muller, R. Hrstka, D. Coomber, D.P. Lane, and B. Vojtesek Chaperone-dependent stabilization and degradation of p53 mutants Oncogene 27 2008 3371 3383
    • (2008) Oncogene , vol.27 , pp. 3371-3383
    • Muller, P.1    Hrstka, R.2    Coomber, D.3    Lane, D.P.4    Vojtesek, B.5
  • 60
  • 61
    • 70349799010 scopus 로고    scopus 로고
    • The cell cycle is a redox cycle; Linking phase-specific targets to cell fate
    • W.C. Burhans, and N.H. Heintz The cell cycle is a redox cycle; linking phase-specific targets to cell fate Free Radic. Biol. Med. 47 2009 1282 1293
    • (2009) Free Radic. Biol. Med. , vol.47 , pp. 1282-1293
    • Burhans, W.C.1    Heintz, N.H.2
  • 62
    • 78650152988 scopus 로고    scopus 로고
    • P53, ROS and senescence in the control of aging
    • A. Vigneron, and K.H. Vousden p53, ROS and senescence in the control of aging Aging 2 2010 471 474
    • (2010) Aging , vol.2 , pp. 471-474
    • Vigneron, A.1    Vousden, K.H.2


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