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Volumn 18, Issue 3, 2011, Pages 506-515

Regulation of PIDD auto-proteolysis and activity by the molecular chaperone Hsp90

Author keywords

Caspase 2; Hsp90; NF B; PIDD

Indexed keywords

BINDING PROTEIN; CASPASE 2; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; I KAPPA B; P53 INDUCED PROTEIN WITH A DEATH DOMAIN; PROTEIN P23; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 79951678012     PISSN: 13509047     EISSN: 14765403     Source Type: Journal    
DOI: 10.1038/cdd.2010.124     Document Type: Article
Times cited : (12)

References (40)
  • 2
    • 26444433872 scopus 로고    scopus 로고
    • Apoptosis caused by p53-induced protein with death domain (PIDD) depends on the death adapter protein RAIDD
    • Berube C, Boucher LM, Ma W, Wakeham A, Salmena L, Hakem R et al. Apoptosis caused by p53-induced protein with death domain (PIDD) depends on the death adapter protein RAIDD. Proc Natl Acad Sci USA 2005; 102: 14314-14320.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 14314-14320
    • Berube, C.1    Boucher, L.M.2    Ma, W.3    Wakeham, A.4    Salmena, L.5    Hakem, R.6
  • 3
    • 0037049549 scopus 로고    scopus 로고
    • A novel Apaf-1-independent putative caspase-2 activation complex
    • DOI 10.1083/jcb.200209004
    • Read SH, Baliga BC, Ekert PG, Vaux DL, Kumar S. A novel Apaf-1-independent putative caspase-2 activation complex. J Cell Biol 2002; 159: 739-745. (Pubitemid 36008356)
    • (2002) Journal of Cell Biology , vol.159 , Issue.5 , pp. 739-745
    • Read, S.H.1    Baliga, B.C.2    Ekert, P.G.3    Vaux, D.L.4    Kumar, S.5
  • 4
    • 2442453730 scopus 로고    scopus 로고
    • The PIDDosome, a Protein Complex Implicated in Activation of Caspase-2 in Response to Genotoxic Stress
    • DOI 10.1126/science.1095432
    • Tinel A, Tschopp J. The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress. Science 2004; 304: 843-846. (Pubitemid 38620177)
    • (2004) Science , vol.304 , Issue.5672 , pp. 843-846
    • Tinel, A.1    Tschopp, J.2
  • 5
    • 28944447430 scopus 로고    scopus 로고
    • PIDD Mediates NF-κB activation in response to DNA damage
    • DOI 10.1016/j.cell.2005.09.036, PII S0092867405010421
    • Janssens S, Tinel A, Lippens S, Tschopp J. PIDD mediates NF-kappaB activation in response to DNA damage. Cell 2005; 123: 1079-1092. (Pubitemid 41785422)
    • (2005) Cell , vol.123 , Issue.6 , pp. 1079-1092
    • Janssens, S.1    Tinel, A.2    Lippens, S.3    Tschopp, J.4
  • 6
    • 33846219997 scopus 로고    scopus 로고
    • Autoproteolysis of PIDD marks the bifurcation between pro-death caspase-2 and pro-survival NF-κB pathway
    • DOI 10.1038/sj.emboj.7601473, PII 7601473
    • Tinel A, Janssens S, Lippens S, Cuenin S, Logette E, Jaccard B et al. Autoproteolysis of PIDD marks the bifurcation between pro-death caspase-2 and pro-survival NF-kappaB pathway. Embo J 2007; 26: 197-208. (Pubitemid 46094711)
    • (2007) EMBO Journal , vol.26 , Issue.1 , pp. 197-208
    • Tinel, A.1    Janssens, S.2    Lippens, S.3    Cuenin, S.4    Logette, E.5    Jaccard, B.6    Quadroni, M.7    Tschopp, J.8
  • 7
    • 59049093349 scopus 로고    scopus 로고
    • DNA-PKcs-PIDDosome: A nuclear caspase-2-activating complex with role in G2/M checkpoint maintenance
    • Shi M, Vivian CJ, Lee KJ, Ge C, Morotomi-Yano K, Manzl C et al. DNA-PKcs-PIDDosome: a nuclear caspase-2-activating complex with role in G2/M checkpoint maintenance. Cell 2009; 136: 508-520.
    • (2009) Cell , vol.136 , pp. 508-520
    • Shi, M.1    Vivian, C.J.2    Lee, K.J.3    Ge, C.4    Morotomi-Yano, K.5    Manzl, C.6
  • 8
    • 33748774114 scopus 로고    scopus 로고
    • Upon intracellular processing, the C-terminal death domain-containing fragment of the p53-inducible PIDD/LRDD protein translocates to the nucleoli and interacts with nucleolin
    • DOI 10.1016/j.bbrc.2006.08.176, PII S0006291X06019978
    • Pick R, Badura S, Bosser S, Zornig M. Upon intracellular processing, the C-terminal death domain-containing fragment of the p53-inducible PIDD/LRDD protein translocates to the nucleoli and interacts with nucleolin. Biochem Biophys Res Commun 2006; 349: 1329-1338. (Pubitemid 44416403)
    • (2006) Biochemical and Biophysical Research Communications , vol.349 , Issue.4 , pp. 1329-1338
    • Pick, R.1    Badura, S.2    Bosser, S.3    Zornig, M.4
  • 10
    • 3242879188 scopus 로고    scopus 로고
    • 'The stress of dying': The role of heat shock proteins in the regulation of apoptosis
    • DOI 10.1242/jcs.01284
    • Beere HM. 'The stress of dying': the role of heat shock proteins in the regulation of apoptosis. J Cell Sci 2004; 117 (Part 13): 2641-2651. (Pubitemid 38997248)
    • (2004) Journal of Cell Science , vol.117 , Issue.13 , pp. 2641-2651
    • Beere, H.M.1
  • 11
    • 23644448266 scopus 로고    scopus 로고
    • Regulation of Nod1 by Hsp90 chaperone complex
    • Hahn JS. Regulation of Nod1 by Hsp90 chaperone complex. FEBS Lett 2005; 579: 4513-4519.
    • (2005) FEBS Lett , vol.579 , pp. 4513-4519
    • Hahn, J.S.1
  • 12
    • 0030869037 scopus 로고    scopus 로고
    • Folding of the glucocorticoid receptor by the heat shock protein (hsp) 90-based chaperone machinery. The role of p23 is to stabilize receptor hsp90 heterocomplexes formed by hsp90.p60.hsp70
    • DOI 10.1074/jbc.272.34.21213
    • Dittmar KD, Demady DR, Stancato LF, Krishna P, Pratt WB. Folding of the glucocorticoid receptor by the heat shock protein (hsp) 90-based chaperone machinery. The role of p23 is to stabilize receptor hsp 90 heterocomplexes formed by hsp90.p60.hsp70. J Biol Chem 1997; 272: 21213-21220. (Pubitemid 27373984)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.34 , pp. 21213-21220
    • Dittmar, K.D.1    Demady, D.R.2    Stancato, L.F.3    Krishna, P.4    Pratt, W.B.5
  • 13
    • 0028064940 scopus 로고
    • Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation
    • Whitesell L, Mimnaugh EG, De Costa B, Myers CE, Neckers LM. Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation. Proc Natl Acad Sci USA 1994; 91: 8324-8328.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.G.2    De Costa, B.3    Myers, C.E.4    Neckers, L.M.5
  • 14
    • 0034708216 scopus 로고    scopus 로고
    • The U box is a modified RING finger - A common domain in ubiquitination [1]
    • DOI 10.1016/S0960-9822(00)00398-5
    • Aravind L, Koonin EV. The U box is a modified RING finger-common domain in ubiquitination. Curr Biol 2000; 10: R132-R134. (Pubitemid 30146770)
    • (2000) Current Biology , vol.10 , Issue.4
    • Aravind, L.1    Koonin, E.V.2
  • 15
    • 1242291789 scopus 로고    scopus 로고
    • CHIP: A link between the chaperone and proteasome systems
    • DOI 10.1379/1466-1268(2003)008<0303:CALBTC>2.0.CO;2
    • McDonough H, Patterson C. CHIP: a link between the chaperone and proteasome systems. Cell Stress Chaperones 2003; 8: 303-308. (Pubitemid 38222876)
    • (2003) Cell Stress and Chaperones , vol.8 , Issue.4 , pp. 303-308
    • McDonough, H.1    Patterson, C.2
  • 16
    • 70350023560 scopus 로고    scopus 로고
    • Cooperative regulation of the interferon regulatory factor-1 tumor suppressor protein by core components of the molecular chaperone machinery
    • Narayan V, Eckert M, Zylicz A, Zylicz M, Ball KL. Cooperative regulation of the interferon regulatory factor-1 tumor suppressor protein by core components of the molecular chaperone machinery. J Biol Chem 2009; 284: 25889-25899.
    • (2009) J Biol Chem , vol.284 , pp. 25889-25899
    • Narayan, V.1    Eckert, M.2    Zylicz, A.3    Zylicz, M.4    Ball, K.L.5
  • 17
    • 0032554763 scopus 로고    scopus 로고
    • Targeting of the protein chaperone, HSP90, by the transformation suppressing agent, radicicol
    • Sharma SV, Agatsuma T, Nakano H. Targeting of the protein chaperone, HSP90, by the transformation suppressing agent, radicicol. Oncogene 1998; 16: 2639-2645. (Pubitemid 28264041)
    • (1998) Oncogene , vol.16 , Issue.20 , pp. 2639-2645
    • Sharma, S.V.1    Agatsuma, T.2    Nakano, H.3
  • 18
    • 0034615701 scopus 로고    scopus 로고
    • Disruption of Hsp96 function results in degradation of the death domain kinase, receptor-interacting protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-κB activation
    • DOI 10.1074/jbc.275.14.10519
    • Lewis J, Devin A, Miller A, Lin Y, Rodriguez Y, Neckers L et al. Disruption of hsp90 function results in degradation of the death domain kinase, receptor-interacting protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-kappaB activation. J Biol Chem 2000; 275: 10519-10526. (Pubitemid 30202115)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.14 , pp. 10519-10526
    • Lewis, J.1    Devin, A.2    Miller, A.3    Lin, Y.4    Rodriguez, Y.5    Neckers, L.6    Liu, Z.-G.7
  • 19
    • 3142719113 scopus 로고    scopus 로고
    • Requirement of Hsp90 activity for IκB kinase (IKK) biosynthesis and for constitutive and inducible IKK and NF-κB activation
    • DOI 10.1038/sj.onc.1207705
    • Broemer M, Krappmann D, Scheidereit C. Requirement of Hsp90 activity for IkappaB kinase (IKK) biosynthesis and for constitutive and inducible IKK and NF-kappaB activation. Oncogene 2004; 23: 5378-5386. (Pubitemid 39005813)
    • (2004) Oncogene , vol.23 , Issue.31 , pp. 5378-5386
    • Broemer, M.1    Krappmann, D.2    Scheidereit, C.3
  • 20
    • 0029812759 scopus 로고    scopus 로고
    • Polyubiquitination and proteasomal degradation of the p185(c-erbB-2) receptor protein-tyrosine kinase induced by geldanamycin
    • DOI 10.1074/jbc.271.37.22796
    • Mimnaugh EG, Chavany C, Neckers L. Polyubiquitination and proteasomal degradation of the p185c-erbB-2 receptor protein-tyrosine kinase induced by geldanamycin. J Biol Chem 1996; 271: 22796-22801. (Pubitemid 26304727)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.37 , pp. 22796-22801
    • Mimnaugh, E.G.1    Chavany, C.2    Neckers, L.3
  • 21
    • 67650164931 scopus 로고    scopus 로고
    • Regulation of LRRK2 stability by the E3 ubiquitin ligase CHIP
    • Ding X, Goldberg MS. Regulation of LRRK2 stability by the E3 ubiquitin ligase CHIP. PLoS ONE 2009; 4: e5949.
    • (2009) PLoS ONE , vol.4
    • Ding, X.1    Goldberg, M.S.2
  • 22
    • 33746705661 scopus 로고    scopus 로고
    • Chaperoning steroid hormone action
    • DOI 10.1016/j.tem.2006.06.003, PII S1043276006001007
    • Picard D. Chaperoning steroid hormone action. Trends Endocrinol Metab 2006; 17: 229-235. (Pubitemid 44164280)
    • (2006) Trends in Endocrinology and Metabolism , vol.17 , Issue.6 , pp. 229-235
    • Picard, D.1
  • 24
    • 0033812557 scopus 로고    scopus 로고
    • Pidd, a new death-domain-containing protein, is induced by p53 and promotes apoptosis
    • Lin Y, Ma W, Benchimol S. Pidd, a new death-domain-containing protein, is induced by p53 and promotes apoptosis. Nat genet 2000; 26: 122-127.
    • (2000) Nat Genet , vol.26 , pp. 122-127
    • Lin, Y.1    Ma, W.2    Benchimol, S.3
  • 25
    • 30344459150 scopus 로고    scopus 로고
    • In situ trapping of activated initiator caspases reveals a role for caspase-2 in heat shock-induced apoptosis
    • DOI 10.1038/ncb1340, PII N1340
    • Tu S, McStay GP, Boucher LM, Mak T, Beere HM, Green DR. In situ trapping of activated initiator caspases reveals a role for caspase-2 in heat shock-induced apoptosis. Nat Cell Biol 2006; 8: 72-77. (Pubitemid 43064799)
    • (2006) Nature Cell Biology , vol.8 , Issue.1 , pp. 72-77
    • Tu, S.1    McStay, G.P.2    Boucher, L.-M.3    Mak, T.4    Beere, H.M.5    Green, D.R.6
  • 27
    • 0036187476 scopus 로고    scopus 로고
    • TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90
    • DOI 10.1016/S1097-2765(02)00450-1
    • Chen G, Cao P, Goeddel DV. TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90. Mol Cell 2002; 9: 401-410. (Pubitemid 34195564)
    • (2002) Molecular Cell , vol.9 , Issue.2 , pp. 401-410
    • Chen, G.1    Cao, P.2    Goeddel, D.V.3
  • 29
    • 0036672209 scopus 로고    scopus 로고
    • Cleave to leave: Structural insights into the dynamic organization of the nuclear pore complex
    • DOI 10.1016/S1097-2765(02)00606-8
    • Dokudovskaya S, Veenhoff LM, Rout MP. Cleave to leave: structural insights into the dynamic organization of the nuclear pore complex. Mol Cell 2002; 10: 221-223. (Pubitemid 35007336)
    • (2002) Molecular Cell , vol.10 , Issue.2 , pp. 221-223
    • Dokudovskaya, S.1    Veenhoff, L.M.2    Rout, M.P.3
  • 30
    • 0036672039 scopus 로고    scopus 로고
    • The three-dimensional structure of the autoproteolytic, nuclear pore-targeting domain of the human nucleoporin Nup98
    • DOI 10.1016/S1097-2765(02)00589-0
    • Hodel AE, Hodel MR, Griffis ER, Hennig KA, Ratner GA, Xu S et al. The three-dimensional structure of the autoproteolytic, nuclear pore-targeting domain of the human nucleoporin Nup98. Mol Cell 2002; 10: 347-358. (Pubitemid 35007349)
    • (2002) Molecular Cell , vol.10 , Issue.2 , pp. 347-358
    • Hodel, A.E.1    Hodel, M.R.2    Griffis, E.R.3    Hennig, K.A.4    Ratner, G.A.5    Xu, S.6    Powers, M.A.7
  • 31
    • 34247265509 scopus 로고    scopus 로고
    • A crucial function of SGT1 and HSP90 in inflammasome activity links mammalian and plant innate immune responses
    • DOI 10.1038/ni1459, PII NI1459
    • Mayor A, Martinon F, De Smedt T, Petrilli V, Tschopp J. A crucial function of SGT1 and HSP90 in inflammasome activity links mammalian and plant innate immune responses. Nat Immunol 2007; 8: 497-503. (Pubitemid 46605918)
    • (2007) Nature Immunology , vol.8 , Issue.5 , pp. 497-503
    • Mayor, A.1    Martinon, F.2    De Smedt, T.3    Petrilli, V.4    Tschopp, J.5
  • 32
    • 43249098558 scopus 로고    scopus 로고
    • Staying in the fold: The SGT1/chaperone machinery in maintenance and evolution of leucine-rich repeat proteins
    • Stuttmann J, Parker JE, Noel LD. Staying in the fold: the SGT1/chaperone machinery in maintenance and evolution of leucine-rich repeat proteins. Plant Signal Behav 2008; 3: 283-285. (Pubitemid 351651930)
    • (2008) Plant Signaling and Behavior , vol.3 , Issue.5 , pp. 283-285
    • Stuttmann, J.1    Parker, J.E.2    Noel, L.D.3
  • 33
    • 62549095266 scopus 로고    scopus 로고
    • Autoinhibition of UNC5b revealed by the cytoplasmic domain structure of the receptor
    • Wang R, Wei Z, Jin H, Wu H, Yu C, Wen W et al. Autoinhibition of UNC5b revealed by the cytoplasmic domain structure of the receptor. Mol Cell 2009; 33: 692-703.
    • (2009) Mol Cell , vol.33 , pp. 692-703
    • Wang, R.1    Wei, Z.2    Jin, H.3    Wu, H.4    Yu, C.5    Wen, W.6
  • 34
    • 43549102208 scopus 로고    scopus 로고
    • HSP90: The Rosetta stone for cellular protein dynamics?
    • Dezwaan DC, Freeman BC. HSP90: the Rosetta stone for cellular protein dynamics? Cell Cycle (Georgetown, Tex) 2008; 7: 1006-1012.
    • (2008) Cell Cycle (Georgetown, Tex) , vol.7 , pp. 1006-1012
    • Dezwaan, D.C.1    Freeman, B.C.2
  • 36
    • 33745223497 scopus 로고    scopus 로고
    • Heat shock induces apoptosis independently of any known initiator caspase-activating complex
    • Milleron RS, Bratton SB. Heat shock induces apoptosis independently of any known initiator caspase-activating complex. J Biol Chem 2006; 281: 16991-17000.
    • (2006) J Biol Chem , vol.281 , pp. 16991-17000
    • Milleron, R.S.1    Bratton, S.B.2
  • 37
    • 34447528828 scopus 로고    scopus 로고
    • The heat shock protein 70 family: Highly homologous proteins with overlapping and distinct functions
    • DOI 10.1016/j.febslet.2007.05.039, PII S0014579307005674, Cellular Stress
    • Daugaard M, Rohde M, Jaattela M. The heat shock protein 70 family: highly homologous proteins with overlapping and distinct functions. FEBS Lett 2007; 581: 3702-3710. (Pubitemid 47081009)
    • (2007) FEBS Letters , vol.581 , Issue.19 , pp. 3702-3710
    • Daugaard, M.1    Rohde, M.2    Jaattela, M.3
  • 38
    • 0035142877 scopus 로고    scopus 로고
    • The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
    • DOI 10.1038/35050509
    • Meacham GC, Patterson C, Zhang W, Younger JM, Cyr DM. The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nat Cell Biol 2001; 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
  • 39
    • 38049143949 scopus 로고    scopus 로고
    • P53-induced protein with a death domain (PIDD) isoforms differentially activate nuclear factor-kappaB and caspase-2 in response to genotoxic stress
    • Cuenin S, Tinel A, Janssens S, Tschopp J. p53-induced protein with a death domain (PIDD) isoforms differentially activate nuclear factor-kappaB and caspase-2 in response to genotoxic stress. Oncogene 2008; 27: 387-396.
    • (2008) Oncogene , vol.27 , pp. 387-396
    • Cuenin, S.1    Tinel, A.2    Janssens, S.3    Tschopp, J.4
  • 40
    • 0021100690 scopus 로고
    • Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
    • Dignam JD, Lebovitz RM, Roeder RG. Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res 1983; 11: 1475-1489.
    • (1983) Nucleic Acids Res , vol.11 , pp. 1475-1489
    • Dignam, J.D.1    Lebovitz, R.M.2    Roeder, R.G.3


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