The co-chaperone p23 is degraded by caspases and the proteasome during apoptosis

FEBS Letters

Volumn 579, Issue 19, 2005, Pages 4187-4192

  Mollerup, Jens ^a   Berchtold, Martin W ^a  

^a UNIVERSITY OF COPENHAGEN   (Denmark)

Author keywords

Caspase 3; Caspase 8; Cytosolic prostaglandin E2 synthase; Hsp90 co chaperone

Indexed keywords

CASPASE; CASPASE 3; CASPASE 8; CHAPERONE; FAS ANTIGEN; HEAT SHOCK PROTEIN 90; PROTEASOME; PROTEIN P23; STAUROSPORINE; TUMOR NECROSIS FACTOR ALPHA RECEPTOR;

AMINO ACID SEQUENCE; ANIMAL CELL; APOPTOSIS; ARTICLE; ATHEROSCLEROTIC PLAQUE; CANCER CELL; CONTROLLED STUDY; DOWN REGULATION; ENZYME DEGRADATION; HUMAN; HUMAN CELL; MOLECULAR WEIGHT; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FUNCTION; PROTEIN STABILITY; PROTEIN STRUCTURE; UPREGULATION;

ANIMALS; CASPASES; CYSTEINE PROTEINASE INHIBITORS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HUMANS; JURKAT CELLS; MICE; MOLECULAR CHAPERONES; MUTAGENESIS, SITE-DIRECTED; NIH 3T3 CELLS; PHOSPHOPROTEINS; PROTEASOME ENDOPEPTIDASE COMPLEX; RECOMBINANT PROTEINS;

EID: 22544438451     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2005.06.045     Document Type: Article

References (30)

1. B.T. Lai, N.W. Chin, A.E. Stanek, W. Keh, and K.W. Lanks Quantitation and intracellular localization of the 85 K heat shock protein by using monoclonal and polyclonal antibodies Mol. Cell. Biol. 4 1984 2802 2810
2. D.F. Smith, L. Whitesell, S.C. Nair, S. Chen, V. Prapapanich, and R.A. Rimerman Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent Mol. Cell. Biol. 15 1995 6804 6812
3. S.J. Felts, and D.O. Toft p23, a simple protein with complex activities Cell Stress Chaperones 8 2003 108 113
4. J.C. Young, and F.U. Hartl Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23 EMBO J. 19 2000 5930 5940
5. P. Workman Overview: translating Hsp90 biology into Hsp90 drugs Curr. Cancer Drug Targets 3 2003 297 300
6. S.M. Roe, C. Prodromou, R. O'Brien, J.E. Ladbury, P.W. Piper, and L.H. Pearl Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin J. Med. Chem. 42 1999 260 266
7. W. Sullivan, B. Stensgard, G. Caucutt, B. Bartha, N. McMahon, E.S. Alnemri, G. Litwack, and D. Toft Nucleotides and two functional states of hsp90 J. Biol. Chem. 272 1997 8007 8012
8. W.P. Sullivan, B.A. Owen, and D.O. Toft The influence of ATP and p23 on the conformation of hsp90 J. Biol. Chem. 277 2002 45942 45948
9. Y. Morishima, K.C. Kanelakis, P.J. Murphy, E.R. Lowe, G.J. Jenkins, Y. Osawa, R.K. Sunahara, and W.B. Pratt The hsp90 cochaperone p23 is the limiting component of the multiprotein hsp90/hsp70-based chaperone system in vivo where it acts to stabilize the client protein: hsp90 complex J. Biol. Chem. 278 2003 48754 48763
10. S. Bose, T. Weikl, H. Bugl, and J. Buchner Chaperone function of Hsp90-associated proteins Science 274 1996 1715 1717
11. B.C. Freeman, D.O. Toft, and R.I. Morimoto Molecular chaperone machines: chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23 Science 274 1996 1718 1720
12. B.C. Freeman, S.J. Felts, D.O. Toft, and K.R. Yamamoto The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies Genes Dev. 14 2000 422 434
13. B.C. Freeman, and K.R. Yamamoto Disassembly of transcriptional regulatory complexes by molecular chaperones Science 296 2002 2232 2235
14. W. Li, K. Jin, T. Nagayama, X. He, J. Chang, M. Minami, S.H. Graham, R.P. Simon, and D.A. Greenberg Increased expression of apoptosis-linked gene 2 (ALG2) in the rat brain after temporary focal cerebral ischemia Neuroscience 96 2000 161 168
15. J. Krebs, and R. Klemenz The ALG-2/AIP-complex, a modulator at the interface between cell proliferation and cell death? A hypothesis Biochim. Biophys. Acta 1498 2000 153 161
16. 2+-binding modulator protein involved in cell proliferation and in cell death Biochim. Biophys. Acta 1600 2002 68 73
17. W. Martinet, D.M. Schrijvers, G.R.Y. De Meyer, A.G. Herman, and M.M. Kockx Western array analysis of human atherosclerotic plaques: downregulation of apoptosis-linked gene 2 Cardiovasc. Res. 60 2003 259 267
18. J. Mollerup, T.N. Krogh, P.F. Nielsen, and M.W. Berchtold Properties of the co-chaperone protein p23 erroneously attributed to ALG-2 (apoptosis-linked gene 2) FEBS Lett. 555 2003 478 482
19. G. Gausdal, B.T. Gjertsen, K.E. Fladmark, H. Demol, J. Vandekerckhove, and S.O. Doskeland Caspase-dependent, geldanamycin-enhanced cleavage of co-chaperone p23 in leukemic apoptosis Leukemia 18 2004 1989 1996
20. J. Dhein, P.T. Daniel, B.C. Trauth, A. Oehm, P. Moller, and P.H. Krammer Induction of apoptosis by monoclonal antibody anti-APO-1 class switch variants is dependent on cross-linking of APO-1 cell surface antigens J. Immunol. 149 1992 3166 3173
21. A. Sawano, and A. Miyawaki Directed evolution of green fluorescent protein by a new versatile PCR strategy for site-directed and semi-random mutagenesis Nucleic Acids Res. 28 2000 E78
22. J. Buchner, H. Grallert, and U. Jakob Analysis of chaperone function using citrate synthase as nonnative substrate protein Methods Enzymol. 290 1998 323 338
23. O. Micheau, S. Lens, O. Gaide, K. Alevizopoulos, and J. Tschopp NF-kappaB signals induce the expression of c-FLIP Mol. Cell Biol. 21 2001 5299 5305
24. T. Weikl, K. Abelmann, and J. Buchner An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone function J. Mol. Biol. 293 1999 685 691
25. P. Pandey, A. Saleh, A. Nakazawa, S. Kumar, S.M. Srinivasula, V. Kumar, R. Weichselbaum, C. Nalin, E.S. Alnemri, D. Kufe, and S. Kharbanda Negative regulation of cytochrome c-mediated oligomerization of Apaf-1 and activation of procaspase-9 by heat shock protein 90 EMBO J. 19 2000 4310 4322
26. J. Lewis, A. Devin, A. Miller, Y. Lin, Y. Rodriguez, L. Neckers, and Z.G. Liu 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. 275 2000 10519 10526
27. C. Zhao, and E. Wang Heat shock protein 90 suppresses tumor necrosis factor alpha induced apoptosis by preventing the cleavage of Bid in NIH3T3 fibroblasts Cell Signal. 16 2004 313 321
28. 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
29. 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
30. P. Connell, C.A. Ballinger, J. Jiang, Y. Wu, L.J. Thompson, J. Hohfeld, and C. Patterson The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins Nat. Cell Biol. 3 2001 93 96