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Titolo:
The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins
Autore:
Connell, P; Ballinger, CA; Jiang, JH; Wu, YX; Thompson, LJ; Hohfeld, J; Patterson, C;
Indirizzi:
Univ N Carolina, Program Mol Cardiol, Chapel Hill, NC 27514 USA Univ N Carolina Chapel Hill NC USA 27514 rdiol, Chapel Hill, NC 27514 USA Univ N Carolina, Lineberger Comprehens Canc Ctr, Chapel Hill, NC USA Univ N Carolina Chapel Hill NC USA prehens Canc Ctr, Chapel Hill, NC USA Univ Texas, Med Branch, Div Cardiol, Galveston, TX 77550 USA Univ Texas Galveston TX USA 77550 h, Div Cardiol, Galveston, TX 77550 USA Max Planck Inst Biochem, Dept Mol Cell Biol, Martinsried, Germany Max Planck Inst Biochem Martinsried Germany Biol, Martinsried, Germany
Titolo Testata:
NATURE CELL BIOLOGY
fascicolo: 1, volume: 3, anno: 2001,
pagine: 93 - 96
SICI:
1465-7392(200101)3:1<93:TCCRPT>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
GLUCOCORTICOID RECEPTOR; MOLECULAR CHAPERONES; HSP90; BINDING; GELDANAMYCIN; DEGRADATION; MACHINERY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
24
Recensione:
Indirizzi per estratti:
Indirizzo: Patterson, C Univ N Carolina, Program Mol Cardiol, Chapel Hill, NC 27514 USA Univ N Carolina Chapel Hill NC USA 27514 Hill, NC 27514 USA
Citazione:
P. Connell et al., "The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins", NAT CELL BI, 3(1), 2001, pp. 93-96

Abstract

To maintain quality control in cells, mechanisms distinguish among improperly folded peptides, mature and functional proteins, and proteins to be targeted for degradation. The molecular chaperones, including heat-shock protein Hsp90, have the ability to recognize misfolded proteins and assist in their conversion to a functional conformation. Disruption of Hsp90 heterocomplexes by the Hsp90 inhibitor geldanamycin leads to substrate degradation through the ubiquitin-proteasome pathway(1-3), implicating this system in protein triage decisions. We previously identified CHIP (carboxyl terminus of Hsc70-interacting protein) to be an interaction partner of Hsc70 (ref. 4). CHIP also interacts directly with a tetratricopeptide repeat acceptor site of Hsp90, incorporating into Hsp90 heterocomplexes and eliciting release ofthe regulatory cofactor p23. Here we show that CHIP abolishes the steroid-binding activity and transactivation potential of the glucocorticoid receptor, a well-characterized Hsp90 substrate(5), even though it has little effect on its synthesis. Instead, CHIP induces ubiquitylation of the glucocorticoid receptor and degradation through the proteasome. By remodelling Hsp90 heterocomplexes to favour substrate degradation, CHIP modulates protein triage decisions that regulate the balance between protein folding and degradation for chaperone substrates.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 22/01/20 alle ore 07:29:31