Protein Turnover: A CHIP Programmed for Proteolysis

The Hsp70 co-chaperone CHIP has recently gained attention as a regulator of protein turnover. CHIP has now been reported to be a component of the ubiquitination cascade, specifically an E3 ligase. CHIP appears to be part of a system that diverts incorrectly folded proteins from chaperones to the pro...

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Bibliographic Details
Published in:Current biology 2002-01, Vol.12 (1), p.R26-R28
Main Authors: Wiederkehr, T., Bukau, B., Buchberger, A.
Format: Article
Language:English
Subjects:
Animals
Carrier Proteins - chemistry
Carrier Proteins - physiology
Cysteine Endopeptidases - metabolism
DNA-Binding Proteins
Ligases - chemistry
Ligases - physiology
Models, Biological
Multienzyme Complexes - metabolism
Proteasome Endopeptidase Complex
Protein Folding
Protein Structure, Tertiary
Proteins - metabolism
Receptors, Glucocorticoid - metabolism
Transcription Factors
Ubiquitin-Protein Ligases
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Summary:The Hsp70 co-chaperone CHIP has recently gained attention as a regulator of protein turnover. CHIP has now been reported to be a component of the ubiquitination cascade, specifically an E3 ligase. CHIP appears to be part of a system that diverts incorrectly folded proteins from chaperones to the proteasome.
ISSN:0960-9822
1879-0445
DOI:10.1016/S0960-9822(01)00644-3