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 proteasome.
Wiederkehr
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Institute for Biochemistry and Molecular Biology, University of Freiburg, Hermann-Herder-Strasse 7, D-79104, Freiburg, Germany.
Bukau
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Buchberger
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A
D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry / Q000502:physiology*; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D004268:DNA-Binding Proteins; D008025:Ligases / Q000737:chemistry / Q000502:physiology; D008954:Models, Biological; D009097:Multienzyme Complexes / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000378:metabolism*; D011965:Receptors, Glucocorticoid / Q000378:metabolism; D014157:Transcription Factors; D044767:Ubiquitin-Protein Ligases
C091732:BCL2-associated athanogene 1 protein; D002352:Carrier Proteins; D004268:DNA-Binding Proteins; D009097:Multienzyme Complexes; D011506:Proteins; D011965:Receptors, Glucocorticoid; D014157:Transcription Factors; C467728:STUB1 protein, human; D044767:Ubiquitin-Protein Ligases; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex; D008025:Ligases