Protein turnover: a CHIP programmed for proteolysis

Curr Biol. 2002 Jan 8;12(1):R26-8. doi: 10.1016/s0960-9822(01)00644-3.

Abstract

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.

Publication types

  • Comment

MeSH terms

  • 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

Substances

  • BCL2-associated athanogene 1 protein
  • Carrier Proteins
  • DNA-Binding Proteins
  • Multienzyme Complexes
  • Proteins
  • Receptors, Glucocorticoid
  • Transcription Factors
  • STUB1 protein, human
  • Ubiquitin-Protein Ligases
  • Cysteine Endopeptidases
  • Proteasome Endopeptidase Complex
  • Ligases