Neuronal DnaJ proteins HSJ1a and HSJ1b: a role in linking the Hsp70 chaperone machine to the ubiquitin-proteasome system?

Biochem Soc Trans. 2004 Aug;32(Pt 4):640-2. doi: 10.1042/BST0320640.

Abstract

The heat-shock protein 70 chaperone machine is functionally connected to the ubiquitin-proteasome system by the co-chaperone CHIP. In this article, we discuss evidence that the neuronal DnaJ proteins HSJ1a and HSJ1b may represent a further link between the cellular protein folding and degradation machineries. We have demonstrated that HSJ1 proteins contain putative ubiquitin interaction motifs and can modulate the cellular processing of rhodopsin, a protein that is targeted for degradation by the proteasome when it is misfolded.

MeSH terms

  • Amino Acid Motifs
  • HSP40 Heat-Shock Proteins
  • Heat-Shock Proteins / chemistry
  • Heat-Shock Proteins / metabolism*
  • Humans
  • Molecular Chaperones / chemistry
  • Molecular Chaperones / metabolism*
  • Neurons / metabolism*
  • Proteasome Endopeptidase Complex / metabolism*
  • Protein Conformation
  • Protein Processing, Post-Translational
  • Rhodopsin / metabolism
  • Ubiquitin / metabolism*

Substances

  • DNAJB2 protein, human
  • HSP40 Heat-Shock Proteins
  • Heat-Shock Proteins
  • Molecular Chaperones
  • Ubiquitin
  • Rhodopsin
  • Proteasome Endopeptidase Complex