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PMID: 15270696 Published · ppublish English Journal Article

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

Biochemical Society transactions ·Vol. 32 ·No. Pt 4 ·2004-08-00 ·Pages 640-2

Chapple JP, van der Spuy J, Poopalasundaram S, Cheetham ME

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,metabolism Humans Molecular Chaperones/chemistry,metabolism Neurons/metabolism Proteasome Endopeptidase Complex/metabolism Protein Conformation Protein Processing, Post-Translational Rhodopsin/metabolism Ubiquitin/metabolism
Chemicals
DNAJB2 protein, human HSP40 Heat-Shock Proteins Heat-Shock Proteins Molecular Chaperones Ubiquitin Rhodopsin Proteasome Endopeptidase Complex
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Chapple J P
Division of Pathology, Institute of Ophthalmology, University College London, 11-43 Bath Street, London EC1V 9EL, UK. [email protected]
van der Spuy J
Poopalasundaram S
Cheetham M E
Article Info
Journal
Biochemical Society transactions
Abbr.
Biochem Soc Trans
ISSN
0300-5127
Published
2004-08-00
Pages
640-2
Language
English
Region
England
NLM ID
7506897
Subset
IM
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