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

被引：22

作者：

Chapple, JP

van der Spuy, J

Poopalasundaram, S

Cheetham, ME

机构：

[1] UCL, Div Pathol, Inst Ophthalmol, London EC1V 9EL, England

[2] UCL, Div Mol Genet, Inst Ophthalmol, London EC1V 9EL, England

来源：

BIOCHEMICAL SOCIETY TRANSACTIONS | 2004年 / 32卷

关键词：

C-terminus of Hsc70-interacting protein (CHIP); heat-shock protein 70 (Hsp70); HSJ1a; rhodopsin; ubiquitin-interacting motif (UIM); ubiquitin-proteasome system;

D O I：

10.1042/BST0320640

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：640 / 642

页数：3

共 20 条

[1]

Ballinger CA, 1999, MOL CELL BIOL, V19, P4535

[2] The chaperone environment at the cytoplasmic face of the endoplasmic reticulum can modulate rhodopsin processing and inclusion formation [J].