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

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

DOI:
10.1042/bst0320640
复制
发表时间:
2004-08-01
影响因子:
3.9
通讯作者:
Cheetham, ME
Cheetham, ME
中科院分区:
生物学3区
文献类型:
--
作者:
Chapple, JP;van der Spuy, J;Cheetham, ME

文献摘要

被引文献

相似文献

热休克蛋白70的伴侣机器通过共伴侣芯片与泛素-蛋白酶体系统功能相连。在这篇文章中,我们讨论了神经元DNAJ蛋白HSJ1a和HSJ1b可能代表细胞蛋白质折叠和降解机制之间的进一步联系的证据。我们已经证明HSJ1蛋白包含假定的泛素相互作用基序,并可以调节视紫红质的细胞处理,视紫红质是一种蛋白质,当它错误折叠时,它会被蛋白酶体降解。
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.