关于 Ydj1/DNAJA1 协同伴侣翻译后修饰的新见解

IF 4.3 3区材料科学 Q1 ENGINEERING, ELECTRICAL & ELECTRONIC

ACS Applied Electronic Materials Pub Date : 2024-02-01 DOI:10.1016/j.cstres.2023.11.001

Megan M. Mitchem , Courtney Shrader , Elizabeth Abedi, Andrew W. Truman

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引用次数: 0

摘要

Hsp70 分子伴侣的活性受包括 J 蛋白在内的一系列辅助辅助伴侣的调控。对 J 蛋白的研究历来侧重于它们的表达、定位和 Hsp70 的激活。越来越多的证据表明，伴侣蛋白的翻译后修饰（PTMs）（伴侣蛋白代码）可微调伴侣蛋白的功能。这篇微型综述总结了目前对主要 J 蛋白 Ydj1 和 DNAJA1 上 PTM 的作用和调控的理解。了解这些 PTM 可为针对癌症和神经退行性疾病的伴侣活性提供新的治疗途径。

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Novel insights into the post-translational modifications of Ydj1/DNAJA1 co-chaperones

The activity of the Hsp70 molecular chaperone is regulated by a suite of helper co-chaperones that include J-proteins. Studies on J-proteins have historically focused on their expression, localization, and activation of Hsp70. There is growing evidence that the post-translational modifications (PTMs) of chaperones (the chaperone code) fine-tune chaperone function. This mini-review summarizes the current understanding of the role and regulation of PTMs on the major J-proteins Ydj1 and DNAJA1. Understanding these PTMs may provide novel therapeutic avenues for targeting chaperone activity in cancer and neurodegenerative diseases.

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来源期刊

ACS Applied Electronic Materials Multiple-

CiteScore

7.20

自引率

4.30%

发文量

567