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Mechanism of Hsp70 specialized interactions in protein translocation and the unfolded protein response.
Open Biology ( IF 5.8 ) Pub Date : 2020-08-19 , DOI: 10.1098/rsob.200089
Natacha Larburu 1 , Christopher J Adams 1 , Chao-Sheng Chen 1 , Piotr R Nowak 1 , Maruf M U Ali 1
Affiliation  

Hsp70 chaperones interact with substrate proteins in a coordinated fashion that is regulated by nucleotides and enhanced by assisting cochaperones. There are numerous homologues and isoforms of Hsp70 that participate in a wide variety of cellular functions. This diversity can facilitate adaption or specialization based on particular biological activity and location within the cell. In this review, we highlight two specialized binding partner proteins, Tim44 and IRE1, that interact with Hsp70 at the membrane in order to serve their respective roles in protein translocation and unfolded protein response signalling. Recent mechanistic data suggest analogy in the way the two Hsp70 homologues (BiP and mtHsp70) can bind and release from IRE1 and Tim44 upon substrate engagement. These shared mechanistic features may underlie how Hsp70 interacts with specialized binding partners and may extend our understanding of the mechanistic repertoire that Hsp70 chaperones possess.



中文翻译:

Hsp70 在蛋白质易位和未折叠蛋白质反应中专门相互作用的机制。

Hsp70 分子伴侣以协调方式与底物蛋白相互作用,该方式受核苷酸调节并通过辅助伴侣蛋白增强。Hsp70 有许多同系物和同种型,它们参与多种细胞功能。这种多样性可以促进基于特定生物活性和细胞内位置的适应或专业化。在这篇综述中,我们重点介绍了两种专门的结合伴侣蛋白 Tim44 和 IRE1,它们与膜上的 Hsp70 相互作用,以便在蛋白质易位和未折叠蛋白质反应信号传导中发挥各自的作用。最近的机械数据表明,两种 Hsp70 同系物(BiP 和 mtHsp70)在底物接合时可以结合 IRE1 和 Tim44 并从其中释放的方式类似。

更新日期:2020-08-19
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