Mechanism of Hsp70 specialized interactions in protein translocation and the unfolded protein response.

Abstract:

: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.

journal_name

Open Biol

journal_title

Open biology

authors

Larburu N,Adams CJ,Chen CS,Nowak PR,Ali MMU

doi

10.1098/rsob.200089

subject

Has Abstract

pub_date

2020-08-01 00:00:00

pages

200089

issue

8

issn

2046-2441

journal_volume

10

pub_type

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