Alternative ATPase domain interactions in eukaryotic Hsp70 chaperones
File(s) fmolb-10-1155784.pdf (822.94 KB)
Published version
Author(s)
Ben-Khoud, Yassin
Cheng, Chao-Sheng
Ali, Maruf
Type
Journal Article
Abstract
Hsp70 molecular chaperones are essential components for maintaining protein homeostasis within cells. They interact with substrate or client proteins in a well characterised fashion that is regulated by ATP and supported by co-chaperones. In eukaryotes there is a vast array of Hsp70 isoforms that may facilitate adaption to a particular cellular compartment and distinct biological role. Emerging data indicate a novel type of interaction between Hsp70 and client protein that does not fit with the classical Hsp70 ATP regulated substrate mechanism. In this review, we highlight Hsp70 ATPase domain interactions with binding partners from various biological systems that we refer to as Hsp70 ATPase alternative binding proteins or HAAB proteins. We identify common mechanistic features that may define how Hsp70 operates when associating with proteins in this alternative HAAB mode of action.
Date Issued
2023-03-16
Date Acceptance
2023-03-06
Citation
Frontiers in Molecular Biosciences, 2023, 10, pp.1-6
ISSN
2296-889X
Publisher
Frontiers Media
Start Page
1
End Page
6
Journal / Book Title
Frontiers in Molecular Biosciences
Volume
10
Copyright Statement
Copyright © 2023 Ben-Khoud, Chen and Ali. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
License URL
Identifier
https://www.frontiersin.org/articles/10.3389/fmolb.2023.1155784/full
Publication Status
Published
Article Number
1155784
Date Publish Online
2023-03-16
