Alternative ATPase domain interactions in eukaryotic Hsp70 chaperones

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 ma...

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Main Authors: Yassin Ben-Khoud, Chao-Sheng Chen, Maruf M. U. Ali
Format: Article
Language:English
Published: Frontiers Media S.A. 2023-03-01
Series:Frontiers in Molecular Biosciences
Subjects:
Online Access:https://www.frontiersin.org/articles/10.3389/fmolb.2023.1155784/full
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author Yassin Ben-Khoud
Chao-Sheng Chen
Maruf M. U. Ali
author_facet Yassin Ben-Khoud
Chao-Sheng Chen
Maruf M. U. Ali
author_sort Yassin Ben-Khoud
collection DOAJ
description 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.
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spelling doaj.art-23553c3b105346ffae070f2f7c82d94c2023-03-16T07:12:35ZengFrontiers Media S.A.Frontiers in Molecular Biosciences2296-889X2023-03-011010.3389/fmolb.2023.11557841155784Alternative ATPase domain interactions in eukaryotic Hsp70 chaperonesYassin Ben-KhoudChao-Sheng ChenMaruf M. U. AliHsp70 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.https://www.frontiersin.org/articles/10.3389/fmolb.2023.1155784/fullHsp70eukaryotic chaperonesBiPIRE1Tim44XIAP
spellingShingle Yassin Ben-Khoud
Chao-Sheng Chen
Maruf M. U. Ali
Alternative ATPase domain interactions in eukaryotic Hsp70 chaperones
Frontiers in Molecular Biosciences
Hsp70
eukaryotic chaperones
BiP
IRE1
Tim44
XIAP
title Alternative ATPase domain interactions in eukaryotic Hsp70 chaperones
title_full Alternative ATPase domain interactions in eukaryotic Hsp70 chaperones
title_fullStr Alternative ATPase domain interactions in eukaryotic Hsp70 chaperones
title_full_unstemmed Alternative ATPase domain interactions in eukaryotic Hsp70 chaperones
title_short Alternative ATPase domain interactions in eukaryotic Hsp70 chaperones
title_sort alternative atpase domain interactions in eukaryotic hsp70 chaperones
topic Hsp70
eukaryotic chaperones
BiP
IRE1
Tim44
XIAP
url https://www.frontiersin.org/articles/10.3389/fmolb.2023.1155784/full
work_keys_str_mv AT yassinbenkhoud alternativeatpasedomaininteractionsineukaryotichsp70chaperones
AT chaoshengchen alternativeatpasedomaininteractionsineukaryotichsp70chaperones
AT marufmuali alternativeatpasedomaininteractionsineukaryotichsp70chaperones