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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Format: | Article |
Language: | English |
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Frontiers Media S.A.
2023-03-01
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Series: | Frontiers in Molecular Biosciences |
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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. |
first_indexed | 2024-04-10T00:12:56Z |
format | Article |
id | doaj.art-23553c3b105346ffae070f2f7c82d94c |
institution | Directory Open Access Journal |
issn | 2296-889X |
language | English |
last_indexed | 2024-04-10T00:12:56Z |
publishDate | 2023-03-01 |
publisher | Frontiers Media S.A. |
record_format | Article |
series | Frontiers in Molecular Biosciences |
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 |