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Role of Hsp70 in Post-Translational Protein Targeting: Tail-Anchored Membrane Proteins and Beyond

Shan, Shu-ou (2023) Role of Hsp70 in Post-Translational Protein Targeting: Tail-Anchored Membrane Proteins and Beyond. International Journal of Molecular Sciences, 24 (2). Art. No. 1170. ISSN 1422-0067. PMCID PMC9866221. doi:10.3390/ijms24021170.

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The Hsp70 family of molecular chaperones acts as a central 'hub' in the cell that interacts with numerous newly synthesized proteins to assist in their biogenesis. Apart from its central and well-established role in facilitating protein folding, Hsp70s also act as key decision points in the cellular chaperone network that direct client proteins to distinct biogenesis and quality control pathways. In this paper, we review accumulating data that illustrate a new branch in the Hsp70 network: the post-translational targeting of nascent membrane and organellar proteins to diverse cellular organelles. Work in multiple pathways suggests that Hsp70, via its ability to interact with components of protein targeting and translocation machineries, can initiate elaborate substrate relays in a sophisticated cascade of chaperones, cochaperones, and receptor proteins, and thus provide a mechanism to safeguard and deliver nascent membrane proteins to the correct cellular membrane. We discuss the mechanistic principles gleaned from better-studied Hsp70-dependent targeting pathways and outline the observations and outstanding questions in less well-studied systems.

Item Type:Article
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URLURL TypeDescription CentralArticle
Shan, Shu-ou0000-0002-6526-1733
Additional Information:© 2023 by the author. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( S.o.S. is supported by grant R35 GM135321 from NIGMS.
Funding AgencyGrant Number
NIHR35 GM135321
Issue or Number:2
PubMed Central ID:PMC9866221
Record Number:CaltechAUTHORS:20230206-9587900.32
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Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:119071
Deposited By: Research Services Depository
Deposited On:09 Mar 2023 17:34
Last Modified:09 Mar 2023 17:34

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