Hop: more than an Hsp70/Hsp90 adaptor protein

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Odunuga, O, Longshaw, Victoria M and Blatch, Gregory L (2004) Hop: more than an Hsp70/Hsp90 adaptor protein. BioEssays, 26 (10). pp. 1058-1068. ISSN 0265-9247

Abstract

Molecular chaperones facilitate the correct folding of other proteins under physiological and stress conditions. Recently it has become evident that various co-chaperone proteins regulate the cellular functions of these chaperones, particularly Hsp70 and Hsp90. Hop is one of the most extensively studied co-chaperones that is able to directly associate with both Hsp70 and Hsp90. The current dogma proposes that Hop functions primarily as an adaptor that directs Hsp90 to Hsp70-client protein complexes in the cytoplasm. However, recent evidence suggests that Hop can also modulate the chaperone activities of these Hsps, and that it is not dedicated to Hsp70 and Hsp90. While the co-chaperone function of Hop within the cytoplasm has been extensively studied, its association with nuclear complexes and prion proteins remains to be elucidated. This article will review the structural features of Hop, and the evidence that its biological function is considerably broader than previously envisaged.

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Additional Information

Online ISSN: 1521-1878

Item type Article
URI https://vuir.vu.edu.au/id/eprint/8165
DOI https://doi.org/10.1002/bies.20107
Official URL http://dx.doi.org/10.1002/bies.20107
Subjects Historical > Faculty/School/Research Centre/Department > School of Biomedical and Health Sciences
Current > FOR Classification > 0601 Biochemistry and Cell Biology
Current > FOR Classification > 0604 Genetics
Keywords ResPubID22220. hop, Hsp70, Hsp90, proteins, molecular chaperones, DNA
Citations in Scopus 160 - View on Scopus
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