Startseite Roles of the nucleotide exchange factor and chaperone Hsp110 in cellular proteostasis and diseases of protein misfolding
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Roles of the nucleotide exchange factor and chaperone Hsp110 in cellular proteostasis and diseases of protein misfolding

  • Unekwu M. Yakubu und Kevin A. Morano ORCID logo EMAIL logo
Veröffentlicht/Copyright: 7. September 2018

Abstract

Cellular protein homeostasis (proteostasis) is maintained by a broad network of proteins involved in synthesis, folding, triage, repair and degradation. Chief among these are molecular chaperones and their cofactors that act as powerful protein remodelers. The growing realization that many human pathologies are fundamentally diseases of protein misfolding (proteopathies) has generated interest in understanding how the proteostasis network impacts onset and progression of these diseases. In this minireview, we highlight recent progress in understanding the enigmatic Hsp110 class of heat shock protein that acts as both a potent nucleotide exchange factor to regulate activity of the foldase Hsp70, and as a passive chaperone capable of recognizing and binding cellular substrates on its own, and its integration into the proteostasis network.

Acknowledgments

We apologize to the many investigators whose contributions we were unable to cite due to the brevity of this minireview. Work in the authors’ laboratory was supported by NIH grants GM074696 (Funder Id: 10.13039/100000057), GM127287 and AG051046 (Funder Id: 10.13039/100000049).

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Received: 2018-04-04
Accepted: 2018-05-30
Published Online: 2018-09-07
Published in Print: 2018-09-25

©2018 Walter de Gruyter GmbH, Berlin/Boston

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