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The Nuclear and DNA-Associated Molecular Chaperone Network.

Authors
  • Gvozdenov, Zlata1, 2
  • Kolhe, Janhavi1
  • Freeman, Brian C1
  • 1 Department of Cell and Developmental Biology, University of Illinois, Urbana-Champaign, Urbana, Illinois 61801.
  • 2 Department Chemie, Technische Universität München, Garching 85748, Germany. , (Germany)
Type
Published Article
Journal
Cold Spring Harbor Perspectives in Biology
Publisher
Cold Spring Harbor Laboratory
Publication Date
Oct 01, 2019
Volume
11
Issue
10
Identifiers
DOI: 10.1101/cshperspect.a034009
PMID: 30745291
Source
Medline
Language
English
License
Unknown

Abstract

Maintenance of a healthy and functional proteome in all cellular compartments is critical to cell and organismal homeostasis. Yet, our understanding of the proteostasis process within the nucleus is limited. Here, we discuss the identified roles of the major molecular chaperones Hsp90, Hsp70, and Hsp60 with client proteins working in diverse DNA-associated pathways. The unique challenges facing proteins in the nucleus are considered as well as the conserved features of the molecular chaperone system in facilitating DNA-linked processes. As nuclear protein inclusions are a common feature of protein-aggregation diseases (e.g., neurodegeneration), a better understanding of nuclear proteostasis is warranted. Copyright © 2019 Cold Spring Harbor Laboratory Press; all rights reserved.

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