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Hsp90 regulation of mitochondrial protein folding: from organelle integrity to cellular homeostasis.

Authors
  • Altieri, Dario C
Type
Published Article
Journal
Cellular and Molecular Life Sciences
Publisher
Springer-Verlag
Publication Date
Jul 01, 2013
Volume
70
Issue
14
Pages
2463–2472
Identifiers
DOI: 10.1007/s00018-012-1177-0
PMID: 23052217
Source
Medline
License
Unknown

Abstract

Although essential for energy production and cell fate decisions, the mechanisms that govern protein homeostasis, or proteostasis, in mitochondria are only recently beginning to emerge. Fresh experimental evidence has uncovered a role of molecular chaperones of the heat shock protein 90 (Hsp90) family in overseeing the protein folding environment in mitochondria. Initially implicated in protection against cell death, there is now evidence that Hsp90-directed protein quality control in mitochondria connects to hosts of cellular homeostatic networks that become prominently exploited in human cancer.

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