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Cell Mol Life Sci. 2013 Jul;70(14):2463-72. doi: 10.1007/s00018-012-1177-0. Epub 2012 Sep 30.

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

Author information

1
Prostate Cancer Discovery and Development Program, The Wistar Institute Cancer Center, 3601 Spruce Street, Philadelphia, PA 19104, USA. daltieri@wistar.org

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.

PMID:
23052217
PMCID:
PMC3727647
DOI:
10.1007/s00018-012-1177-0
[Indexed for MEDLINE]
Free PMC Article

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