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

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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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Acknowledgments

This work was supported by National Institutes of Health Grants CA140043, CA78810 and CA118005.

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The author declares that no conflict of interest exists.

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

    Dario C. Altieri

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Altieri, D.C. Hsp90 regulation of mitochondrial protein folding: from organelle integrity to cellular homeostasis. Cell. Mol. Life Sci. 70, 2463–2472 (2013). https://doi.org/10.1007/s00018-012-1177-0

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