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Biochim Biophys Acta. 2012 Mar;1823(3):648-55. doi: 10.1016/j.bbamcr.2011.07.018. Epub 2011 Aug 10.

Post-translational modifications of Hsp90 and their contributions to chaperone regulation.

Author information

1
National Cancer Institute, Bethesda, MD, USA. mollapourm@mail.nih.gov

Abstract

Molecular chaperones, as the name suggests, are involved in folding, maintenance, intracellular transport, and degradation of proteins as well as in facilitating cell signaling. Heat shock protein 90 (Hsp90) is an essential eukaryotic molecular chaperone that carries out these processes in normal and cancer cells. Hsp90 function in vivo is coupled to its ability to hydrolyze ATP and this can be regulated by co-chaperones and post-translational modifications. In this review, we explore the varied roles of known post-translational modifications of cytosolic and nuclear Hsp90 (phosphorylation, acetylation, S-nitrosylation, oxidation and ubiquitination) in fine-tuning chaperone function in eukaryotes. This article is part of a Special Issue entitled: Heat Shock Protein 90 (HSP90).

PMID:
21856339
PMCID:
PMC3226900
DOI:
10.1016/j.bbamcr.2011.07.018
[Indexed for MEDLINE]
Free PMC Article

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