Journal
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
Volume 1823, Issue 3, Pages 648-655Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamcr.2011.07.018
Keywords
Heat shock protein 90; Hsp82; Post-translational modification; phosphotylation; Acetylation; Oxidation; Nitrosylation
Categories
Funding
- NIH
- National Cancer Institute
- Center for Cancer Research
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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). Published by Elsevier B.V.
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