title: Post-translational modifications of Hsp90 and their contributions to chaperone regulation.
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).
authors.affiliation: National Cancer Institute, Bethesda, MD, USA. mollapourm@mail.nih.gov
authors.forename: Mehdi
authors.initials: M
authors.lastname: Mollapour
authors.forename: Len
authors.initials: L
authors.lastname: Neckers
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D018841:HSP90 Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D018832:Molecular Chaperones / Q000235:genetics / Q000378:metabolism*; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational
chemical_list: D018841:HSP90 Heat-Shock Proteins; D018832:Molecular Chaperones; D000255:Adenosine Triphosphate