Related Experiment Video
Updated: May 30, 2026

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
Published on: June 7, 2018
Post-translational modifications of Hsp90 and their contributions to chaperone regulation
1National 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).
Related Concept Videos
Bacterial Protein Maturation
Molecular Chaperones and Protein Folding
The...
Molecular Chaperones and Protein Folding
The...
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.
Regulation of the Unfolded Protein Response
Protein Modifications in the RER
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.

