Post-translational modifications of Hsp90 and translating the chaperone code.

The Journal of Biological Chemistry
Sarah J BackeMehdi Mollapour

Abstract

Cells have a remarkable ability to synthesize large amounts of protein in a very short period of time. Under these conditions, many hydrophobic surfaces on proteins may be transiently exposed, and the likelihood of deleterious interactions is quite high. To counter this threat to cell viability, molecular chaperones have evolved to help nascent polypeptides fold correctly and multimeric protein complexes assemble productively, while minimizing the danger of protein aggregation. Heat shock protein 90 (Hsp90) is an evolutionarily conserved molecular chaperone that is involved in the stability and activation of at least 300 proteins, also known as clients, under normal cellular conditions. The Hsp90 clients participate in the full breadth of cellular processes, including cell growth and cell cycle control, signal transduction, DNA repair, transcription, and many others. Hsp90 chaperone function is coupled to its ability to bind and hydrolyze ATP, which is tightly regulated both by co-chaperone proteins and post-translational modifications (PTMs). Many reported PTMs of Hsp90 alter chaperone function and consequently affect myriad cellular processes. Here, we review the contributions of PTMs, such as phosphorylation, acetylation, SU...Continue Reading

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Citations

Feb 10, 2021·Cell Stress & Chaperones·Patricija van Oosten-HawleAndrew W Truman
Mar 21, 2021·Nature Reviews. Drug Discovery·Qin WuDalia Barsyte-Lovejoy
Oct 6, 2020·Cellular Signalling·Akhil Kotwal, Sreedhar Amere Subbarao
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Sep 30, 2021·Cell Stress & Chaperones·Mark R WoodfordMehdi Mollapour
Aug 11, 2021·Annual Review of Microbiology·Sue WicknerOlivier Genest

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