A Remodeled Hsp90 Molecular Chaperone Ensemble with the Novel Cochaperone Aarsd1 Is Required for Muscle Differentiation

Molecular and Cellular Biology
Pablo C EcheverríaD Picard

Abstract

Hsp90 is the ATP-consuming core component of a very abundant molecular chaperone machine that handles a substantial portion of the cytosolic proteome. Rather than one machine, it is in fact an ensemble of molecular machines, since most mammalian cells express two cytosolic isoforms of Hsp90 and a subset of up to 40 to 50 cochaperones and regulate their interactions and functions by a variety of posttranslational modifications. We demonstrate that the Hsp90 ensemble is fundamentally remodeled during muscle differentiation and that this remodeling is not just a consequence of muscle differentiation but possibly one of the drivers to accompany and to match the vast proteomic changes associated with this process. As myoblasts differentiate into myotubes, Hsp90α disappears and only Hsp90β remains, which is the only isoform capable of interacting with the novel muscle-specific Hsp90 cochaperone Aarsd1L. Artificially maintaining Hsp90α or knocking down Aarsd1L expression interferes with the differentiation of C2C12 myotubes. During muscle differentiation, Aarsd1L replaces the more ubiquitous cochaperone p23 and in doing so dampens the activity of the glucocorticoid receptor, one of the Hsp90 clients relevant to muscle functions. This ...Continue Reading

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Citations

Apr 22, 2017·Nature Reviews. Molecular Cell Biology·Florian H SchopfJohannes Buchner
Dec 23, 2017·International Journal of Molecular Sciences·Casey CarlisleDave Pilgrim
Aug 31, 2018·International Journal of Molecular Sciences·Abdullah HoterHassan Y Naim
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May 8, 2021·Cell Death & Disease·Tatiana TiagoSerena Carra
Jul 27, 2021·EMBO Reports·Jörg HöhfeldBettina Warscheid
Jan 1, 2022·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Blair TuptaArnab Ghosh

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