Mapping of the contraction-induced phosphoproteome identifies TRIM28 as a significant regulator of skeletal muscle size and function.

Autor:	Steinert ND; Department of Comparative Biosciences, University of Wisconsin-Madison, Madison, WI, USA; School of Veterinary Medicine, University of Wisconsin-Madison, Madison, WI, USA., Potts GK; Department of Chemistry, University of Wisconsin-Madison, Madison, WI, USA., Wilson GM; Department of Chemistry, University of Wisconsin-Madison, Madison, WI, USA., Klamen AM; Department of Comparative Biosciences, University of Wisconsin-Madison, Madison, WI, USA; School of Veterinary Medicine, University of Wisconsin-Madison, Madison, WI, USA., Lin KH; Department of Comparative Biosciences, University of Wisconsin-Madison, Madison, WI, USA; School of Veterinary Medicine, University of Wisconsin-Madison, Madison, WI, USA., Hermanson JB; Department of Comparative Biosciences, University of Wisconsin-Madison, Madison, WI, USA; School of Veterinary Medicine, University of Wisconsin-Madison, Madison, WI, USA., McNally RM; Department of Comparative Biosciences, University of Wisconsin-Madison, Madison, WI, USA; School of Veterinary Medicine, University of Wisconsin-Madison, Madison, WI, USA., Coon JJ; Department of Chemistry, University of Wisconsin-Madison, Madison, WI, USA; Genome Center of Wisconsin, University of Wisconsin-Madison, Madison, WI, USA; Morgridge Institute for Research, Madison, WI, USA; Department of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, WI, USA., Hornberger TA; Department of Comparative Biosciences, University of Wisconsin-Madison, Madison, WI, USA; School of Veterinary Medicine, University of Wisconsin-Madison, Madison, WI, USA. Electronic address: troy.hornberger@wisc.edu.
Jazyk:	angličtina
Zdroj:	Cell reports [Cell Rep] 2021 Mar 02; Vol. 34 (9), pp. 108796.
DOI:	10.1016/j.celrep.2021.108796
Abstrakt:	Mechanical signals, such as those evoked by maximal-intensity contractions (MICs), can induce an increase in muscle mass. Rapamycin-sensitive signaling events are widely implicated in the regulation of this process; however, recent studies indicate that rapamycin-insensitive signaling events are also involved. Thus, to identify these events, we generate a map of the MIC-regulated and rapamycin-sensitive phosphoproteome. In total, we quantify more than 10,000 unique phosphorylation sites and find that more than 2,000 of these sites are significantly affected by MICs, but remarkably, only 38 of the MIC-regulated events are mediated through a rapamycin-sensitive mechanism. Further interrogation of the rapamycin-insensitive phosphorylation events identifies the S473 residue on Tripartite Motif-Containing 28 (TRIM28) as one of the most robust MIC-regulated phosphorylation sites, and extensive follow-up studies suggest that TRIM28 significantly contributes to the homeostatic regulation of muscle size and function as well as the hypertrophy that occurs in response to increased mechanical loading. Competing Interests: Declaration of interests The authors declare no conflicts of interest. (Copyright © 2021 The Author(s). Published by Elsevier Inc. All rights reserved.)
Databáze:	MEDLINE
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