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Signaling networks that regulate skeletal muscle contraction are highly conserved, with the current understanding that contractile proteins are targets for a wide range of kinases. However, the identification of the biological roles of phosphoproteins remains challenging due to heterogeneity. In this study, we performed a phosphoproteome analysis of the mouse tibialis anterior to identify phosphorylation events that might underlie the formation of exercise-induced muscle contracture. We compared skeletal muscles of wild-type mice with mice with either impaired or enhanced skeletal muscle contractile function (cpmt mice or dcpmt mice). Of the 1143 phosphopeptides identified, we selected 11 phosphopeptides that were differentially phosphorylated between skeletal muscles with impaired and enhanced contractile function. Five of the 11 peptides were predicted to bind to the 14-3-3 and calmodulin families. Using mass spectrometry, we verified four of the 11 phosphopeptides and four were novel. One of the novel phosphopeptides (pSer102-Ser102-Ser103) was identified as a phosphorylated form of atrogin-1 and the other novel phosphopeptides were from the sarcoplasmic reticulum proteins ATP2A1 and DPYL2. Finally, we conducted a phosphoproteome analysis of human normal and Duchenne muscular dystrophy skeletal muscles to verify our findings in mice. Our results identified a novel muscle-specific protein as a target for phosphorylation at a site that can bind to 14-3-3. This suggests that phosphorylation of the identified peptides in mice with muscle contracture may be involved in regulating protein function. This study presents the first known phosphoproteome of a mouse skeletal muscle and identification of potential phosphorylation events that regulate skeletal muscle contractility.Perinatal outcome for women with congenital heart disease and a significant pulmonary artery gradient.
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