Quantitative Assessment of Proteome and Ubiquitinome Regulation in Skeletal Muscle following Denervation-Induced Atrophy using in vivo SILAC

摘要

In this study, the proteome and ubiquitinome of mouse GAST muscle tissue was quantified at different stages following surgical excision of sciatic nerve. A trend is observed in the differential expression of proteins, with regulation increasing over time post denervation. An interesting regulation of ubiquitinated proteins involved in canonical pathways like signalling, protein ubiquitination, metabolism, etc. is observed after one week following denervation, showing that ubiquitination plays a role in the physiological mechanisms of denervation-induced muscular atrophy and associated processes. We mapped 1100 endogenous di-Gly modified sites on mouse skeletal muscle proteins, enabling site-specific identification and quantification of ubiquitination following denervation. Increased regulation of some ubiquitinated sites not corresponding to degradation at the protein level potentially highlights other functions than proteasomal degradation.