Global Analysis of Muscle-specific Kinase Signaling by Quantitative Phosphoproteomics

• DOI: 10.1074/mcp.m113.036087
• Publication Date: 2014-06-05T04:18:30Z
• Authors: Gerhard Dürnberger; Bahar Z. Camurdan...; Matthias Tomschik; Michael Schutzbier; Elisabeth Roitinger; Otto Hudecz; Karl Mechtler; Ruth Herbst
• Keywords: Phosphoproteomics; Cell Signaling

The development of the neuromuscular synapse depends on signaling processes that involve protein phosphorylation as a crucial regulatory event. Muscle-specific kinase (MuSK) is key molecule at whose activity required for formation mature and functional synapse. However, cascade downstream MuSK regulation different components are still poorly understood. In this study we used quantitative phosphoproteomics approach to events their temporal MuSK. We identified total 10,183 phosphopeptides, which 203 were significantly up- or down-regulated. Regulated phosphopeptides classified into four clusters according profiles. Within these found an overrepresentation specific classes associated with cellular functions. particular, enrichment regulated phosphoproteins involved in posttranscriptional mechanisms cytoskeletal organization. These findings provide novel insights complex network form basis future mechanistic studies.