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NMJ formation depends on the Agrin\/Lrp4\/MuSK\/Dok\u20107 signaling pathway. However, signaling downstream of Dok\u20107 remains incompletely understood. Here we used the phosphorylated iTRAQ technique to identify downstream molecules of Dok\u20107 in muscle cells. We found 16 Agrin\/Dok\u20107\u2010mediated serine\/threonine phosphorylated proteins, and we validated the role of one phosphorylated protein, JPH2, in regulating AChR clustering. Our phosphoproteomics analysis sheds light on the underappreciated signaling network downstream of Agrin\/Dok\u20107, thus providing new clues for understanding pathogenesis and developing treatment methods for neuromuscular diseases.<\/jats:p>","DOI":"10.1002\/1873-3468.70050","type":"journal-article","created":{"date-parts":[[2025,4,28]],"date-time":"2025-04-28T06:04:23Z","timestamp":1745820263000},"page":"2142-2156","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Agrin\/Dok\u20107\u2010induced\n                    <scp>JPH<\/scp>\n                    2 phosphorylation in muscle cells is involved in\n                    <scp>AC<\/scp>\n                    h\n                    <scp>R<\/scp>\n                    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