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. 1999 Sep 6;146(5):1133–1146. doi: 10.1083/jcb.146.5.1133

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© 1999 The Rockefeller University Press

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

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Tyrosine phosphorylation of MuSK ectodomain mutants. MuSK ^−/− myotubes were transfected with the indicated constructs (Fig. 2 a), treated with agrin for 10 min (+) or left untreated (−), and then subjected to immunoprecipitation with anti-MuSK. Immunoblots were probed with antiphosphotyrosine (a), stripped, and reprobed with anti-MuSK (b). (lanes 1 and 2) Untransfected myoblasts; (lanes 3 and 4) myoblasts transfected with wild-type MuSK (construct 1); (lanes 5 and 6) myoblasts transfected with construct 11; and (lanes 7 and 8) myoblasts transfected with construct 13. Wild-type MuSK and construct 11, both of which mediate agrin-induced AChR clustering, also show agrin-dependent tyrosine phosphorylation. Mutant 13, which does not mediate agrin-dependent tyrosine phosphorylation, shows a high level of agrin-independent phosphorylation but only slight agrin-dependent phosphorylation.