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Utrophin is the autosomal homolog of dystrophin, the product of the Duchenne's muscular dystrophy (DMD) locus. Utrophin is of therapeutic interest since its over-expression can compensate dystrophin's absence. Utrophin is enriched at neuromuscular junctions due to heregulin-mediated utrophin-A promoter activation. We demonstrate that heregulin activated MSK1/2 and phosphorylated histone H3 at serine 10 in cultured C2C12 muscle cells, in an ERK-dependent manner. MSK1/2 inhibition suppressed heregulin-mediated utrophin-A activation. MSK1 over-expression potentiated heregulin-mediated utrophin-A activation and chromatin remodeling at the utrophin-A promoter. These results identify MSK1/2 as key effectors modulating utrophin-A expression as well as identify novel targets for DMD therapy.

Original publication




Journal article



Publication Date





4153 - 4158


Animals, Cells, Cultured, Chromatin Assembly and Disassembly, Enzyme Activation, Epigenesis, Genetic, Histones, Mice, Models, Genetic, Muscle Cells, Neuregulin-1, Phosphorylation, Promoter Regions, Genetic, Ribosomal Protein S6 Kinases, 90-kDa, Utrophin