Dystrophin is phosphorylated by endogenous protein kinases.

@article{Luise1993DystrophinIP,
  title={Dystrophin is phosphorylated by endogenous protein kinases.},
  author={Marco Luise and Cristina Presotto and Leigha Senter and Romeo Betto and Stefania Ceoldo and Sandra Furlan and Sergio Salvatori and Roger Allen Sabbadini and Giovanni Salviati},
  journal={The Biochemical journal},
  year={1993},
  volume={293 ( Pt 1)},
  pages={243-7}
}
Dystrophin, the protein coded by the gene missing in Duchenne muscular dystrophy, is assumed to be a component of the membrane cytoskeleton of skeletal muscle. Like other cytoskeletal proteins in different cell types, dystrophin bound to sarcolemma membranes was found to be phosphorylated by endogenous protein kinases. The phosphorylation of dystrophin was activated by cyclic AMP, cyclic GMP, calcium and calmodulin, and was inhibited by cyclic AMP-dependent protein kinase peptide inhibitor… CONTINUE READING