Phosphorylation of Ser-3 of cofilin regulates its essential function on actin.

@article{Moriyama1996PhosphorylationOS,
  title={Phosphorylation of Ser-3 of cofilin regulates its essential function on actin.},
  author={Kenji Moriyama and Kazuko Iida and Ichiro Yahara},
  journal={Genes to cells : devoted to molecular & cellular mechanisms},
  year={1996},
  volume={1 1},
  pages={73-86}
}
BACKGROUND Cofilin is a low-molecular weight actin-modulating protein, and is structurally and functionally conserved in eucaryotes from yeast to mammals. The functions of cofilin appear to be regulated by phosphorylation and dephosphorylation. RESULTS A proteolytic study of phosphorylated porcine cofilin and expression of a mutated cofilin in cultured cells revealed that Ser-3 is the unique phosphorylation site. Phosphorylated cofilin was found not to bind to either F- or G-actin while… CONTINUE READING
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