Phosphorylation of smooth muscle caldesmon by mitogen-activated protein (MAP) kinase and expression of MAP kinase in differentiated smooth muscle cells.

@article{Childs1992PhosphorylationOS,
  title={Phosphorylation of smooth muscle caldesmon by mitogen-activated protein (MAP) kinase and expression of MAP kinase in differentiated smooth muscle cells.},
  author={Timothy Childs and Mark H Watson and Jasbinder S. Sanghera and Donald L. Campbell and Steven Pelech and Alan S. Mak},
  journal={The Journal of biological chemistry},
  year={1992},
  volume={267 32},
  pages={22853-9}
}
Smooth muscle caldesmon was phosphorylated in vitro by sea star p44mpk up to 2.0 mol of phosphate/mol of protein at both Ser and Thr residues. The phosphorylation sites were contained mainly in the COOH-terminal 10-kDa cyanogen bromide fragment which houses the binding sites for calmodulin, tropomyosin, and F-actin. Tryptic peptide maps of 32P-labeled caldesmon by p44mpk and p34cdc2 showed that while both enzymes recognized similar sites of phosphorylation, they have different preferred sites… CONTINUE READING
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