Identification of Ser38 as the site in cardiac sarcoplasmic reticulum Ca(2+)-ATPase that is phosphorylated by Ca2+/calmodulin-dependent protein kinase.

@article{Toyofuku1994IdentificationOS,
  title={Identification of Ser38 as the site in cardiac sarcoplasmic reticulum Ca(2+)-ATPase that is phosphorylated by Ca2+/calmodulin-dependent protein kinase.},
  author={Toshihiko Toyofuku and K Curotto Kurzydlowski and N. Narayanan and David MacLennan},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 42},
  pages={26492-6}
}
In previous studies (Xu, A., Hawkins, C., and Narayanan, N. (1993) J. Biol. Chem. 268, 8394-8397), the Ca(2+)-ATPase of cardiac muscle sarcoplasmic reticulum (SERCA2) was shown to be phosphorylated by Ca2+/calmodulin-dependent protein kinase II (CaM kinase) on a serine residue, likely to be either Ser38, Ser167, or Ser531. SERCA2 and SERCA2 mutants S38A, S167A, and S531A were expressed in HEK-293 cells and tested for phosphorylation with CaM kinase. Mutant S38A was not phosphorylated, while… CONTINUE READING

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