Regulation of surface localization of the small conductance Ca2+-activated potassium channel, Sk2, through direct phosphorylation by cAMP-dependent protein kinase.

@article{Ren2006RegulationOS,
  title={Regulation of surface localization of the small conductance Ca2+-activated potassium channel, Sk2, through direct phosphorylation by cAMP-dependent protein kinase.},
  author={Yajun Ren and Lyndon Forbes Barnwell and Jon C. Alexander and Farah D Lubin and John P Adelman and Paul J. Pfaffinger and Laura A Schrader and Anne E. Anderson},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 17},
  pages={11769-79}
}
Small conductance, Ca2+-activated voltage-independent potassium channels (SK channels) are widely expressed in diverse tissues; however, little is known about the molecular regulation of SK channel subunits. Direct alteration of ion channel subunits by kinases is a candidate mechanism for functional modulation of these channels. We find that activation of cyclic AMP-dependent protein kinase (PKA) with forskolin (50 microm) causes a dramatic decrease in surface localization of the SK2 channel… CONTINUE READING

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Naunyn-Schmiedeberg’s Arch. Pharmacol

  • R. Markstein, M. Matsumoto, C. Kohler, H. Togashi, M. Yoshioka, D. Hoyer
  • APRIL 28,
  • 1999

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