Calmodulin binding to M-type K+ channels assayed by TIRF/FRET in living cells.

@article{Bal2008CalmodulinBT,
  title={Calmodulin binding to M-type K+ channels assayed by TIRF/FRET in living cells.},
  author={Manjot Bal and Oleg Leonidovych Zaika and Pamela Martin and Mark S. Shapiro},
  journal={The Journal of physiology},
  year={2008},
  volume={586 9},
  pages={2307-20}
}
Calmodulin (CaM) binds to KCNQ2-4 channels within their carboxy termini, where it regulates channel function. The existing data have not resolved the Ca2+ dependence of the interaction between the channels and CaM. We performed glutathione S-transferase (GST)-pull-down assays between purified KCNQ2-4 carboxy termini and CaM proteins to determine the Ca2+ dependence of the interaction in vitro. The assays showed substantial Ca2+ dependence of the interaction of the channels with wild-type (WT… CONTINUE READING

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