Protein kinase C (PKC)-induced phosphorylation of ROMK1 is essential for the surface expression of ROMK1 channels.

@article{Lin2002ProteinKC,
  title={Protein kinase C (PKC)-induced phosphorylation of ROMK1 is essential for the surface expression of ROMK1 channels.},
  author={Daohong Lin and Hyacinth Sterling and Kenneth M Lerea and Gerhard Giebisch and Wenhui Wang},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 46},
  pages={44278-84}
}
We carried out in vitro phosphorylation assays to determine whether ROMK1 is a substrate of protein kinase C (PKC) and used the two-electrode voltage clamp method to investigate the role of serine residues 4, 183, and 201, the three putative PKC phosphorylation sites, in the regulation of ROMK1 channel activity. Incubation of the purified His-tagged ROMK1 protein with PKC and radiolabeled ATP resulted in (32)P incorporation into ROMK1 detected by autoradiography. Moreover, the in vitro… CONTINUE READING