Article
Protein kinase C (PKC)-induced phosphorylation of ROMK1 is essential for the surface expression of ROMK1 channels.
The Journal of biological chemistry - 15 Nov 2002
Lin DaoHong, Sterling Hyacinth, Lerea Kenneth M, Giebisch Gerhard, Wang Wen-Hui
Abstract excerpt
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...
Topics
- Adenosine Triphosphate
- Animals
- Barium
- Blotting, Western
- COS Cells
- Cell Line
- Escherichia coli
- Green Fluorescent Proteins
- Humans
- Immunohistochemistry
- Luminescent Proteins
- Microscopy, Confocal
- Microscopy, Fluorescence