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Regulation of ROMK1 channel by protein kinase A via a phosphatidylinositol 4,5-bisphosphate-dependent mechanism
Journal article   Open access   Peer reviewed

Regulation of ROMK1 channel by protein kinase A via a phosphatidylinositol 4,5-bisphosphate-dependent mechanism

Horng-Huei Liou, Shi-Sheng Zhou and Chou-Long Huang
Proceedings of the National Academy of Sciences - PNAS, Vol.96(10), pp.5820-5825
05/11/1999
DOI: 10.1073/pnas.96.10.5820
PMCID: PMC21944
PMID: 10318968
url
https://doi.org/10.1073/pnas.96.10.5820View
Published (Version of record) Open Access

Abstract

ROMK inward-rectifier K + channels control renal K + secretion. The activity of ROMK is regulated by protein kinase A (PKA), but the molecular mechanism for regulation is unknown. Having found that direct interaction with membrane phosphatidylinositol 4,5-bisphosphate (PIP 2 ) is essential for channel activation, we investigate here the role of PIP 2 in regulation of ROMK1 by PKA. By using adenosine-5′-[γ-thio]triphosphate) (ATP[γS]) as the substrate, we found that PKA does not directly activate ROMK1 channels in membranes that are devoid of PIP 2 . Rather, phosphorylation by PKA + ATP[γS] lowers the concentration of PIP 2 necessary for activation of the channels. In solution-binding assays, anti-PIP 2 antibodies bind PIP 2 and prevent PIP 2 –channel interaction. In inside-out membrane patches, antibodies inhibit the activity of the channels. PKA treatment then decreases the sensitivity of ROMK1 for inhibition by the antibodies, indicating an enhanced interaction between PIP 2 and the phosphorylated channels. Conversely, mutation of the PKA phosphorylation sites in ROMK1 decreases PIP 2 interaction with the channels. Thus, PKA activates ROMK1 channels by enhancing PIP 2 –channel interaction.
Biological Sciences

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