NDLI: Protein kinase C mediated pH i -regulation of ROMK1 channels via a phosphatidylinositol-4,5-bisphosphate-dependent mechanism

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Protein kinase C mediated pH i -regulation of ROMK1 channels via a phosphatidylinositol-4,5-bisphosphate-dependent mechanism

Content Provider	Springer Nature Link
Author	Huang, Po Tsang Lee, Chien Hsing Liou, Horng Huei Lou, Kuo Long
Copyright Year	2011
Abstract	The protein kinase C (PKC) pathway is important for the regulation of K+ transport. The renal outer medullar K+ (ROMK1) channels show an exquisite sensitivity to intracellular protons (pH i ) (effective pK a approximately 6.8) and play a key role in K+ homeostasis during metabolic acidosis. Our molecular dynamic simulation results suggest that PKC-mediated phosphorylation on Thr-193 may disrupt the PIP2-channel interaction via a charge–charge interaction between Thr-193 and Arg-188. Therefore, we investigated the role of PKC and pH i in regulation of ROMK1 channel activity using a giant patch clamp with Xenopus oocytes expressing wild-type and mutant ROMK1 channels. ROMK1 channels pre-incubated with the PKC activator phorbol-12-myristate-13-acetate exhibited increased sensitivity to pH i (effective pK a shifted to pH approximately 7.0). In the presence of GF109203X—a PKC selective inhibitor—the effective pK a for inhibition of ROMK1 channels by pH i decreased (effective pK a shifted to pH approximately 6.5). The pH i sensitivity of ROMK1 channels mediated by PKC appeared to be dependent of PIP2 depletion. The giant patch clamp together with site direct mutagenesis revealed that Thr-193 is the phosphorylation site on PKC that regulates the pH i sensitivity of ROMK1 channels. Mutation of PKC-induced phosphorylation sites (T193A) decreases the pH i sensitivity and increases the interaction of channel-PIP2. Taken together, these results provide new insights into the molecular mechanisms underlying the pH i gating of ROMK1 channel regulation by PKC.
Starting Page	2929
Ending Page	2941
Page Count	13
File Format	PDF
ISSN	16102940
Journal	Journal of Molecular Modeling
Volume Number	18
Issue Number	7
e-ISSN	09485023
Language	English
Publisher	Springer-Verlag
Publisher Date	2011-12-03
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	PKC ROMK1 channel PIP2 Intracellular proton Effective pK a PMA Health Informatics Computer Application in Life Sciences Life Sciences Molecular Medicine Biomedicine general Computer Applications in Chemistry
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Physical and Theoretical Chemistry Computational Theory and Mathematics Catalysis Inorganic Chemistry Computer Science Applications

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Phosphatidylinositol 4,5-Bisphosphate and Intracellular pH Regulate the ROMK1 Potassium Channel via Separate but Interrelated Mechanisms

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