Protein kinase C mediated pHi-regulation of ROMK1 channels via a phosphatidylinositol-4,5-bisphosphate-dependent mechanism
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- 作者：Po-Tsang Huang (1)
Chien-Hsing Lee (234)
Horng-Huei Liou (25) hhl@ntu.edu.tw
Kuo-Long Lou (1678) kllou@ntu.edu.tw - 关键词：PKC – ; ROMK1 channel – ; PIP2 – ; Intracellular proton – ; Effective pK a – ; PMA
- 刊名：Journal of Molecular Modeling
- 出版年：2012
- 出版时间：July 2012
- 年：2012
- 卷：18
- 期：7
- 页码：2929-2941
- 全文大小：892.2 KB
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- 刊物类别：Chemistry and Materials Science
- 刊物主题：Chemistry
Computer Applications in Chemistry
Biomedicine
Molecular Medicine
Health Informatics and Administration
Life Sciences
Computer Application in Life Sciences - 出版者：Springer Berlin / Heidelberg
- ISSN：0948-5023
文摘
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.