Structural determinants and specificities for ROMK1-phosphoinositide interaction

American Journal of Physiology. Renal Physiology
Wei-Zhong ZengChou-Long Huang

Abstract

We have recently reported that direct interaction between phosphatidylinositol bisphosphate (PIP(2)) and the COOH-terminal cytoplasmic domain of ROMK1 is important for opening of the channel. We identified arginine-188 of ROMK1 as a critical residue for this interaction. Here, we further report that substitution of a neutral amino acid for lysine-181, arginine-217, or lysine-218 decreases single-channel open probability for the full-conductance state and increases the frequency of opening at a subconductance state. Compared with wild-type ROMK1 channels, these substitution mutants also display an increased sensitivity to the block by anti-PIP(2) antibodies and to inhibition by intracellular protons. These results indicate that, like arginine-188, lysine-181, arginine-217, and lysine-218 are also involved in interactions with PIP(2) and are critical for ROMK1 to open at full conductance. Using synthetic phosphoinositides containing phosphates at different positions in the head group, we also examined the specificities of phosphoinositides in the regulation of ROMK1 channels. We found that phosphoinositides containing phosphate at both positions 4 and 5 of the inositol head group have the highest efficacy in activating ROMK1 chan...Continue Reading

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Citations

Jul 11, 2014·European Journal of Pharmacology·Chien-Hsing Lee, Horng-Huei Liou
Jan 15, 2003·Proceedings of the National Academy of Sciences of the United States of America·Tibor RohácsDiomedes E Logothetis
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Oct 9, 2014·Annual Review of Physiology·Diomedes E LogothetisLia Baki
May 24, 2007·Pflügers Archiv : European journal of physiology·Diomedes E LogothetisAvia Rosenhouse-Dantsker
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Jul 25, 2018·Molecular Neurobiology·Jonathan P GiblinXavier Gasull
Oct 12, 2007·American Journal of Physiology. Renal Physiology·Chou-Long Huang

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