NDLI: Regulation of ROMK1 K+ channel activity involves phosphorylation processes.

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Regulation of ROMK1 K+ channel activity involves phosphorylation processes.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Wang, W. Ho, K. Giebisch, G. Mcnicholas, C. M. Hebert, S. C.
Description	Author Affiliation: McNicholas CM ( Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT 06510.);
Abstract	An inwardly rectifying, ATP-regulated K+ channel with a distinctive molecular architecture, ROMK1, was recently cloned from rat kidney. Using patch clamp techniques, we have investigated the regulation of ROMK1 with particular emphasis on phosphorylation/dephosphorylation processes. Spontaneous channel rundown occurred after excision of membrane patches into ATP-free bath solutions in the presence of Mg2+. Channel rundown was almost completely abolished after excision of patches into either Mg(2+)-free bathing solutions or after preincubation with the broad-spectrum phosphatase inhibitor, orthovanadate, in the presence of Mg2+. MgATP preincubation also inhibited channel rundown in a dose-dependent manner. In addition, the effect of the specific phosphatase inhibitors okadaic acid (1 microM) and calyculin A (1 microM) was also investigated. The presence of either okadaic acid or calyculin A failed to inhibit channel rundown. Taken together, these data suggest that rundown of ROMK1 involves a Mg(2+)-dependent dephosphorylation process. Channel activity was also partially restored after the addition of MgATP to the bath solution. Addition of exogenous cAMP-dependent protein kinase A (PKA) catalytic subunit led to a further increase in channel open probability. Addition of Na2ATP, in the absence of Mg2+, was ineffective, suggesting that restoration of channel activity is a Mg(2+)-dependent process. Addition of the specific PKA inhibitor, PKI, to the bath solution led to a partial, reversible inhibition in channel activity. Thus, PKA-dependent phosphorylation processes are involved in the modulation of channel activity. This observation is consistent with the presence of potential PKA phosphorylation sites on ROMK1.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	17
Volume Number	91
Language	English
Publisher	National Academy of Sciences
Publisher Date	1994-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Kidney Physiology Potassium Channels, Inwardly Rectifying Potassium Channels Adenosine Triphosphate Pharmacology Animals Cloning, Molecular Cyclic AMP-Dependent Protein Kinases Antagonists & Inhibitors Metabolism Ethers, Cyclic Ion Channel Gating Kinetics Magnesium Membrane Potentials Drug Effects Okadaic Acid Oocytes Oxazoles Phosphoprotein Phosphatases Phosphorylation Biosynthesis Time Factors Vanadates Xenopus Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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