ArticleProceedings of the National Academy of Sciences of the United States of America2006
Subunit-subunit interactions are critical for proton sensitivity of ROMK: evidence in support of an intermolecular gating mechanism.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed, 34 citations in OpenAlex.
- Genome mining yields putative disease-associated ROMK variants with distinct defects.PLoS genetics · 2023Article
- Comparison of KHandbook of experimental pharmacology · 2021Article
- Three Decades of Chloride Intracellular Channel Proteins: From Organelle to Organ Physiology.Current protocols in pharmacology · 2018Review
- Inwardly Rectifying KNeurochemical research · 2017Article
- Inter-subunit disulfide locking of the human P2X3 receptor elucidates ectodomain movements associated with channel gating.Purinergic signalling · 2016Article
- Article
- Molecular aspects of structure, gating, and physiology of pH-sensitive background K2P and Kir K+-transport channels.Physiological reviews · 2015Review
- Protein kinase C mediated pH(i)-regulation of ROMK1 channels via a phosphatidylinositol-4,5-bisphosphate-dependent mechanism.Journal of molecular modeling · 2012Article
- Regulation of transport in the connecting tubule and cortical collecting duct.Comprehensive Physiology · 2012Review
- Separate gating mechanisms mediate the regulation of K2P potassium channel TASK-2 by intra- and extracellular pH.The Journal of biological chemistry · 2010Article
- Rearrangements in the relative orientation of cytoplasmic domains induced by a membrane-anchored protein mediate modulations in Kv channel gating.The Journal of biological chemistry · 2009Article
- A comprehensive guide to the ROMK potassium channel: form and function in health and disease.American journal of physiology. Renal physiology · 2009Review
- Structural changes in the cytoplasmic pore of the Kir1.1 channel during pHi-gating probed by FRET.Journal of biomedical science · 2009Article
- Long-pore electrostatics in inward-rectifier potassium channels.The Journal of general physiology · 2008Article
- Molecular mechanism of pH sensing in KcsA potassium channels.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Destabilization of ATP-sensitive potassium channel activity by novel KCNJ11 mutations identified in congenital hyperinsulinism.The Journal of biological chemistry · 2008Article
- Article
- Role of conserved glycines in pH gating of Kir1.1 (ROMK).Biophysical journal · 2006Article
- Random mutagenesis screening indicates the absence of a separate H(+)-sensor in the pH-sensitive Kir channels.Channels (Austin, Tex.)Article
- The Kir channel immunoglobulin domain is essential for Kir1.1 (ROMK) thermodynamic stability, trafficking and gating.Channels (Austin, Tex.)Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The tetrameric K channel ROMK provides an important pathway for K secretion by the mammalian kidney, and the gating of this channel is highly sensitive to changes in cytosolic pH. Although charge-charge interactions have been implicated in pH sensing by this K channel tetramer, the molecular mechanism linking pH sensing and the gating of ion channels is poorly understood. The x-ray crystal structure KirBac1.1, a prokaryotic ortholog of ROMK, has suggested that channel gating involves intermolecular interactions of the N- and C-terminal domains of adjacent subunits. Here we studied channel gating behavior to changes in pH using giant patch clamping of Xenopus laevis oocytes expressing WT or mutant ROMK, and we present evidence that no single charged residue provides the pH sensor. Instead, we show that N-C- and C-C-terminal subunit-subunit interactions form salt bridges, which function to stabilize ROMK in the open state and which are modified by protons. We identify a highly conserved C-C-terminal arginine-glutamate (R-E) ion pair that forms an intermolecular salt bridge and responds to changes in proton concentration. Our results support the intermolecular model for pH gating of inward rectifier K channels.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.