ArticleThe Journal of physiology2002
Molecular mechanism of a COOH-terminal gating determinant in the ROMK channel revealed by a Bartter's disease mutation.
Article in The Journal of physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 26 citations in OpenAlex.
- Regulation of transport in the connecting tubule and cortical collecting duct.Comprehensive Physiology · 2012Review
- Hypertension resistance polymorphisms in ROMK (Kir1.1) alter channel function by different mechanisms.American journal of physiology. Renal physiology · 2010Article
- CFTR chloride channel in the apical compartments: spatiotemporal coupling to its interacting partners.Integrative biology : quantitative biosciences from nano to macro · 2010Review
- A comprehensive guide to the ROMK potassium channel: form and function in health and disease.American journal of physiology. Renal physiology · 2009Review
- MUPP1 complexes renal K+ channels to alter cell surface expression and whole cell currents.American journal of physiology. Renal physiology · 2009Article
- C-terminal determinants of Kir4.2 channel expression.The Journal of membrane biology · 2006Article
- Molecular diversity and regulation of renal potassium channels.Physiological reviews · 2005Review
- The human tumour suppressor gene SLC5A8 expresses a Na+-monocarboxylate cotransporter.The Journal of physiology · 2004Article
- 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
6 authors at 3 institutions in 1 country.
Funding
Abstract
The ROMK subtypes of inward-rectifier K(+) channels mediate potassium secretion and regulate NaCl reabsorption in the kidney. Loss-of-function mutations in this pH-sensitive K(+) channel cause Bartter's disease, a familial salt wasting nephropathy. One disease-causing mutation truncates the extreme COOH-terminus and induces a closed gating conformation. Here we identify a region within the deleted domain that plays an important role in pH-dependent gating. The domain contains a structural element that functionally interacts with the pH sensor in the cytoplasmic NH(2)-terminus to set a physiological range of pH sensitivity. Removal of the domain shifts the pK(a) towards alkaline pH values, causing channel inactivation under physiological conditions. Suppressor mutations within the pH sensor rescued channel gating and trans addition of the cognate peptide restored pH sensitivity. A specific interdomain interaction was revealed in an in vitro protein-protein binding assay between the NH(2)- and COOH-terminal cytoplasmic domains expressed as bacterial fusion proteins. These results provide new insights into the molecular mechanisms underlying Kir channel regulation and channel gating defects that are associated with Bartter's disease.
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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.