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December 1, 1998Journal of Biological ChemistryOpen Access

pH-dependent Gating of ROMK (Kir1.1) Channels Involves Conformational Changes in Both N and C Termini

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Population

ROMK (Kir1.1) channels

Design

Preclinical

Authors

USUwe SchulteHHHartmut HahnHWHeinrich Wiesinger

Discussion

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Overview

Indicates dual-terminal movement in Kir1.1 pH gating; leaves open applicability to human cardiovascular channel regulation.

Structured PICO

P
Population
ROMK (Kir1.1) channels
I
Intervention
Mutagenesis of intracellular cysteines and exposure to water-soluble oxidants and sulfhydryl reagents
O
Outcome
Reactivity of cysteine residues (Cys49 and Cys308) to thiol reagents in open vs closed statessurrogate

The study demonstrates that pH-dependent gating of Kir1.1 channels involves conformational changes in both the N and C termini.

Cite This Study

Schulte et al. (1998) studied this question.

synapsesocial.com/papers/6a962012fb86bd36df01c67bhttps://doi.org/10.1074/jbc.273.51.34575
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Extracellular K+ and Intracellular pH Allosterically Regulate Renal Kir1.1 Channels1996 · 74 citations
  2. 2Regulation of ROMK1 K+ channel activity involves phosphorylation processes.1994 · 140 citations
  3. 3Phosphorylation of the ATP-sensitive, Inwardly Rectifying K+ Channel, ROMK, by Cyclic AMP-dependent Protein Kinase1996 · 135 citations
  4. 4Activation of the atrial K <sub>ACh</sub> channel by the βγ subunits of G proteins or intracellular Na <sup>+</sup> ions depends on the presence of phosphatidylinositol phosphates1998 · 246 citations
  5. 5Acetylcholine Receptor Channel Structure Probed in Cysteine-Substitution Mutants1992 · 673 citations