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October 11, 1999The Journal of General PhysiologyOpen Access

A Mutation Linked with Bartter's Syndrome Locks Kir 1.1a (Romk1) Channels in a Closed State

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Population

Oocyte model expressing wild-type and mutant inward rectifying renal K(+) channels (Kir 1.1a / ROMK)

Comparison

Expression of truncated mutant channels and… vs Wild-type Kir 1.1a channels

Design

Preclinical

Authors

TFThomas P. FlaggMTMargaret TateJMJean Mérot

Discussion

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Overview

No immediate clinical implications for Bartter syndrome; leaves open therapeutic targeting of the Kir1.1 COOH terminus.

Structured PICO

P
Population
Oocyte model expressing wild-type and mutant inward rectifying renal K(+) channels (Kir 1.1a / ROMK)
I
Intervention
Expression of truncated mutant channels (Kir 1.1a 331X, Kir 1.1a 351X) and coexpression with wild-type subunits
C
Comparator
Wild-type Kir 1.1a channels
O
Outcome
Channel activity, plasmalemma localization, and open-state occupancysurrogate

The study identifies the extreme COOH terminus of the Kir 1.1a channel as a critical domain for subunit oligomerization and open-state stabilization, providing a mechanistic basis for the loss of function in a Bartter's syndrome mutation.

Cite This Study

Flagg et al. (1999) studied this question.

synapsesocial.com/papers/6a815b8526f0d7dff79cd5bahttps://doi.org/10.1085/jgp.114.5.685
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Also Consider

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

  1. 1Regulation of ROMK1 K+ channel activity involves phosphorylation processes.1994 · 140 citations
  2. 2K <sub>ATP</sub> channel inhibition by ATP requires distinct functional domains of the cytoplasmic C terminus of the pore-forming subunit1998 · 197 citations
  3. 3Localization of the ROMK protein on apical membranes of rat kidney nephron segments1997 · 195 citations
  4. 4Is the secretory K channel in the rat CCT ROMK?1997 · 93 citations
  5. 5Characterization of stretch‐activated ion channels in Xenopus oocytes.1990 · 104 citations