ArticleJournal of biomedical science2009
Structural changes in the cytoplasmic pore of the Kir1.1 channel during pHi-gating probed by FRET.
Article in Journal of biomedical science, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 4 citations in OpenAlex.
- LRET Determination of Molecular Distances during pH Gating of the Mammalian Inward Rectifier Kir1.1b.Biophysical journal · 2018Article
- Patch-clamp fluorometry: electrophysiology meets fluorescence.Biophysical journal · 2014Review
- Structural rearrangements underlying ligand-gating in Kir channels.Nature communications · 2012Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
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Abstract
Kir1.1 channels are important in maintaining K+ homeostasis in the kidney. Intracellular acidification reversibly closes the Kir1.1 channel and thus decreases K+ secretion. In this study, we used Foster resonance energy transfer (FRET) to determine whether the conformation of the cytoplasmic pore changes in response to intracellular pH (pHi)-gating in Kir1.1 channels fused with enhanced cyan fluorescent protein (ECFP) and enhanced yellow fluorescent protein (EYFP) (ECFP-Kir1.1-EYFP). Because the fluorescence intensities of ECFP and EYFP were affected at pHi < 7.4 where pHi-gating occurs in the ECFP-Kir1.1-EYFP construct, we examined the FRET efficiencies of an ECFP-S219R-EYFP mutant, which is completed closed at pHi 7.4 and open at pHi 10.0. FRET efficiency was increased from 25% to 40% when the pHi was decreased from 10.0 to 7.4. These results suggest that the conformation of the cytoplasmic pore in the Kir1.1 channel changes in response to pHi gating such that the N- and C-termini move apart from each other at pHi 7.4, when the channel is open.
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