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• W2127637662 abstract "Interactions between nontransmembrane domains and the lipid membrane are proposed to modulate activity of many ion channels. In Kir channels, the so-called “slide-helix” is proposed to interact with the lipid headgroups and control channel gating. We examined this possibility directly in a cell-free system consisting of KirBac1.1 reconstituted into pure lipid vesicles. Cysteine substitution of positively charged slide-helix residues (R49C and K57C) leads to loss of channel activity that is rescued by in situ restoration of charge following modification by MTSET+ or MTSEA+, but not MTSES− or neutral MMTS. Strikingly, activity is also rescued by modification with long-chain alkyl-MTS reagents. Such reagents are expected to partition into, and hence tether the side chain to, the membrane. Systematic scanning reveals additional slide-helix residues that are activated or inhibited following alkyl-MTS modification. A pattern emerges whereby lipid tethering of the N terminus, or C terminus, of the slide-helix, respectively inhibits, or activates, channel activity. This study establishes a critical role of the slide-helix in Kir channel gating, and directly demonstrates that physical interaction of soluble domains with the membrane can control ion channel activity." @default.
• W2127637662 created "2016-06-24" @default.
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• W2127637662 date "2007-08-13" @default.
• W2127637662 modified "2023-10-13" @default.
• W2127637662 title "Control of Inward Rectifier K Channel Activity by Lipid Tethering of Cytoplasmic Domains" @default.
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• W2127637662 doi "https://doi.org/10.1085/jgp.200709764" @default.
• W2127637662 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2151642" @default.
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• W2127637662 hasPublicationYear "2007" @default.
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