ArticleThe Journal of biological chemistry2013
Decomposition of slide helix contributions to ATP-dependent inhibition of Kir6.2 channels.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Non-radioactive RbMethods in molecular biology (Clifton, N.J.) · 2024Article
- Gating and modulation of an inward-rectifier potassium channel.The Journal of general physiology · 2023Article
- Ligand-mediated Structural Dynamics of a Mammalian Pancreatic KJournal of molecular biology · 2022Article
- Sequence determinants of subtype-specific actions of KCNQ channel openers.The Journal of physiology · 2017Article
- Emerging complexities of lipid regulation of potassium channels.The Journal of general physiology · 2016Article
- A Conserved Residue Cluster That Governs Kinetics of ATP-dependent Gating of Kir6.2 Potassium Channels.The Journal of biological chemistry · 2015Article
- Channel function reconstitution and re-animation: a single-channel strategy in the postcrystal age.The Journal of physiology · 2015Review
- Inward rectifiers and their regulation by endogenous polyamines.Frontiers in physiology · 2014Review
- Pharmacological rescue of trafficking-impaired ATP-sensitive potassium channels.Frontiers in physiology · 2013Review
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Regulation of inwardly rectifying potassium channels by intracellular ligands couples cell membrane excitability to important signaling cascades and metabolic pathways. We investigated the molecular mechanisms that link ligand binding to the channel gate in ATP-sensitive Kir6.2 channels. In these channels, the "slide helix" forms an interface between the cytoplasmic (ligand-binding) domain and the transmembrane pore, and many slide helix mutations cause loss of function. Using a novel approach to rescue electrically silent channels, we decomposed the contribution of each interface residue to ATP-dependent gating. We demonstrate that effective inhibition by ATP relies on an essential aspartate at residue 58. Characterization of the functional importance of this conserved aspartate, relative to other residues in the slide helix, has been impossible because of loss-of-function of Asp-58 mutant channels. The Asp-58 position exhibits an extremely stringent requirement for aspartate because even a highly conservative mutation to glutamate is insufficient to restore normal channel function. These findings reveal unrecognized slide helix elements that are required for functional channel expression and control of Kir6.2 gating by intracellular ATP.
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