ArticleThe Journal of general physiology1998
Mechanism of ATP-sensitive K channel inhibition by sulfhydryl modification.
Article in The Journal of general physiology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 36 citations in OpenAlex.
- Redox Regulation of KAntioxidants & redox signaling · 2024Review
- Fatiguing contractions increase protein S-glutathionylation occupancy in mouse skeletal muscle.Redox biology · 2018Article
- Postranslational Modification of Ion Channels in Colonic Inflammation.Current neuropharmacology · 2015Review
- Hydrogen sulfide as endothelium-derived hyperpolarizing factor sulfhydrates potassium channels.Circulation research · 2011Article
- Redox regulation of the mitochondrial K(ATP) channel in cardioprotection.Biochimica et biophysica acta · 2011Article
- Molecular basis and structural insight of vascular K(ATP) channel gating by S-glutathionylation.The Journal of biological chemistry · 2011Article
- Oxidative stress and beta-cell dysfunction.Pflugers Archiv : European journal of physiology · 2010Review
- Nitric oxide activates ATP-sensitive potassium channels in mammalian sensory neurons: action by direct S-nitrosylation.Molecular pain · 2009Article
- Molecular mechanisms and clinical implications of reversible protein S-glutathionylation.Antioxidants & redox signaling · 2008Review
- ATP8A1 activity and phosphatidylserine transbilayer movement.Journal of receptor, ligand and channel research · 2008Article
- Determinant role of membrane helices in K ATP channel gating.The Journal of membrane biology · 2005Article
- Identification of residues contributing to the ATP binding site of Kir6.2.The EMBO journal · 2003Article
- Mechanism of Kir6.2 channel inhibition by sulfhydryl modification: pore block or allosteric gating?The Journal of physiology · 2002Article
- Interaction of stilbene disulphonates with cloned K(ATP) channels.British journal of pharmacology · 2001Article
- Cytoplasmic amino and carboxyl domains form a wide intracellular vestibule in an inwardly rectifying potassium channel.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- Molecular analysis of ATP-sensitive K channel gating and implications for channel inhibition by ATP.The Journal of general physiology · 1998Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ATP-sensitive potassium (KATP) channels are reversibly inhibited by intracellular ATP. Agents that interact with sulfhydryl moieties produce an irreversible inhibition of KATP channel activity when applied to the intracellular membrane surface. ATP appears to protect against this effect, suggesting that the cysteine residue with which thiol reagents interact may either lie within the ATP-binding site or be inaccessible when the channel is closed. We have examined the interaction of the membrane-impermeant thiol-reactive agent p-chloromercuriphenylsulphonate (pCMPS) with the cloned beta cell KATP channel. This channel comprises the pore-forming Kir6.2 and regulatory SUR1 subunits. We show that the cysteine residue involved in channel inhibition by pCMPS resides on the Kir6.2 subunit and is located at position 42, which lies within the NH2 terminus of the protein. Although ATP protects against the effects of pCMPS, the ATP sensitivity of the KATP channel was unchanged by mutation of C42 to either valine (V) or alanine (A), suggesting that ATP does not interact directly with this residue. These results are consistent with the idea that C42 is inaccessible to the intracellular solution, and thereby protected from interaction with pCMPS when the channel is closed by ATP. We also observed that the C42A mutation does not affect the ability of SUR1 to endow Kir6.2 with diazoxide sensitivity, and reduces, but does not prevent, the effects of MgADP and tolbutamide, which are mediated via SUR1. The Kir6.2-C42A (or V) mutant channel may provide a suitable background for cysteine-scanning mutagenesis studies.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.