ArticleBiophysical journal2003
Molecular basis for Kir6.2 channel inhibition by adenine nucleotides.
Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
18 citing papers in PubMed, 48 citations in OpenAlex.
- Dynamic duo: Kir6 and SUR in KChannels (Austin, Tex.) · 2024Review
- The Importance of Molecular Genetic Testing for Precision Diagnostics, Management, and Genetic Counseling in MODY Patients.International journal of molecular sciences · 2024Article
- Cryo-electron microscopy structures and progress toward a dynamic understanding of KThe Journal of general physiology · 2018Review
- Functional mapping of the N-terminal arginine cluster and C-terminal acidic residues of Kir6.2 channel fused to a G protein-coupled receptor.Biochimica et biophysica acta. Biomembranes · 2017Article
- KATP Channels in the Cardiovascular System.Physiological reviews · 2016Review
- Muscle KATP channels: recent insights to energy sensing and myoprotection.Physiological reviews · 2010Review
- Impact of disease-causing SUR1 mutations on the KATP channel subunit interface probed with a rhodamine protection assay.The Journal of biological chemistry · 2010Article
- How ATP inhibits the open K(ATP) channel.The Journal of general physiology · 2008Article
- Remodelling of the SUR-Kir6.2 interface of the KATP channel upon ATP binding revealed by the conformational blocker rhodamine 123.The Journal of physiology · 2007Article
- ATP-sensitive K+ channels: regulation of bursting by the sulphonylurea receptor, PIP2 and regions of Kir6.2.The Journal of physiology · 2006Article
- ATP sensitivity of ATP-sensitive K+ channels: role of the gamma phosphate group of ATP and the R50 residue of mouse Kir6.2.The Journal of physiology · 2005Article
- Novel nucleotide-binding sites in ATP-sensitive potassium channels formed at gating interfaces.The EMBO journal · 2005Article
- Modeling regulation of cardiac KATP and L-type Ca2+ currents by ATP, ADP, and Mg2+.Biophysical journal · 2005Article
- Functional analysis of a structural model of the ATP-binding site of the KATP channel Kir6.2 subunit.The EMBO journal · 2005Article
- Concerted gating mechanism underlying KATP channel inhibition by ATP.Biophysical journal · 2004Article
- Long-chain acyl-CoA esters and phosphatidylinositol phosphates modulate ATP inhibition of KATP channels by the same mechanism.The Journal of physiology · 2003Article
- Molecular mechanism for ATP-dependent closure of the K+ channel Kir6.2.The Journal of physiology · 2003Article
- Identification of residues contributing to the ATP binding site of Kir6.2.The EMBO journal · 2003Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
K(ATP) channels are comprised of a pore-forming protein, Kir6.x, and the sulfonylurea receptor, SURx. Interaction of adenine nucleotides with Kir6.2 positively charged amino acids such as K185 and R201 on the C-terminus causes channel closure. Substitution of these amino acids with other positively charged residues had small effects on inhibition by adenine nucleotide, while substitution with neutral or negative residues had major effects, suggesting electrostatic interactions between Kir6.2 positive charges and adenine nucleotide negative phosphate groups. Furthermore, R201 mutation decreased channel sensitivity to ATP, ADP, and AMP to a similar extent, but K185 mutation decreased primarily ATP and ADP sensitivity, leaving the AMP sensitivity relatively unaffected. Thus, channel inhibition by ATP may involve interaction of the alpha-phosphate with R201 and interaction of the beta-phosphate with K185. In addition, decreased open probability due to rundown or sulfonylureas caused an increase in ATP sensitivity in the K185 mutant, but not in the R201 mutant. Thus, the beta-phosphate may bind in a state-independent fashion to K185 to destabilize channel openings, while R201 interacts with the alpha-phosphate to stabilize a channel closed configuration. Substitution of R192 on the C-terminus and R50 on the N-terminus with different charged residues also affected ATP sensitivity. Based on these results a structural scheme is proposed, which includes features of other recently published models.
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Registered trials
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.