ArticleJournal of proteome research2008
Interaction of asymmetric ABCC9-encoded nucleotide binding domains determines KATP channel SUR2A catalytic activity.
Article in Journal of proteome research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- ABCC9 knockdown attenuates isoproterenol‑induced myocardial hypertrophy by inhibiting the PI3K/AKT signaling pathway.Molecular medicine reports · 2026Article
- KScientific reports · 2022Article
- Covalent crosslinking of graphene oxide and carbon nanotube into hydrogels enhances nerve cell responses.Journal of materials chemistry. B · 2016Article
- ABCC9/SUR2 in the brain: Implications for hippocampal sclerosis of aging and a potential therapeutic target.Ageing research reviews · 2015Review
- Human acetyl-CoA carboxylase 2 expressed in silkworm Bombyx mori exhibits posttranslational biotinylation and phosphorylation.Applied microbiology and biotechnology · 2014Article
- Characterization of the human NEK7 interactome suggests catalytic and regulatory properties distinct from those of NEK6.Journal of proteome research · 2014Article
- ABCC9 is a novel Brugada and early repolarization syndrome susceptibility gene.International journal of cardiology · 2014Article
- Spot14/Mig12 heterocomplex sequesters polymerization and restrains catalytic function of human acetyl-CoA carboxylase 2.Journal of molecular recognition : JMR · 2013Article
- Advances in cardiac ATP-sensitive K+ channelopathies from molecules to populations.Circulation. Arrhythmia and electrophysiology · 2011Article
- K(ATP) channels process nucleotide signals in muscle thermogenic response.Critical reviews in biochemistry and molecular biology · 2010Article
- Human K(ATP) channelopathies: diseases of metabolic homeostasis.Pflugers Archiv : European journal of physiology · 2010Review
- The ATPase activities of sulfonylurea receptor 2A and sulfonylurea receptor 2B are influenced by the C-terminal 42 amino acids.The FEBS journal · 2010Article
- Quaternary structure of KATP channel SUR2A nucleotide binding domains resolved by synchrotron radiation X-ray scattering.Journal of structural biology · 2010Article
- KATP channel Kir6.2 E23K variant overrepresented in human heart failure is associated with impaired exercise stress response.Human genetics · 2009Article
- Targeted disruption of K(ATP) channels aggravates cardiac toxicity in cocaine abuse.Clinical and translational science · 2009Article
- ATP-sensitive K+ channel knockout induces cardiac proteome remodeling predictive of heart disease susceptibility.Journal of proteome research · 2009Article
- Proteomic profiling of KATP channel-deficient hypertensive heart maps risk for maladaptive cardiomyopathic outcome.Proteomics · 2009Article
- KCNJ11 knockout morula re-engineered by stem cell diploid aggregation.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2009Article
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5 authors.
Funding
Abstract
Nucleotide binding domains (NBDs) secure ATP-binding cassette (ABC) transporter function. Distinct from traditional ABC transporters, ABCC9-encoded sulfonylurea receptors (SUR2A) form, with Kir6.2 potassium channels, ATP-sensitive K+ (K ATP) channel complexes. SUR2A contains ATPase activity harbored within NBD2 and, to a lesser degree, NBD1, with catalytically driven conformations exerting determinate linkage on the Kir6.2 channel pore. While homodomain interactions typify NBDs of conventional ABC transporters, heterodomain NBD interactions and their functional consequence have not been resolved for the atypical SUR2A protein. Here, nanoscale protein topography mapped assembly of monodisperse purified recombinant SUR2A NBD1/NBD2 domains, precharacterized by dynamic light scattering. Heterodomain interaction produced conformational rearrangements inferred by secondary structural change in circular dichroism, and validated by atomic force and transmission electron microscopy. Physical engagement of NBD1 with NBD2 translated into enhanced intrinsic ATPase activity. Molecular modeling delineated a complemental asymmetry of NBD1/NBD2 ATP-binding sites. Mutation in the predicted catalytic base residue, D834E of NBD1, altered NBD1 ATPase activity disrupting potentiation of catalytic behavior in the NBD1/NBD2 interactome. Thus, NBD1/NBD2 assembly, resolved by a panel of proteomic approaches, provides a molecular substrate that determines the optimal catalytic activity in SUR2A, establishing a paradigm for the structure-function relationship within the K ATP channel complex.
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