ArticleThe Journal of biological chemistry2005
The glycolytic enzymes, glyceraldehyde-3-phosphate dehydrogenase, triose-phosphate isomerase, and pyruvate kinase are components of the K(ATP) channel macromolecular complex and regulate its function.
Article in The Journal of biological chemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.
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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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Who cites it
66 citing papers in PubMed, 130 citations in OpenAlex.
- The Remarkable Role of Triosephosphate Isomerase in Diabetes Pathophysiology.International journal of molecular sciences · 2025Review
- Modulation of pain by ketones: a mini-review.American journal of physiology. Cell physiology · 2025Review
- Glucose and glycogen affects CaPhysiological reports · 2024Article
- Review
- Electro-metabolic signaling.The Journal of general physiology · 2024Article
- Exercise and fatigue: integrating the role of KEuropean journal of applied physiology · 2023Review
- Article
- Proteomic Profiling of Mouse Brain Pyruvate Kinase Binding Proteins: A Hint for Moonlighting Functions of PKM1?International journal of molecular sciences · 2023Article
- Metabolic cycles and signals for insulin secretion.Cell metabolism · 2022Review
- KScientific reports · 2022Article
- Possible role of ketone bodies in the generation of burst suppression electroencephalographic pattern.Frontiers in neuroscience · 2022Article
- Lactate is an energy substrate for rodent cortical neurons and enhances their firing activity.eLife · 2021Article
- Comprehensive Proteomics Analysis of In Vitro Canine Oviductal Cell-Derived Extracellular Vesicles.Animals : an open access journal from MDPI · 2021Article
- Lactate activation of α-cell KMolecular metabolism · 2020Article
- Pyruvate Kinase Controls Signal Strength in the Insulin Secretory Pathway.Cell metabolism · 2020Article
- Mitochondrial Proton Leak Regulated by Cyclophilin D Elevates Insulin Secretion in Islets at Nonstimulatory Glucose Levels.Diabetes · 2020Article
- Another Consequence of the Warburg Effect? Metabolic Regulation of NaFrontiers in oncology · 2020Review
- Potassium and Sodium Channels and the Warburg Effect: Biophysical Regulation of Cancer Metabolism.Bioelectricity · 2019Article
- Ketogenic and anaplerotic dietary modifications ameliorate seizure activity in Drosophila models of mitochondrial encephalomyopathy and glycolytic enzymopathy.Molecular genetics and metabolism · 2019Article
- Contractile function of the excised hagfish heart during anoxia exposure.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2019Article
6 more citing papers are in PubMed but not listed here.
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Authors and funding
11 authors at 1 institution in 1 country.
Funding
Abstract
The regulation of ATP-sensitive potassium (K(ATP)) channel activity is complex and a multitude of factors determine their open probability. Physiologically and pathophysiologically, the most important of these are intracellular nucleotides, with a long-recognized role for glycolytically derived ATP in regulating channel activity. To identify novel regulatory subunits of the K(ATP) channel complex, we performed a two-hybrid protein-protein interaction screen, using as bait the mouse Kir6.2 C terminus. Screening a rat heart cDNA library, we identified two potential interacting proteins to be the glycolytic enzymes, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and triose-phosphate isomerase. The veracity of interaction was verified by co-immunoprecipitation techniques in transfected mammalian cells. We additionally demonstrated that pyruvate kinase also interacts with Kir6.2 subunits. The physiological relevance of these interactions is illustrated by the demonstration that native Kir6.2 protein similarly interact with GAPDH and pyruvate kinase in rat heart membrane fractions and that Kir6.2 protein co-localize with these glycolytic enzymes in rat ventricular myocytes. The functional relevance of our findings is demonstrated by the ability of GAPDH or pyruvate kinase substrates to directly block the K(ATP) channel under patch clamp recording conditions. Taken together, our data provide direct evidence for the concept that key enzymes involved in glycolytic ATP production are part of a multisubunit K(ATP) channel protein complex. Our data are consistent with the concept that the activity of these enzymes (possibly by ATP formation in the immediate intracellular microenvironment of this macromolecular K(ATP) channel complex) causes channel closure.
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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.