Cited by 107Pancreatic function and diabetesIon channel regulation and functionIon Transport and Channel Regulation

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ATP-sensitive K + channels and disease: from molecule to malady

Ashcroft, Frances M.·2007·American Journal of Physiology-Endocrinology and Metabolism

DOI 10.1152/ajpendo.00348.2007

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Abstract

This essay is based on a lecture given to the American Physiological Society in honor of Walter B. Cannon, an advocate of homeostasis. It focuses on the role of the ATP-sensitive potassium K(+) (K(ATP)) channel in glucose homeostasis and, in particular, on its role in insulin secretion from pancreatic beta-cells. The beta-cell K(ATP) channel comprises pore-forming Kir6.2 and regulatory SUR1 subunits, and mutations in either type of subunit can result in too little or too much insulin release. Here, I review the latest information on the relationship between K(ATP) channel structure and function, and consider how mutations in the K(ATP) channel genes lead to neonatal diabetes or congenital hyperinsulinism.

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“A similar KATP channel had also just been described by Dan Cook and Nick Hales in inside-out patches excised from pancreatic -cells (10).”
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Activating mutations in the gene encoding the ATP-sensitive potassium-channel subunit Kir6.2 and permanent neonatal diabetes
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Large-Scale Association Studies of Variants in Genes Encoding the Pancreatic β-Cell KATP Channel Subunits Kir6.2 (KCNJ11) and SUR1 (ABCC8) Confirm That the KCNJ11 E23K Variant Is Associated With Type 2 Diabetes
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“The resultant decrease in potassium ion efflux depolarizes the β-cell membrane potential, leading to activation of voltage-gated calcium channels, calcium influx, and calcium-stimulated insulin granule exocytosis (Figure 1B).(21) Graded increases in plasma glucose and subsequent metabolism lead to proportional decreas…”
The KATP Channel and Neonatal Diabetes
Shimomura, K. (2009) · Endocrine Journal · doi:10.1507/endocrj.k08e-160 · Cited by 20
An In-Frame Deletion in Kir6.2 (KCNJ11) Causing Neonatal Diabetes Reveals a Site of Interaction between Kir6.2 and SUR1
Craig, T. J., Shimomura, K., Holl, R. W., Flanagan, S. E., Ellard, S., & Ashcroft, F. M. (2009) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2009-0159 · Cited by 18
Self-citation
Variable phenotypic spectrum of diabetes mellitus in a family carrying a novel KCNJ11 gene mutation
D’Amato, E., Tammaro, P., Craig, T. J., Tosi, A., Giorgetti, R., Lorini, R., & Ashcroft, F. M. (2008) · Diabetic Medicine · doi:10.1111/j.1464-5491.2008.02443.x · Cited by 24
Self-citation
Expression of an activating mutation in the gene encoding the KATP channel subunit Kir6.2 in mouse pancreatic β cells recapitulates neonatal diabetes
Girard, C. A., Wunderlich, F. T., Shimomura, K., Collins, S., Kaizik, S., Proks, P., Abdulkader, F., Clark, A., Ball, V., Zubcevic, L., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci35772 · Cited by 105
Self-citation
‘Resistance is futile?’ – paradoxical inhibitory effects of K ATP channel closure in glucagon‐secreting α‐cells
Zhang, Q., Dou, H., & Rorsman, P. (2020) · The Journal of Physiology · doi:10.1113/jp279775 · Cited by 31
“2A) or high glucose (Zhang et al. 2013; Babinsky et al. 2017).”
The ATP-sensitive K channel is seizure protective and required for effective dietary therapy in a model of mitochondrial encephalomyopathy
Fogle, K. J., Hertzler, J. I., Shon, J. H., & Palladino, M. (2016) · Journal of neurogenetics · doi:10.1080/01677063.2016.1252765 · Cited by 20
“KATP is found in many tissues, including pancreatic b cells where their contribution to insulin release makes them drug targets in diabetes (Ashcroft, 2007; Hibino et al., 2010) and hyperinsulinism (Dunne, Cosgrove, Shepherd, Aynsley-Green, & Lindley, 2004).”
Background
KCNJ11 knockout morula re-engineered by stem cell diploid aggregation
Nelson, T. J., Martinez‐Fernandez, A., & Terzic, A. (2008) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2008.0179 · Cited by 18
“2 subunit of KATP channels (Aguilar-Bryan et al. 1995; Inagaki et al. 1995), are pathogenic in a syndrome that encompasses diabetes, developmental delay and epilepsy (Proks et al. 2004; Hattersley & Ashcroft 2005; Gloyn et al. 2006; Ashcroft 2007).”
BackgroundInfluential
KATP channel mutations in congenital hyperinsulinism: Progress and challenges towards mechanism-based therapies
ElSheikh, A., & Shyng, S. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1161117 · Cited by 18
Channelopathies: Decoding Disease Pathogenesis
Terzic, A., & Pérez-Terzic, C. (2010) · Science Translational Medicine · doi:10.1126/scitranslmed.3001433 · Cited by 18
Interaction between mutations in the slide helix of Kir6.2 associated with neonatal diabetes and neurological symptoms
Männikkö, R., Jefferies, C., Flanagan, S. E., Hattersley, A. T., Ellard, S., & Ashcroft, F. M. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp554 · Cited by 19
“The increase in heterozygous KATP currents recorded in the presence of MgATP is similar to that found for other neonatal diabetes mutations associated with neurological symptoms and greater than for mutations that cause neonatal diabetes alone (3).”
BackgroundResultInfluentialSelf-citation
A conserved tryptophan at the membrane–water interface acts as a gatekeeper for Kir6.2/SUR1 channels and causes neonatal diabetes when mutated
Männikkö, R., Stansfeld, P. J., Ashcroft, A. S., Hattersley, A. T., Sansom, M. S. P., Ellard, S., & Ashcroft, F. M. (2011) · The Journal of Physiology · doi:10.1113/jphysiol.2011.209700 · Cited by 19
Self-citation
Ca2+Channels on the Move
Taylor, C. W., Prole, D. L., & Rahman, T. (2009) · Biochemistry · doi:10.1021/bi901739t · Cited by 39
Modeling K,ATP-Dependent Excitability in Pancreatic Islets
Silva, J. R., Cooper, P., & Nichols, C. G. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2014.09.037 · Cited by 12
The first clinical case of a mutation at residue K185 of Kir6.2 (KCNJ11): a major ATP‐binding residue
Shimomura, K., de Nanclares, G. P., Foutinou, C., Caimari, M., Castaño, L. A., & Ashcroft, F. M. (2009) · Diabetic Medicine · doi:10.1111/j.1464-5491.2009.02901.x · Cited by 17
Self-citation
Real-time imaging of intracellular hydrogen peroxide in pancreatic islets
Neal, A. S., Rountree, A. M., Kernan, K. A., Yserloo, B. V., Zhang, H., Reed, B. J., Osborne, W. R. A., Wang, W., & Sweet, I. R. (2016) · Biochemical Journal · doi:10.1042/bcj20160481 · Cited by 14
“channels has shed light on some causes of impaired insulin secretion [3, 4].”
Background
Enhanced antidiabetic efficacy and safety of compound K⁄β-cyclodextrin inclusion complex in zebrafish
Nam, Y., Lê, H. T., Rodriguez, I., Kim, E. Y., Kim, K., Jeong, S. Y., Woo, S.-H., Lee, Y. R., Castañeda, R., Hong, J., et al. (2016) · Journal of Ginseng Research · doi:10.1016/j.jgr.2016.08.007 · Cited by 14
“Closure of the KATP channels leads to membrane depolarization, the opening of voltagegated Ca2þ channels, and Ca2þ inflow and increase, which result in insulin secretion [32,33].”
Background
A role of the sulfonylurea receptor 1 in endocytic trafficking of ATP-sensitive potassium channels
Bruederle, C. E., Gay, J. W., & Shyng, S. (2011) · Traffic : the International Journal of Intracellular Transport · doi:10.1111/j.1600-0854.2011.01227.x · Cited by 14
Genotype‐phenotype correlation of K ATP channel gene defects causing permanent neonatal diabetes in Indian patients
Gopi, S., Kavitha, B., Kanthimathi, S., Kannan, A., Kumar, R., Joshi, R., Kanodia, S., Arya, A., Pendsey, S., Pendsey, S., et al. (2020) · Pediatric Diabetes · doi:10.1111/pedi.13109 · Cited by 17
Sixty Years of Drug Discovery for Type 2 Diabetes: Where Are We Now?
Clapham, J. C. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9882-1_1 · Cited by 15
Running out of time: the decline of channel activity and nucleotide activation in adenosine triphosphate-sensitive K-channels
Proks, P., Puljung, M. C., Vedovato, N., Sachse, G., Mulvaney, R., & Ashcroft, F. M. (2016) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2015.0426 · Cited by 11
Self-citation
A Novel KCNJ11 Mutation Associated with Transient Neonatal Diabetes
Gole, E., Oikonomou, S., Ellard, S., Franco, E. D., & Karavanaki, K. (2017) · Journal of Clinical Research in Pediatric Endocrinology · doi:10.4274/jcrpe.5166 · Cited by 14
Tetrameric structure of SUR2B revealed by electron microscopy of oriented single particles
Fotinou, C., Aittoniemi, J., de Wet, H., Polidori, A., Pucci, B., Sansom, M. S. P., Vénien‐Bryan, C., & Ashcroft, F. M. (2012) · FEBS Journal · doi:10.1111/febs.12097 · Cited by 11
Self-citation
Memantine has no effect on KATP channels in pancreatic β cells
Imai, R., Misaka, S., Horita, S., Yokota, S., O’hashi, R., Maejima, Y., & Shimomura, K. (2018) · BMC Research Notes · doi:10.1186/s13104-018-3715-9 · Cited by 10
Detection of KATP channels subunits in human term placental explants and evaluation of their implication in human placental lactogen (hPL) and human chorionic gonadotropin (hCG) release
Lybaert, P., Hoofd, C., Guldner, D., Vegh, G., Delporte, C., Meuris, S., & Lebrun, P. (2013) · Placenta · doi:10.1016/j.placenta.2013.03.006 · Cited by 11
A universally conserved residue in the SUR1 subunit of the KATP channel is essential for translating nucleotide binding at SUR1 into channel opening
de Wet, H., Shimomura, K., Aittoniemi, J., Ahmad, N., Lafond, M., Sansom, M. S. P., & Ashcroft, F. M. (2012) · The Journal of Physiology · doi:10.1113/jphysiol.2012.236075 · Cited by 13
Self-citation
Risk loci for type 2 diabetes – Quo vadis?
Weijers, R. N. M. (2009) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm.2009.077 · Cited by 4
Ameliorative Effects of Flavonoids from Platycodon grandiflorus Aerial Parts on Alloxan-Induced Pancreatic Islet Damage in Zebrafish
Nam, Y., Kim, E. B., Kang, J., Kim, J. S., Jeon, Y., Shin, S.-W., Kang, T.-H., & Kwak, J. (2023) · Nutrients · doi:10.3390/nu15071798 · Cited by 9
“When K ATP channels are shut, insulin is secreted, and when they are open, insulin is inhibited [5].”
Background
Mice expressing a human KATP channel mutation have altered channel ATP sensitivity but no cardiac abnormalities
Clark, R. H., Männikkö, R., Stuckey, D., Iberl, M., Clarke, K. J., & Ashcroft, F. M. (2012) · Diabetologia · doi:10.1007/s00125-011-2428-6 · Cited by 10
Self-citation
Accounting for Near-Normal Glucose Sensitivity in Kir6.2[AAA] Transgenic Mice
Tsaneva-Atanasova, K. T., & Sherman, A. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2009.07.060
Pharmacogenomics of sulfonylureas in type 2 diabetes mellitus; a systematic review
Karkhaneh, L., Tabatabaei-Malazy, O., Bandarian, F., Mohseni, S., & Larijani, B. (2021) · Journal of Diabetes and Metabolic Disorders · doi:10.1007/s40200-021-00908-x · Cited by 7
KATP channel dependent heart multiome atlas
Arrell, D. K., Park, S., Yamada, S., Alekseev, A. E., Garmany, A., Jeon, R., Vučković, I., Lindor, J. Z., & Terzic, A. (2022) · Scientific Reports · doi:10.1038/s41598-022-11323-4 · Cited by 6
Mouse models of β-cell KATP channel dysfunction
Brereton, M. F., & Ashcroft, F. M. (2013) · Drug Discovery Today Disease Models · doi:10.1016/j.ddmod.2013.02.001 · Cited by 5
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Methods for Characterizing Disease-Associated ATP-Sensitive Potassium Channel Mutations
Kandasamy, B., & Shyng, S. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7362-0_8 · Cited by 7
Eugenosedin-A improves obesity-related hyperglycemia by regulating ATP-sensitive K+ channels and insulin secretion in pancreatic β cells
Lin, R., Yen, Y.-K., Lee, C., Hsieh, S., Chang, Y., Juan, Y., Long, C., Shen, K., & Wu, B. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.112447 · Cited by 4
An Egyptian case of congenital hyperinsulinism of infancy due to a novel mutation in KCNJ11 encoding Kir6.2 and response to octreotide
Sherif, E., Abdelmaksoud, A., Elbarbary, N., & Njølstad, P. (2013) · Acta Diabetologica · doi:10.1007/s00592-010-0217-1 · Cited by 4
“Insulin hypersecretion that characterizes CHI results from permanent depolarization of the b-cell membrane and thereby continuous Ca2? influx and insulin secretion [23].”
Background
Ion Channels and Regulation of Insulin Secretion in Beta-Cells
Oluwamodupe, C., & Babalola, O. O. (2024) · Current Molecular Biology Reports · doi:10.1007/s40610-024-00162-z · Cited by 5
“It has been shown that pancreatic beta cells can have intra-cellular chloride concentrations greater than 35 mm [38, 47].”
Phosphoinositol metabolism affects AMP kinase-dependent K-ATP currents in rat substantia nigra dopamine neurons
Shen, K., Munhall, A. C., & Johnson, S. (2018) · Brain Research · doi:10.1016/j.brainres.2018.10.027 · Cited by 3
“They are probably best characterized in pancreatic beta-cells where closure of the channel by ATP causes membrane depolarization and calcium influx and thereby triggering insulin release (Ashcroft, 2007).”
Background
Hyperinsulinemic Hypoglycemias in Infancy and Childhood - Diagnostic Therapeutic Algorithm with Contribution of Two Cases
Kaleva, N., Ivanov, I., Panova, M., Shabanova, T. D., & Delgyanska, D. S. (2010) · Folia Medica · doi:10.2478/v10153-010-0008-z · Cited by 3
The Association Between genetic variations of KCNj11 gene and type 2 diabetes mellitus in a sample of Iraqi population.
Hussieny, B. A. A., & Alsahlawi, M. M. R. (2023) · Al-Kufa University Journal for Biology · doi:10.36320/ajb/v13.i2.11759 · Cited by 1
Anti-diabetic drug binding site in KATP channels revealed by Cryo-EM
Martin, G. M., Kandasamy, B., DiMaio, F., Yoshioka, C., & Shyng, S. (2017) · bioRxiv · doi:10.1101/172908 · Cited by 2
Inherited pediatric metabolic epilepsies
Pearl, P. L., & Yu, Y. (2013) · Expert Opinion on Orphan Drugs · doi:10.1517/21678707.2013.758580 · Cited by 2
“These mutations “lock in” the KATP channel in an open state, even under hyperglycemic conditions [29,30].”
Background
Protein Kinases and Pancreatic Islet Function
Xavier, G. D. S. (2012) · InTech eBooks · doi:10.5772/37282 · Cited by 1
Advances in Cardiac ATP-Sensitive K+ Channelopathies From Molecules to Populations
Terzic, A., Alekseev, A., Yamada, S., Reyes, S., & Olson, T. M. (2011) · Circulation: Arrhythmia and Electrophysiology · doi:10.1161/circep.110.957662 · Cited by 2
Phenotype of a transient neonatal diabetes point mutation (SUR1-R1183W) in mice
Sachse, G., Haythorne, E., Proks, P., Stewart, M. E., Cater, H. L., Ellard, S., Davies, B., & Ashcroft, F. M. (2020) · Wellcome Open Research · doi:10.12688/wellcomeopenres.15529.2 · Cited by 2
“ATP-sensitive potassium (K ATP ) channels play a pivotal role in coupling blood glucose levels to insulin secretion (Ashcroft, 2007).”
Self-citation
Diabetes mellitus beim Frühgeborenen: Erstmalige Behandlung mit Sulfonylharnstoff
Holl, R. (2009) · Klinische Pädiatrie · doi:10.1055/s-0029-1192017 · Cited by 1
Targeted analysis of whole exome sequencing in Thai patients with neonatal diabetes
Plengvidhya, N., Tangjarusritaratorn, T., Teerawattanapong, N., Narkdontri, T., Innang, S., Songlilitchuwong, S., Suthon, S., & Tangjittipokin, W. (2026) · Human Genetics · doi:10.1007/s00439-025-02815-0
“These two genes are the most frequent causes of both transient and permanent NDM. Variants in KCNJ11 or ABCC8 impair the KATP chan - nel’s sensitivity to ATP, causing persistent channel opening, membrane hyperpolarization, and reduced insulin secretion (Ashcroft 2007).”
Benguet Kankanaey self-representations in local films in Benguet, Philippines
Dalocdoc, P. J. (2025) · International journal of humanities, literature & arts · doi:10.21744/ijhla.v8n1.2367
“Coined by Richard Terdiman, it characterizes the “theory and practice of symbolic resistance" (Ashcroft, 2007).”
Integrative Study of the Structural and Dynamical Properties of a KirBac3.1 Mutant: Functional Implication of a Highly Conserved Tryptophan in the Transmembrane Domain
Fagnen, C., Bannwarth, L., Oubella, I., Zuniga, D., Haouz, A., Forest, É., Scala, R., Bendahhou, S., Zorzi, R. D., Pérahia, D., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms23010335
Maturity Onset Diabetes of the Young (MODY): Eine monogene Form der pankreatischen β-Zell-Dysfunktion
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The right stuff: beta-cell channels, cycles, and sensors.
Halban, P. (2008) · American Journal of Physiology. Endocrinology and Metabolism · doi:10.1152/ajpendo.90692.2008
Frances Ashcroft: 2007 Walter B. Cannon Physiology in Perspective Lecture.
Benos, D. (2007) · American Journal of Physiology. Endocrinology and Metabolism · doi:10.1152/ajpendo.00530.2007
“This is an example of translational research at its finest! This body of work, summarized in the accompanying article (1), demonstrates unequivocally how a full understanding of the molecular basis of ion channel dysfunction can lead to better disease management.”
Background
Research Progress on the Relationship between KATP Channels and Migraine
阳思绮, 欧. (2026) · Advances in Clinical Medicine · doi:10.12677/acm.2026.1682811
Glucose acts as a ligand for glucokinase to trigger postprandial secretion of GLP-1
Li, C., Li, M., Yang, H.-Y., Tian, X., Zhang, C., Zhao, L., Wu, J., Zhang, C., Liu, S., Yang, X., et al. (2026) · Vita · doi:10.15302/vita.2026.07.0059 · Cited by 2
Infant with diabetes – a diagnostic challenge for paediatricians
Brandt-Varma, A., & Myśliwiec, M. (2021) · Pediatria Polska · doi:10.5114/polp.2020.103508
“It is known that diabetes caused by mutations in the gene KCJN11 is sensitive to sulfonylurea treatment [4, 11].”
Background

Authors: Ashcroft, F. M.
Affiliations: University of Oxford (GB)
Corresponding author: Ashcroft, Frances M.
ORCID: Ashcroft, Frances M.
Venue: American Journal of Physiology-Endocrinology and Metabolism
Publisher: American Physiological Society
Published: 2007-10
Volume: 293
Issue: 4
Pages: E880-E889
ISSN: 0193-1849 (ISSN-L)
1522-1555
DOI: 10.1152/ajpendo.00348.2007
OpenAlex: W2134991186
Cited by: 107
References: 0
Citations by year: 2026: 3 · 2024: 1 · 2023: 3 · 2022: 1 · 2021: 6 · 2020: 7 · 2019: 1 · 2018: 2 · 2017: 8 · 2016: 10 · 2015: 1 · 2014: 6 · 2013: 10 · 2012: 6
FWCI: 12.29
Type: journal article
Language: en
Open access: closed
Locations: American Journal of Physiology-Endocrinology and Metabolism (publishedVersion)
PubMed (publishedVersion)
Funders: Wellcome Trust
Diabetes UK
Topics: Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Pancreatic function and diabetes
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion Transport and Channel Regulation
Keywords: ATP-sensitive potassium channels, Kir6.2, SUR1, pancreatic beta cells, insulin secretion, glucose homeostasis, neonatal diabetes, congenital hyperinsulinism, ion channel mutations, channel structure and function
MeSH terms: Kcnj11 Channel, Adenosine Triphosphate, Animals, Diabetes Mellitus, Glucose, Homeostasis, Humans, Models, Biological, Models, Molecular, Mutation, Potassium Channels, Potassium Channels, Inwardly Rectifying, Channelopathies

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ATP-sensitive K + channels and disease: from molecule to malady

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