The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
K ATP channel inhibition by ATP requires distinct functional domains of the cytoplasmic C terminus of the pore-forming subunit
Open accessAbstract
ATP-sensitive potassium (“K ATP ”) channels are rapidly inhibited by intracellular ATP. This inhibition plays a crucial role in the coupling of electrical activity to energy metabolism in a variety of cells. The K ATP channel is formed from four each of a sulfonylurea receptor (SUR) regulatory subunit and an inwardly rectifying potassium (K ir 6.2) pore-forming subunit. We used systematic chimeric and point mutagenesis, combined with patch-clamp recording, to investigate the molecular basis of ATP-dependent inhibition gating of mouse pancreatic β cell K ATP channels expressed in Xenopus oocytes. We identified distinct functional domains of the presumed cytoplasmic C-terminal segment of the K ir 6.2 subunit that play an important role in this inhibition. Our results suggest that one domain is associated with inhibitory ATP binding and another with gate closure.
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Cites
Intracellular ATP directly blocks K+ channels in pancreatic B-cells
Cook, D. L., & Hales, N. (1984) · Nature · doi:10.1038/311271a0 · Cited by 1,208
Glucose induces closure of single potassium channels in isolated rat pancreatic β-cells
Ashcroft, F. M., Harrison, D. E., & Ashcroft, S. J. H. (1984) · Nature · doi:10.1038/312446a0 · Cited by 1,113
Association and Stoichiometry of KATP Channel Subunits
Clement, J. P., Kunjilwar, K., Gonzalez, G., Schwanstecher, M., Panten, U., Aguilar-Bryan, L., & Bryan, J. (1997) · Neuron · doi:10.1016/s0896-6273(00)80321-9 · Cited by 692
Cited by
Inwardly Rectifying Potassium Channels: Their Structure, Function, and Physiological Roles
Hibino, H., Inanobe, A., Furutani, K., Murakami, S., Findlay, I., & Kurachi, Y. (2010) · Physiological Reviews · doi:10.1152/physrev.00021.2009 · Cited by 1,539
KATP channels as molecular sensors of cellular metabolism
Nichols, C. G. (2006) · Nature · doi:10.1038/nature04711 · Cited by 851
Hyperinsulinism in Infancy: From Basic Science to Clinical Disease
DUNNE, M. J., COSGROVE, K. E., SHEPHERD, R. M., AYNSLEY-GREEN, A., & LINDLEY, K. J. (2004) · Physiological Reviews · doi:10.1152/physrev.00022.2003 · Cited by 294
Targeted Overactivity of β Cell KATP Channels Induces Profound Neonatal Diabetes
Koster, J. C., Marshall, B. A., Ensor, N., Corbett, J. A., & Nichols, C. G. (2000) · Cell · doi:10.1016/s0092-8674(00)80701-1 · Cited by 287
Pharmacological Agents That Directly Modulate Insulin Secretion
Doyle, M. E., & Egan, J. M. (2003) · Pharmacological Reviews · doi:10.1124/pr.55.1.7 · Cited by 256
Metadata
- Authors
- Drain, P., Li, L., & Wang, J.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1998-11-10
- Volume
- 95
- Issue
- 23
- Pages
- 13953-13958
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2126317206
- Cited by
- 193
- References
- 3
- FWCI
- 5.18
- Type
- journal article
- Language
- en
- Open access
- green
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- Drain, P., Li, L., & Wang, J. (1998). K ATP channel inhibition by ATP requires distinct functional domains of the cytoplasmic C terminus of the pore-forming subunit. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.95.23.13953
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