Source:http://linkedlifedata.com/resource/pubmed/id/14684870
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
37
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| pubmed:dateCreated |
2003-12-19
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| pubmed:databankReference | |
| pubmed:abstractText |
Neuronal stressors such as hypoxia and firing of action potentials at very high frequencies cause intracellular Na+ to rise and ATP to be consumed faster than it can be regenerated. We report the cloning of a gene encoding a K+ channel, Slick, and demonstrate that functionally it is a hybrid between two classes of K+ channels, Na+-activated (KNa) and ATP-sensitive (KATP) K+ channels. The Slick channel is activated by intracellular Na+ and Cl- and is inhibited by intracellular ATP. Slick is widely expressed in the CNS and is detected in heart. We identify a consensus ATP binding site near the C terminus of the channel that is required for ATP and its nonhydrolyzable analogs to reduce open probability. The convergence of Na+, Cl-, and ATP sensitivity in one channel may endow Slick with the ability to integrate multiple indicators of the metabolic state of a cell and to adjust electrical activity appropriately.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
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| pubmed:month |
Dec
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| pubmed:issn |
1529-2401
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| pubmed:author | |
| pubmed:issnType |
Electronic
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| pubmed:day |
17
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| pubmed:volume |
23
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
11681-91
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:14684870-Adenosine Triphosphate,
pubmed-meshheading:14684870-Amino Acid Sequence,
pubmed-meshheading:14684870-Animals,
pubmed-meshheading:14684870-CHO Cells,
pubmed-meshheading:14684870-Cells, Cultured,
pubmed-meshheading:14684870-Chlorides,
pubmed-meshheading:14684870-Cloning, Molecular,
pubmed-meshheading:14684870-Cricetinae,
pubmed-meshheading:14684870-Electric Conductivity,
pubmed-meshheading:14684870-Humans,
pubmed-meshheading:14684870-Ion Channel Gating,
pubmed-meshheading:14684870-Kinetics,
pubmed-meshheading:14684870-Molecular Sequence Data,
pubmed-meshheading:14684870-Potassium Channels,
pubmed-meshheading:14684870-Rats,
pubmed-meshheading:14684870-Sequence Alignment,
pubmed-meshheading:14684870-Sodium,
pubmed-meshheading:14684870-Tissue Distribution,
pubmed-meshheading:14684870-Xenopus
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| pubmed:year |
2003
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| pubmed:articleTitle |
Slick (Slo2.1), a rapidly-gating sodium-activated potassium channel inhibited by ATP.
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| pubmed:affiliation |
Department of Pharmacology, Yale University School of Medicine, New Haven, Connecticut 06520, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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