| pubmed-article:10545132 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10545132 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
| pubmed-article:10545132 | lifeskim:mentions | umls-concept:C0439799 | lld:lifeskim |
| pubmed-article:10545132 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:10545132 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:10545132 | pubmed:dateCreated | 2000-2-1 | lld:pubmed |
| pubmed-article:10545132 | pubmed:abstractText | 1. G protein-gated inwardly rectifying K+ (GIRK) channels are activated independently by Gbetagamma and internal Na+ via mechanisms requiring phosphatidylinositol phosphates. An aspartate (Asp) at position 226 in GIRK2 is crucial for Na+-dependent activation of GIRK1-GIRK2 heteromeric channels. We expressed wild-type and mutant GIRK1-GIRK2 channels in Xenopus oocytes and tested the effects of Na+ and neutralizing Asp226 on the functional interactions of the channels with phosphatidylinositol 4, 5-bisphosphate (PIP2). 2. The rate of inhibition of GIRK1-GIRK2 currents by application of anti-PIP2 antibody to inside-out membrane patches was slowed > 2-fold by the D226N mutation in GIRK2 and by increasing internal [Na+]. The reverse mutation in GIRK1 (N217D) increased the rate of inhibition. 3. The dose-response relationship for activation by purified PIP2 was shifted to lower concentrations in the presence of 20 mM Na+. 4. Three synthetic isoforms of PIP2, PI(4,5)P2, PI(3,4)P2 and PI(3,5)P2, activated GIRK channels with similar potencies. 5. We conclude that Na+ directly interacts with Asp226 of GIRK2 to reduce the negative electrostatic potential and promote the functional interaction of the channels with PIP2. | lld:pubmed |
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| pubmed-article:10545132 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:10545132 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10545132 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10545132 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:10545132 | pubmed:issn | 0022-3751 | lld:pubmed |
| pubmed-article:10545132 | pubmed:author | pubmed-author:Murrell-Lagna... | lld:pubmed |
| pubmed-article:10545132 | pubmed:author | pubmed-author:IkaII | lld:pubmed |
| pubmed-article:10545132 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10545132 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:10545132 | pubmed:volume | 520 Pt 3 | lld:pubmed |
| pubmed-article:10545132 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10545132 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10545132 | pubmed:pagination | 645-51 | lld:pubmed |
| pubmed-article:10545132 | pubmed:dateRevised | 2010-8-25 | lld:pubmed |
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| pubmed-article:10545132 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10545132 | pubmed:articleTitle | Molecular mechanism for sodium-dependent activation of G protein-gated K+ channels. | lld:pubmed |
| pubmed-article:10545132 | pubmed:affiliation | Department of Pharmacology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QJ, UK. | lld:pubmed |
| pubmed-article:10545132 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10545132 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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