pubmed-article:10082974 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10082974 | lifeskim:mentions | umls-concept:C1709130 | lld:lifeskim |
pubmed-article:10082974 | lifeskim:mentions | umls-concept:C0032821 | lld:lifeskim |
pubmed-article:10082974 | lifeskim:mentions | umls-concept:C0178702 | lld:lifeskim |
pubmed-article:10082974 | lifeskim:mentions | umls-concept:C0812204 | lld:lifeskim |
pubmed-article:10082974 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
pubmed-article:10082974 | lifeskim:mentions | umls-concept:C0521116 | lld:lifeskim |
pubmed-article:10082974 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:10082974 | pubmed:dateCreated | 1999-4-27 | lld:pubmed |
pubmed-article:10082974 | pubmed:abstractText | NM23 (NDP kinase) modulates the gating of muscarinic K+ channels by agonists through a mechanism distinct from GTP regeneration. To better define the function of NM23 in this pathway and to identify sites in NM23 that are important for its role in muscarinic K+ channel function, we utilized MDA-MB-435 human breast carcinoma cells that express low levels of NM23-H1. M2 muscarinic receptors and GIRK1/GIRK4 channel subunits were co-expressed in cells stably transfected with vector only (control), wild-type NM23-H1, or several NM23-H1 mutants. Lysates from all cell lines tested exhibit comparable nucleoside diphosphate (NDP) kinase activity. Whole cell patch clamp recordings revealed a substantial reduction of the acute desensitization of muscarinic K+ currents in cells overexpressing NM23-H1. The mutants NM23-H1P96S and NM23-H1S44A resembled wild-type NM23-H1 in their ability to reduce desensitization. In contrast, mutants NM23-H1S120G and NM23-H1S120A completely abolished the effect of NM23-H1 on desensitization of muscarinic K+ currents. Furthermore, NM23-H1S120G potentiated acute desensitization, indicating that this mutant retains the ability to interact with the muscarinic pathway, but has properties antithetical to those of the wild-type protein. We conclude that NM23 acts as a suppressor of the processes leading to the desensitization of muscarinic K+ currents, and that Ser-120 is essential for its actions. | lld:pubmed |
pubmed-article:10082974 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10082974 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10082974 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10082974 | pubmed:language | eng | lld:pubmed |
pubmed-article:10082974 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10082974 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10082974 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10082974 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10082974 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10082974 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10082974 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10082974 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10082974 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10082974 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10082974 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10082974 | pubmed:month | Mar | lld:pubmed |
pubmed-article:10082974 | pubmed:issn | 0006-3002 | lld:pubmed |
pubmed-article:10082974 | pubmed:author | pubmed-author:DoyleM BMB | lld:pubmed |
pubmed-article:10082974 | pubmed:author | pubmed-author:SteegP SPS | lld:pubmed |
pubmed-article:10082974 | pubmed:author | pubmed-author:OteroA SAS | lld:pubmed |
pubmed-article:10082974 | pubmed:author | pubmed-author:HartsoughM... | lld:pubmed |
pubmed-article:10082974 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10082974 | pubmed:day | 8 | lld:pubmed |
pubmed-article:10082974 | pubmed:volume | 1449 | lld:pubmed |
pubmed-article:10082974 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10082974 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10082974 | pubmed:pagination | 157-68 | lld:pubmed |
pubmed-article:10082974 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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pubmed-article:10082974 | pubmed:year | 1999 | lld:pubmed |
pubmed-article:10082974 | pubmed:articleTitle | Wild-type NM23-H1, but not its S120 mutants, suppresses desensitization of muscarinic potassium current. | lld:pubmed |
pubmed-article:10082974 | pubmed:affiliation | Department of Molecular Physiology and Biological Physics, University of Virginia Medical School, Charlottesville, VA 22906, USA. ado2t@virginia.edu | lld:pubmed |
pubmed-article:10082974 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10082974 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10082974 | lld:pubmed |