| pubmed-article:15590641 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15590641 | lifeskim:mentions | umls-concept:C0007447 | lld:lifeskim |
| pubmed-article:15590641 | lifeskim:mentions | umls-concept:C0312418 | lld:lifeskim |
| pubmed-article:15590641 | lifeskim:mentions | umls-concept:C1425223 | lld:lifeskim |
| pubmed-article:15590641 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:15590641 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:15590641 | lifeskim:mentions | umls-concept:C0439799 | lld:lifeskim |
| pubmed-article:15590641 | lifeskim:mentions | umls-concept:C0036667 | lld:lifeskim |
| pubmed-article:15590641 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:15590641 | pubmed:dateCreated | 2005-2-21 | lld:pubmed |
| pubmed-article:15590641 | pubmed:abstractText | TRPM4, a Ca(2+)-activated cation channel of the transient receptor potential superfamily, undergoes a fast desensitization to Ca(2+). The mechanisms underlying the alterations in Ca(2+) sensitivity are unknown. Here we show that cytoplasmic ATP reversed Ca(2+) sensitivity after desensitization, whereas mutations to putative ATP binding sites resulted in faster and more complete desensitization. Phorbol ester-induced activation of protein kinase C (PKC) increased the Ca(2+) sensitivity of wild-type TRPM4 but not of two mutants mutated at putative PKC phosphorylation sites. Overexpression of a calmodulin mutant unable to bind Ca(2+) dramatically reduced TRPM4 activation. We identified five Ca(2+)-calmodulin binding sites in TRPM4 and showed that deletion of any of the three C-terminal sites strongly impaired current activation by reducing Ca(2+) sensitivity and shifting the voltage dependence of activation to very positive potentials. Thus, the Ca(2+) sensitivity of TRPM4 is regulated by ATP, PKC-dependent phosphorylation, and calmodulin binding at the C terminus. | lld:pubmed |
| pubmed-article:15590641 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15590641 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15590641 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15590641 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15590641 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15590641 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15590641 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15590641 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15590641 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15590641 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15590641 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15590641 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:15590641 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:15590641 | pubmed:author | pubmed-author:NiliusBerndB | lld:pubmed |
| pubmed-article:15590641 | pubmed:author | pubmed-author:ZhuMichael... | lld:pubmed |
| pubmed-article:15590641 | pubmed:author | pubmed-author:PrenenJeanJ | lld:pubmed |
| pubmed-article:15590641 | pubmed:author | pubmed-author:VoetsThomasT | lld:pubmed |
| pubmed-article:15590641 | pubmed:author | pubmed-author:OwsianikGrzeg... | lld:pubmed |
| pubmed-article:15590641 | pubmed:author | pubmed-author:TangJisenJ | lld:pubmed |
| pubmed-article:15590641 | pubmed:author | pubmed-author:JanssensAnnel... | lld:pubmed |
| pubmed-article:15590641 | pubmed:author | pubmed-author:WangChunboC | lld:pubmed |
| pubmed-article:15590641 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15590641 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:15590641 | pubmed:volume | 280 | lld:pubmed |
| pubmed-article:15590641 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15590641 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15590641 | pubmed:pagination | 6423-33 | lld:pubmed |
| pubmed-article:15590641 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:15590641 | pubmed:meshHeading | pubmed-meshheading:15590641... | lld:pubmed |
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| pubmed-article:15590641 | pubmed:meshHeading | pubmed-meshheading:15590641... | lld:pubmed |
| pubmed-article:15590641 | pubmed:meshHeading | pubmed-meshheading:15590641... | lld:pubmed |
| pubmed-article:15590641 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15590641 | pubmed:articleTitle | Regulation of the Ca2+ sensitivity of the nonselective cation channel TRPM4. | lld:pubmed |
| pubmed-article:15590641 | pubmed:affiliation | Department of Physiology, Campus Gasthuisberg, KU Leuven, B-3000 Leuven, Belgium. bernd.nilius@med.kuleuven.ac.be | lld:pubmed |
| pubmed-article:15590641 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15590641 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15590641 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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