| pubmed-article:14657398 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14657398 | lifeskim:mentions | umls-concept:C0039336 | lld:lifeskim |
| pubmed-article:14657398 | lifeskim:mentions | umls-concept:C0031676 | lld:lifeskim |
| pubmed-article:14657398 | lifeskim:mentions | umls-concept:C0178719 | lld:lifeskim |
| pubmed-article:14657398 | lifeskim:mentions | umls-concept:C0022009 | lld:lifeskim |
| pubmed-article:14657398 | lifeskim:mentions | umls-concept:C0070798 | lld:lifeskim |
| pubmed-article:14657398 | lifeskim:mentions | umls-concept:C1336676 | lld:lifeskim |
| pubmed-article:14657398 | lifeskim:mentions | umls-concept:C1160185 | lld:lifeskim |
| pubmed-article:14657398 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:14657398 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:14657398 | pubmed:issue | 25 | lld:pubmed |
| pubmed-article:14657398 | pubmed:dateCreated | 2003-12-10 | lld:pubmed |
| pubmed-article:14657398 | pubmed:abstractText | The transduction of taste is a fundamental process that allows animals to discriminate nutritious from noxious substances. Three taste modalities, bitter, sweet, and amino acid, are mediated by G protein-coupled receptors that signal through a common transduction cascade: activation of phospholipase C beta2, leading to a breakdown of phosphatidylinositol-4,5-bisphosphate (PIP2) into diacylglycerol and inositol 1,4,5-trisphosphate, which causes release of Ca2+ from intracellular stores. The ion channel, TRPM5, is an essential component of this cascade; however, the mechanism by which it is activated is not known. Here we show that heterologously expressed TRPM5 forms a cation channel that is directly activated by micromolar concentrations of intracellular Ca2+ (K1/2 = 21 microM). Sustained exposure to Ca2+ desensitizes TRPM5 channels, but PIP2 reverses desensitization, partially restoring channel activity. Whole-cell TRPM5 currents can be activated by intracellular Ca2+ and show strong outward rectification because of voltage-sensitive gating of the channels. TRPM5 channels are nonselective among monovalent cations and not detectably permeable to divalent cations. We propose that the regulation of TRPM5 by Ca2+ mediates sensory activation in the taste system. | lld:pubmed |
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| pubmed-article:14657398 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14657398 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14657398 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:14657398 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14657398 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:14657398 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:14657398 | pubmed:author | pubmed-author:LumF GFG | lld:pubmed |
| pubmed-article:14657398 | pubmed:author | pubmed-author:LimanEmily... | lld:pubmed |
| pubmed-article:14657398 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14657398 | pubmed:day | 9 | lld:pubmed |
| pubmed-article:14657398 | pubmed:volume | 100 | lld:pubmed |
| pubmed-article:14657398 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14657398 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14657398 | pubmed:pagination | 15160-5 | lld:pubmed |
| pubmed-article:14657398 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:14657398 | pubmed:meshHeading | pubmed-meshheading:14657398... | lld:pubmed |
| pubmed-article:14657398 | pubmed:meshHeading | pubmed-meshheading:14657398... | lld:pubmed |
| pubmed-article:14657398 | pubmed:meshHeading | pubmed-meshheading:14657398... | lld:pubmed |
| pubmed-article:14657398 | pubmed:meshHeading | pubmed-meshheading:14657398... | lld:pubmed |
| pubmed-article:14657398 | pubmed:meshHeading | pubmed-meshheading:14657398... | lld:pubmed |
| pubmed-article:14657398 | pubmed:meshHeading | pubmed-meshheading:14657398... | lld:pubmed |
