| pubmed-article:21653882 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21653882 | lifeskim:mentions | umls-concept:C0006675 | lld:lifeskim |
| pubmed-article:21653882 | lifeskim:mentions | umls-concept:C0035647 | lld:lifeskim |
| pubmed-article:21653882 | lifeskim:mentions | umls-concept:C0596981 | lld:lifeskim |
| pubmed-article:21653882 | lifeskim:mentions | umls-concept:C0054450 | lld:lifeskim |
| pubmed-article:21653882 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:21653882 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:21653882 | lifeskim:mentions | umls-concept:C1421170 | lld:lifeskim |
| pubmed-article:21653882 | lifeskim:mentions | umls-concept:C1425400 | lld:lifeskim |
| pubmed-article:21653882 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:21653882 | lifeskim:mentions | umls-concept:C1948027 | lld:lifeskim |
| pubmed-article:21653882 | lifeskim:mentions | umls-concept:C0205374 | lld:lifeskim |
| pubmed-article:21653882 | pubmed:issue | 26 | lld:pubmed |
| pubmed-article:21653882 | pubmed:dateCreated | 2011-6-29 | lld:pubmed |
| pubmed-article:21653882 | pubmed:abstractText | Cardiac transient receptor potential canonical (TRPC) channels are crucial upstream components of Ca(2+)/calcineurin/nuclear factor of activated T cells (NFAT) signaling, thereby controlling cardiac transcriptional programs. The linkage between TRPC-mediated Ca(2+) signals and NFAT activity is still incompletely understood. TRPC conductances may govern calcineurin activity and NFAT translocation by supplying Ca(2+) either directly through the TRPC pore into a regulatory microdomain or indirectly via promotion of voltage-dependent Ca(2+) entry. Here, we show that a point mutation in the TRPC3 selectivity filter (E630Q), which disrupts Ca(2+) permeability but preserves monovalent permeation, abrogates agonist-induced NFAT signaling in HEK293 cells as well as in murine HL-1 atrial myocytes. The E630Q mutation fully retains the ability to convert phospholipase C-linked stimuli into L-type (Ca(V)1.2) channel-mediated Ca(2+) entry in HL-1 cells, thereby generating a dihydropyridine-sensitive Ca(2+) signal that is isolated from the NFAT pathway. Prevention of PKC-dependent modulation of TRPC3 by either inhibition of cellular kinase activity or mutation of a critical phosphorylation site in TRPC3 (T573A), which disrupts targeting of calcineurin into the channel complex, converts cardiac TRPC3-mediated Ca(2+) signaling into a transcriptionally silent mode. Thus, we demonstrate a dichotomy of TRPC-mediated Ca(2+) signaling in the heart constituting two distinct pathways that are differentially linked to gene transcription. Coupling of TRPC3 activity to NFAT translocation requires microdomain Ca(2+) signaling by PKC-modified TRPC3 complexes. Our results identify TRPC3 as a pivotal signaling gateway in Ca(2+)-dependent control of cardiac gene expression. | lld:pubmed |
| pubmed-article:21653882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21653882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21653882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21653882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21653882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21653882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21653882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21653882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21653882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21653882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21653882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21653882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21653882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21653882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21653882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21653882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21653882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21653882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21653882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21653882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21653882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21653882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21653882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21653882 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21653882 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21653882 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21653882 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21653882 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21653882 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21653882 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21653882 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21653882 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21653882 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21653882 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21653882 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:21653882 | pubmed:issn | 1091-6490 | lld:pubmed |
| pubmed-article:21653882 | pubmed:author | pubmed-author:GroschnerKlau... | lld:pubmed |
| pubmed-article:21653882 | pubmed:author | pubmed-author:PoteserMichae... | lld:pubmed |
| pubmed-article:21653882 | pubmed:author | pubmed-author:KappeC... | lld:pubmed |
| pubmed-article:21653882 | pubmed:author | pubmed-author:RomaninChrist... | lld:pubmed |
| pubmed-article:21653882 | pubmed:author | pubmed-author:StocknerThoma... | lld:pubmed |
| pubmed-article:21653882 | pubmed:author | pubmed-author:GlasnovToma... | lld:pubmed |
| pubmed-article:21653882 | pubmed:author | pubmed-author:SchleiferHann... | lld:pubmed |
| pubmed-article:21653882 | pubmed:author | pubmed-author:LichteneggerM... | lld:pubmed |
| pubmed-article:21653882 | pubmed:author | pubmed-author:SchernthanerM... | lld:pubmed |
| pubmed-article:21653882 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21653882 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:21653882 | pubmed:volume | 108 | lld:pubmed |
| pubmed-article:21653882 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21653882 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21653882 | pubmed:pagination | 10556-61 | lld:pubmed |
| pubmed-article:21653882 | pubmed:dateRevised | 2011-9-28 | lld:pubmed |
| pubmed-article:21653882 | pubmed:meshHeading | pubmed-meshheading:21653882... | lld:pubmed |
| pubmed-article:21653882 | pubmed:meshHeading | pubmed-meshheading:21653882... | lld:pubmed |
| pubmed-article:21653882 | pubmed:meshHeading | pubmed-meshheading:21653882... | lld:pubmed |
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| pubmed-article:21653882 | pubmed:meshHeading | pubmed-meshheading:21653882... | lld:pubmed |
| pubmed-article:21653882 | pubmed:meshHeading | pubmed-meshheading:21653882... | lld:pubmed |
| pubmed-article:21653882 | pubmed:meshHeading | pubmed-meshheading:21653882... | lld:pubmed |
| pubmed-article:21653882 | pubmed:meshHeading | pubmed-meshheading:21653882... | lld:pubmed |
| pubmed-article:21653882 | pubmed:meshHeading | pubmed-meshheading:21653882... | lld:pubmed |
| pubmed-article:21653882 | pubmed:meshHeading | pubmed-meshheading:21653882... | lld:pubmed |
| pubmed-article:21653882 | pubmed:meshHeading | pubmed-meshheading:21653882... | lld:pubmed |
| pubmed-article:21653882 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21653882 | pubmed:articleTitle | PKC-dependent coupling of calcium permeation through transient receptor potential canonical 3 (TRPC3) to calcineurin signaling in HL-1 myocytes. | lld:pubmed |
| pubmed-article:21653882 | pubmed:affiliation | Institute of Pharmaceutical Sciences, University of Graz, 8010 Graz, Austria. | lld:pubmed |
| pubmed-article:21653882 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21653882 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:22065 | entrezgene:pubmed | pubmed-article:21653882 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:21653882 | lld:entrezgene |
