| pubmed-article:16959851 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16959851 | lifeskim:mentions | umls-concept:C0034721 | lld:lifeskim |
| pubmed-article:16959851 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
| pubmed-article:16959851 | lifeskim:mentions | umls-concept:C0006772 | lld:lifeskim |
| pubmed-article:16959851 | lifeskim:mentions | umls-concept:C0004083 | lld:lifeskim |
| pubmed-article:16959851 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:16959851 | lifeskim:mentions | umls-concept:C0851827 | lld:lifeskim |
| pubmed-article:16959851 | lifeskim:mentions | umls-concept:C1701901 | lld:lifeskim |
| pubmed-article:16959851 | lifeskim:mentions | umls-concept:C0205232 | lld:lifeskim |
| pubmed-article:16959851 | lifeskim:mentions | umls-concept:C0908152 | lld:lifeskim |
| pubmed-article:16959851 | pubmed:issue | Pt 1 | lld:pubmed |
| pubmed-article:16959851 | pubmed:dateCreated | 2006-11-19 | lld:pubmed |
| pubmed-article:16959851 | pubmed:abstractText | The Ca(2+)-selective TRPV6 as well as the L-type Ca(2+) channel are regulated by the Ca(2+)-binding protein calmodulin (CaM). Here, we investigated the interaction of CaM with rat (r)TRPV6 in response to alterations of intracellular Ca(2+), employing Ca(2+)-imaging and patch-clamp techniques. Additionally, confocal Förster resonance energy transfer (FRET) microscopy on living cells was utilized as a key method to visualize in vivo protein-protein interactions essential for CaM regulation of rTRPV6 activity. The effects of overexpressed CaM or its Ca(2+)-insensitive mutant (CaM(MUT)) was probed on various rTRPV6 mutants and fragments in an attempt to elucidate the molecular mechanism of Ca(2+)/CaM-dependent regulation and to pinpoint the physiologically relevant rTRPV6-CaM interaction site. A significant reduction of rTRPV6 activity, as well as an increase in current inactivation, were observed when CaM was overexpressed in addition to endogenous CaM. The Ca(2+)-insensitive CaM(MUT), however, failed to affect rTRPV6-derived currents. Accordingly, live cell confocal FRET microscopy revealed a robust interaction for CaM but not CaM(MUT) with rTRPV6, suggesting a strict Ca(2+) dependence for their association. Indeed, interaction of rTRPV6 or its C terminus with CaM increased with rising intracellular Ca(2+) levels, as observed by dynamic FRET measurements. An rTRPV6Delta(695-727) mutant with the very C-terminal end deleted, yielded Ca(2+) currents with a markedly reduced inactivation in accordance with a lack of CaM interaction as substantiated by FRET microscopy. These results, in contrast with those for CaM-dependent L-type Ca(2+) channel inactivation, demonstrate a dynamic association of CaM with the very C-terminal end of rTRPV6 (aa 695-727), and this enables acceleration of the rate of rTRPV6 current inactivation with increasing intracellular CaM concentrations. | lld:pubmed |
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| pubmed-article:16959851 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16959851 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16959851 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16959851 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16959851 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16959851 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16959851 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:16959851 | pubmed:issn | 0022-3751 | lld:pubmed |
| pubmed-article:16959851 | pubmed:author | pubmed-author:GroschnerKlau... | lld:pubmed |
| pubmed-article:16959851 | pubmed:author | pubmed-author:SchindlRainer... | lld:pubmed |
| pubmed-article:16959851 | pubmed:author | pubmed-author:KahrHeikeH | lld:pubmed |
| pubmed-article:16959851 | pubmed:author | pubmed-author:RomaninChrist... | lld:pubmed |
| pubmed-article:16959851 | pubmed:author | pubmed-author:FritschReinha... | lld:pubmed |
| pubmed-article:16959851 | pubmed:author | pubmed-author:HofbauerMicha... | lld:pubmed |
| pubmed-article:16959851 | pubmed:author | pubmed-author:HackMarlene... | lld:pubmed |
| pubmed-article:16959851 | pubmed:author | pubmed-author:MoritzSieglin... | lld:pubmed |
| pubmed-article:16959851 | pubmed:author | pubmed-author:DerlerIsabell... | lld:pubmed |
| pubmed-article:16959851 | pubmed:author | pubmed-author:MuikMartinM | lld:pubmed |
| pubmed-article:16959851 | pubmed:author | pubmed-author:KepplingerKla... | lld:pubmed |
| pubmed-article:16959851 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16959851 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:16959851 | pubmed:volume | 577 | lld:pubmed |
| pubmed-article:16959851 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16959851 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16959851 | pubmed:pagination | 31-44 | lld:pubmed |
| pubmed-article:16959851 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:16959851 | pubmed:meshHeading | pubmed-meshheading:16959851... | lld:pubmed |
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| pubmed-article:16959851 | pubmed:meshHeading | pubmed-meshheading:16959851... | lld:pubmed |
| pubmed-article:16959851 | pubmed:meshHeading | pubmed-meshheading:16959851... | lld:pubmed |
| pubmed-article:16959851 | pubmed:meshHeading | pubmed-meshheading:16959851... | lld:pubmed |
| pubmed-article:16959851 | pubmed:meshHeading | pubmed-meshheading:16959851... | lld:pubmed |
| pubmed-article:16959851 | pubmed:meshHeading | pubmed-meshheading:16959851... | lld:pubmed |
| pubmed-article:16959851 | pubmed:meshHeading | pubmed-meshheading:16959851... | lld:pubmed |
| pubmed-article:16959851 | pubmed:meshHeading | pubmed-meshheading:16959851... | lld:pubmed |
| pubmed-article:16959851 | pubmed:meshHeading | pubmed-meshheading:16959851... | lld:pubmed |
| pubmed-article:16959851 | pubmed:meshHeading | pubmed-meshheading:16959851... | lld:pubmed |
| pubmed-article:16959851 | pubmed:meshHeading | pubmed-meshheading:16959851... | lld:pubmed |
| pubmed-article:16959851 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16959851 | pubmed:articleTitle | Dynamic but not constitutive association of calmodulin with rat TRPV6 channels enables fine tuning of Ca2+-dependent inactivation. | lld:pubmed |
| pubmed-article:16959851 | pubmed:affiliation | Institute for Biophysics, University of Linz, Altenbergerstr. 69, A-4040 Linz, Austria. | lld:pubmed |
| pubmed-article:16959851 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16959851 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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