| Literature DB >> 16645049 |
M Vig1, C Peinelt, A Beck, D L Koomoa, D Rabah, M Koblan-Huberson, S Kraft, H Turner, A Fleig, R Penner, J-P Kinet.
Abstract
Store-operated Ca2+ entry is mediated by Ca2+ release-activated Ca2+ (CRAC) channels following Ca2+ release from intracellular stores. We performed a genome-wide RNA interference (RNAi) screen in Drosophila cells to identify proteins that inhibit store-operated Ca2+ influx. A secondary patch-clamp screen identified CRACM1 and CRACM2 (CRAC modulators 1 and 2) as modulators of Drosophila CRAC currents. We characterized the human ortholog of CRACM1, a plasma membrane-resident protein encoded by gene FLJ14466. Although overexpression of CRACM1 did not affect CRAC currents, RNAi-mediated knockdown disrupted its activation. CRACM1 could be the CRAC channel itself, a subunit of it, or a component of the CRAC signaling machinery.Entities:
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Year: 2006 PMID： 16645049 PMCID： PMC5685805 DOI： 10.1126/science.1127883
Source DB: PubMed Journal: Science ISSN： 0036-8075 Impact factor: 47.728