Citation:
M Vig, C Peinelt, A Beck, DL Koomoa, D Rabah, M Koblan-Huberson, S Kraft, H Turner, A Fleig, R Penner, and J-P Kinet. 2006. “CRACM1 is a plasma membrane protein essential for store-operated Ca2+ entry.” Science, 312, 5777, Pp. 1220-3.
 | 2006_Science_Vig.pdf | 913 KB |
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.