@article {825336,
	title = {CRACM1 is a plasma membrane protein essential for store-operated Ca2+ entry.},
	journal = {Science},
	volume = {312},
	year = {2006},
	month = {2006 May 26},
	pages = {1220-3},
	abstract = {<p>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.</p>},
	keywords = {Animals, calcium, Calcium Channels, Cell Line, Cell Membrane, drosophila melanogaster, Drosophila Proteins, Endoplasmic Reticulum, Humans, Ion Transport, Jurkat Cells, Membrane Proteins, Patch-Clamp Techniques, Reverse Transcriptase Polymerase Chain Reaction, RNA Interference, RNA, Small Interfering},
	issn = {1095-9203},
	doi = {10.1126/science.1127883},
	author = {Vig, M and Peinelt, C and Beck, A and Koomoa, D L and Rabah, D and Koblan-Huberson, M and Kraft, S and Turner, H and Fleig, A and Penner, R and Kinet, J-P}
}
