Abstract
Store-operated Ca
2+
entry is mediated by Ca
2+
release–activated Ca
2+
(CRAC) channels following Ca
2+
release from intracellular stores. We performed a genome-wide RNA interference (RNAi) screen in
Drosophila
cells to identify proteins that inhibit store-operated Ca
2+
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.