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Originally published in Science Express on 27 April 2006
Science 26 May 2006:
Vol. 312. no. 5777, pp. 1220 - 1223
DOI: 10.1126/science.1127883
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Reports

CRACM1 Is a Plasma Membrane Protein Essential for Store-Operated Ca2+ Entry

M. Vig,1* C. Peinelt,2 A. Beck,2 D. L. Koomoa,2 D. Rabah,1 M. Koblan-Huberson,1 S. Kraft,1 H. Turner,2 A. Fleig,2 R. Penner,2* J.-P. Kinet1*

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.

1 Department of Pathology, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, MA 02215, USA.
2 Center for Biomedical Research at The Queen's Medical Center and John A. Burns School of Medicine at the University of Hawaii, Honolulu, HI 96813, USA.

* To whom correspondence should be addressed. E-mail: mvig{at}bidmc.harvard.edu (M.V.); rpenner{at}hawaii.edu (R.P.); jkinet{at}bidmc.harvard.edu (J.-P.K.)

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