CRACM1 is a plasma membrane protein essential for store-operated Ca2+ entry

被引：1102

作者：

Vig, M.

Peinelt, C.

Beck, A.

Koomoa, D. L.

Rabah, D.

Koblan-Huberson, M.

Kraft, S.

Turner, H.

Fleig, A.

Penner, R.

Kinet, J. -P.

机构：

[1] Beth Israel Deaconess Med Ctr, Dept Pathol, Boston, MA 02215 USA

[2] Harvard Univ, Sch Med, Boston, MA 02215 USA

[3] Univ Hawaii, John A Burns Sch Med, Honolulu, HI 96813 USA

[4] Univ Hawaii, Queens Med Ctr, Biomed Res Ctr, Honolulu, HI 96813 USA

来源：

SCIENCE | 2006年 / 312卷 / 5777期

关键词：

D O I：

10.1126/science.1127883

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Store-operited 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.

引用

页码：1220 / 1223

页数：4

共 15 条

[1] A severe defect in CRAC Ca2+ channel activation and altered K+ channel gating in T cells from immunodeficient patients [J].