Calmodulin regulates Ca2+-dependent feedback inhibition of store-operated interaction with a site in the Ca2+ influx by C terminus of TrpC1

被引：112
|
作者：
Singh, BB
Liu, XB
Tang, JS
Zhu, MX
Ambudkar, IS [1 ]
机构：
[1] Natl Inst Dent & Craniofacial Res, Secretory Physiol Sect, Gene Therapy & Therapeut Branch, NIH, Bethesda, MD 20892 USA
[2] Ohio State Univ, Neurobiotechnol Ctr, Columbus, OH 43210 USA
来源：
MOLECULAR CELL | 2002年 / 9卷 / 04期
关键词：
D O I：
10.1016/S1097-2765(02)00506-3
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The mechanism involved in [Ca2+](i)-dependent feedback inhibition of store-operated Ca2+ entry (SOCE) is not yet known. Expression of Call-insensitive calmodulin (Mut-CaM) but not wild-type CaM increased SOCE and decreased its Call-dependent inactivation. Expression of TrpC1 lacking C terminus aa 664-793 (TrpC1DeltaC) also attenuated Ca2+-dependent inactivation of SOCE. CaM interacted with endogenous and expressed TrpC1 and with GST-TrpC1 C terminus but not with TrpC1DeltaC. Two CaM binding domains, aa 715749 and aa 758-793, were identified. Expression of TrpC1Delta758-793 but not TrpC1Delta715-749 mimicked the effects of TrpC1DeltaC and Mut-CaM on SOCE. These data demonstrate that CaM mediates Ca2+-dependent feedback inhibition of SOCE via binding to a domain in the C terminus of TrpC1. These findings reveal an integral role for TrpC1 in the regulation of SOCE.
引用
收藏
页码：739 / 750
页数：12
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