通过与兰尼碱受体的构象偶联对储存式通道进行门控。

Gating of store-operated channels by conformational coupling to ryanodine receptors.

作者信息

Kiselyov K I, Shin D M, Wang Y, Pessah I N, Allen P D, Muallem S

机构信息

Department of Physiology, University of Texas Southwestern Medical Center, Dallas 75235, USA.

出版信息

Mol Cell. 2000 Aug;6(2):421-31. doi: 10.1016/s1097-2765(00)00041-1.

DOI:10.1016/s1097-2765(00)00041-1

PMID:10983988

Abstract

We report here that RyRs interact with and gate the store-operated hTrp3 and Icrac channels. This gating contributes to activation of hTrp3 and Icrac by agonists. Coupling of hTrp3 to IP3Rs or RyRs in the same cells was found to be mutually exclusive. Biochemical and functional evidence suggest that mutually exclusive coupling reflects clustering and segregation of hTrp3-IP3R and hTrp3-RyR complexes in plasma membrane microdomains. Gating of CCE by RyRs indicates that gating by conformational coupling is not unique to skeletal muscle but is a general mechanism for communication between events in the plasma and endoplasmic reticulum membranes.

摘要

我们在此报告，兰尼碱受体（RyRs）与储存-操作性hTrp3和Icrac通道相互作用并对其进行门控。这种门控作用有助于激动剂对hTrp3和Icrac的激活。研究发现，同一细胞中hTrp3与IP3Rs或RyRs的偶联是相互排斥的。生化和功能证据表明，相互排斥的偶联反映了hTrp3-IP3R和hTrp3-RyR复合物在质膜微结构域中的聚集和分离。RyRs对钙库操纵性钙内流（CCE）的门控表明，构象偶联门控并非骨骼肌所特有，而是质膜和内质网膜中事件之间通讯的一种普遍机制。