Protein-protein interaction and functionTRPC channels

被引:43
作者
Kiselyov, K [1 ]
Kim, JY
Zeng, WZ
Muallem, S
机构
[1] Univ Pittsburgh, Dept Biol Sci, Pittsburgh, PA 15260 USA
[2] Univ Texas, SW Med Ctr, Dept Physiol, Dallas, TX 75390 USA
来源
PFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY | 2005年 / 451卷 / 01期
关键词
TRPC channels; multimerization; scaffolds; insertion/retrieval; ER/PM communication; channel gating;
D O I
10.1007/s00424-005-1442-2
中图分类号
Q4 [生理学];
学科分类号
071003 ;
摘要
Since their identification in the concluding years of the last century, the mammalian transient receptor potential ( canonical) ( TRPC) channels have remained in the limelight as the primary candidates for the Ca2+ entry pathway activated by the hormones, growth factors, and neurotransmitters that exert their effect through activation of PLC. Although TRPC channels have been shown clearly to mediate, at least in part, receptor-activated Ca2+ entry in literally all cell types, several of their central characteristics, as recorded in expression systems using recombinant channels, differ from those of the native receptor-dependent Ca2+ influx channels. The present review attempts to highlight the interaction of TRPC channels with other proteins, which may explain the variability of TRPC channel activation and regulatory mechanisms observed with the native and recombinant channels. These include the homologous and heterotopous interactions of TRPC channel isoforms, the interaction of TRPC channels with calmodulin, PLC gamma, IP3 receptors, and with scaffolding proteins like InaD, EBP50/NEHRF, caveolin, Janctate and Homers.
引用
收藏
页码:116 / 124
页数:9
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