Mechanism and functional significance of TRPC channel multimerization

作者：Villereal Mitchel L^*

来源：Seminars in Cell & Developmental Biology, 2006, 17(6): 618-629.

DOI：10.1016/j.semcdb.2006.10.010

• store-operated channels
• receptor-operated channels
• heteromeric channels
• TRPC channels
• capacitative calcium entry

Ca2+ signaling regulates many important physiological events within a diverse set of living organisms. In particular, sustained Ca2+ signals play an important role in controlling cell proliferation, cell differentiation and the activation of immune cells. Two key elements for the generation of sustained Ca2+ signals are store-operated and receptor-operated Ca2+ channels that are activated downstream of phospholipase C (PLC) stimulation, in response to G-protein-coupled receptor or growth factor receptor stimulation. One goal of this review is to help clarify the role of canonical transient receptor potential (TRPC) proteins in the formation of native store-operated and native receptor-operated channels. Toward that end, data from studies of endogenous TRPC proteins will be reviewed in detail to highlight the strong case for the involvement of certain TRPC proteins in the formation of one subtype of store-operated channel, which exhibits a low Ca2+-selectivity, in contrast to the high Ca2+-selectivity exhibited by the CRAC subtype of store-operated channel. A second goal of this review is to highlight the growing body of evidence indicating that native store-operated and native receptor-operated channels are formed by the heteromultimerization of TRPC subunits. Furthermore, evidence will be provided to argue that some TRPC proteins are able to form multiple channel types.

• 出版日期2006-12