Receptor-operated cation channels formed by TRPC4 and TRPC5

TRPC4 and TRPC5 form cation channels that contribute to phospholipase C-dependent Ca2+ entry following stimulation of G-protein-coupled receptors or receptor tyrosine kinases. Surprisingly, in different studies, TRPC4 and TRPC5 have been shown to form either store-operated channels with a relatively high Ca2+ permeability, or nonselective cation channels activated independently of store depletion. In this review, we summarize and discuss data on the regulation and permeability properties of TRPC4 and TRPC5, and data on native channels that might be composed of these isoforms.