Receptor-operated cation channels formed by TRPC4 and TRPC5.
TRPC4 and TRPC5 form cation channels that contribute to phospholipase C-dependent Ca(2+) 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 Ca(2+) 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.
Plant
Tim D
TD
Institut für Pharmakologie und Toxikologie, FB-Medizin, Philipps-Universität-Marburg, Karl-von-Frisch-Strasse 1, 35033, Marburg, Germany. plant@staff.uni-marburg.de
Schaefer
Michael
M
D000818:Animals; D002118:Calcium / Q000378:metabolism*; D015220:Calcium Channels / Q000235:genetics / Q000378:metabolism / Q000502:physiology; D006801:Humans; D015640:Ion Channel Gating / Q000502:physiology*; D051379:Mice; D010740:Phospholipases / Q000378:metabolism*; D051381:Rats; D043562:Receptors, G-Protein-Coupled / Q000378:metabolism*; D050052:TRPC Cation Channels / Q000235:genetics / Q000378:metabolism / Q000502:physiology*
D015220:Calcium Channels; D043562:Receptors, G-Protein-Coupled; D050052:TRPC Cation Channels; C489571:TRPC4 ion channel; C491780:TRPC5 protein, human; C112021:Trpc5 protein, mouse; C503500:Trpc5 protein, rat; D010740:Phospholipases; D002118:Calcium