The diacylgylcerol-sensitive TRPC3/6/7 subfamily of cation channels: functional characterization and physiological relevance.
Among the "classical" or "canonical" transient receptor potential (TRPC) family, the TRPC3, -6, and -7 channels share 75% amino acid identity and are gated by exposure to diacylglycerol. TRPC3, TRPC6, and TRPC7 interact physically and coassemble to form functional tetrameric channels. This review focuses on the TRPC3/6/7 subfamily and describes their functional properties and regulation as homomers obtained from overexpression studies in cell lines. It also summarizes their heteromultimerization potential in vitro and in vivo and presents initial data concerning their physiological functions analyzed in isolated tissues with downregulated channel activity and gene-deficient mouse models.
Dietrich
Alexander
A
Institut für Pharmakologie und Toxikologie, PhilippsUniversität Marburg, Karl-von-Frisch-Str. 1, 35043 Marburg, Germany. dietrica@staff.uni-marburg.de
Kalwa
Hermann
H
Rost
Benjamin R
BR
Gudermann
Thomas
T
D000818:Animals; D004075:Diglycerides / Q000494:pharmacology*; D006801:Humans; D020836:Protein Structure, Quaternary; D050052:TRPC Cation Channels / Q000737:chemistry / Q000187:drug effects / Q000502:physiology*; D014018:Tissue Distribution; D010738:Type C Phospholipases / Q000502:physiology
D004075:Diglycerides; D050052:TRPC Cation Channels; C104603:TRPC3 cation channel; C498501:TRPC7 protein, human; D010738:Type C Phospholipases