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	Neuron Mar (2001); 29(3):645-55
TRPC1 and TRPC5 form a novel cation channel in mammalian brain.
Strubing C, Krapivinsky G, Krapivinsky L, Clapham DE
Howard Hughes Medical Institute, Cardiovascular Research, Children's Hospital, 320 Longwood Avenue, Department of Neurobiology, Harvard Medical School, Boston, MA 02115, USA.
Abstract: TRP proteins are cation channels responding to receptor-dependent activation of phospholipase C. Mammalian (TRPC) channels can form hetero-oligomeric channels in vitro, but native TRPC channel complexes have not been identified to date. We demonstrate here that TRPC1 and TRPC5 are subunits of a heteromeric neuronal channel. Both TRPC proteins have overlapping distributions in the hippocampus. Coexpression of TRPC1 and TRPC5 in HEK293 cells resulted in a novel nonselective cation channel with a voltage dependence similar to NMDA receptor channels, but unlike that of any reported TRPC channel. TRPC1/TRPC5 heteromers were activated by G(q)-coupled receptors but not by depletion of intracellular Ca(2+) stores. In contrast to the more common view of the TRP family as comprising store-operated channels, we propose that many TRPC heteromers form diverse receptor-regulated nonselective cation channels in the mammalian brain.
[PUBMED: 11301024]