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Neuron. 2001 Mar;29(3):645-55.

TRPC1 and TRPC5 form a novel cation channel in mammalian brain.

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1
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.

PMID:
11301024
[Indexed for MEDLINE]
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