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EMBO reports 9, 5, 472–479 (2008)
doi:10.1038/embor.2008.29
AOP Published online: 7 March 2008
Formation of a new receptor-operated channel by heteromeric assembly of TRPP2 and TRPC1 subunits
Chang-Xi Bai1*, Aurélie Giamarchi2*, Lise Rodat-Despoix2, Françoise Padilla2, Tamyra Downs1, Leonidas Tsiokas1 & Patrick Delmas2
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1 University of Oklahoma Health Sciences Center, 975 NE 10th Street, Oklahoma City, Oklahoma, 73104, USA
2 CNRS, UMR 6231, IFR Jean Roche, Université de la Méditerranée, Boulevard Pierre Dramard, 13916, Marseille Cedex 20, France
To whom correspondence should be addressed
Leonidas Tsiokas Tel: +1 405 271 8001 ext 46211; Fax: +1 405 271 3758; E-mail: leonidas-tsiokas@ouhsc.edu
Patrick Delmas Tel: +33 4 91 69 89 70; Fax: +33 4 91 69 89 77; E-mail: patrick.delmas@univmed.fr
* These authors contributed equally to this work
Received 19 July 2007; Accepted 30 January 2008; Published online 7 March 2008.
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Abstract
Although several protein–protein interactions have been reported between transient receptor potential (TRP) channels, they are all known to occur exclusively between members of the same group. The only intergroup interaction described so far is that of TRPP2 and TRPC1; however, the significance of this interaction is unknown. Here, we show that TRPP2 and TRPC1 assemble to form a channel with a unique constellation of new and TRPP2/TRPC1-specific properties. TRPP2/TRPC1 is activated in response to G-protein-coupled receptor activation and shows a pattern of single-channel conductance, amiloride sensitivity and ion permeability distinct from that of TRPP2 or TRPC1 alone. Native TRPP2/TRPC1 activity is shown in kidney cells by complementary gain-of-function and loss-of-function experiments, and its existence under physiological conditions is supported by colocalization at the primary cilium and by co-immunoprecipitation from kidney membranes. Identification of the heteromultimeric TRPP2/TRPC1 channel has implications in mechanosensation and cilium-based Ca2+ signalling.
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