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Moving TRPs to the Membrane

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Science  17 Sep 2004:
Vol. 305, Issue 5691, pp. 1681
DOI: 10.1126/science.305.5691.1681c

Singh et al. report that cation channels of the transient receptor potential (TRP) family are dynamically inserted into the plasma membrane in response to ligand stimulation of G protein-coupled receptors, as recently found after stimulation of receptor tyrosine kinases. The authors identified proteins involved in exocytosis—vesicle-associated membrane protein 2 (VAMP2) and α soluble N-ethylmaleimide-sensitive factor attachment protein (αSNAP) as interacting partners for the N-terminal domain of TRPC3 in a yeast two-hybrid screen. The interaction with proteins involved in exocytosis was confirmed with heterologously expressed proteins in transfected cells and endogenously expressed protein in rat brain. Exposure of human embryonic kidney cells expressing TRPC3 to the GPCR ligand carbachol resulted in increased abundance of TRPC3 at the cell surface, and this insertion was inhibited by cleavage of VAMP2 with tetanus toxin. Measurements of calcium influx with fluorescent indicators verified that the channels were functional. Thus, regulated insertion appears to contribute to agonist-stimulated TRP activity and calcium signaling. — NG

Mol. Cell 15, 635 (2004).

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