Abstract
Canonical transient receptor potential (TPRC) channels are Ca2+-permeable nonselective cation channels that are widely expressed in numerous cell types. Seven different members of TRPC channels are isolated and canonical type of TRP channel family transduces signals of GPCR with various external stimuli. TRPC4 channels are known to be regulated by Gαi proteins. However, the molecular mechanism how Gαi proteins activate TRPC4 still remains to be questionable. To investigate the mechanism, we used whole patch clamp and FRET (FluorescenceResonance Energy transfer). We tagged mTRPC4 and G protein with CFP and YFP, respectively, and transiently transfected HEK293 cells with FRET pair. FRET efficiency between TRPC4 and Gα was 8.08 2.24% (n = 11) and was greater than those between TRPC4 and Gβγ (4.00 1.67 (n = 11)). At the HEK293 cell transfected with M2 muscarinic receptor, application of carbachol (CCh) increased FRET efficieny from 9.66 4.64 % (n = 7) to 26.27 10.09 % (n = 7). Intracellular 0.2mM GTPγS also increased FRET efficiency and TRPC4 current. In conclusion, we suggest that Gαi closely locates near TRPC4 and regulates TRPC4 channel activity.∗ This research was supported by the National Research Foundation of Korea (NRF) funded by the Korea government (MEST) (2008-2005948 and 2010-0019472).
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