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Conserved Gating Elements in TRPC4 and TRPC5 Channels
2013
Journal of Biological Chemistry
Gating mechanisms of TRPC channels are mostly unknown. Results: Replacing the highly conserved glycine residue within the linker between transmembrane domains 4 and 5 by serine renders TRPC4 and TRPC5 channels constitutively active. Conclusion: TRPC channel opening seems to require similar constraints than the voltage-gated potassium channels. Significance: Novel mechanistic insights into structural requirements of TRPC channel gating are provided.
doi:10.1074/jbc.m113.478305
pmid:23677990
pmcid:PMC3707650
fatcat:27irul2sjzb4xb5vub3ae6u7qy