Conserved Gating Elements in TRPC4 and TRPC5 Channels

Andreas Beck, Tilman Speicher, Christof Stoerger, Thomas Sell, Viviane Dettmer, Siti A. Jusoh, Ammar Abdulmughni, Adolfo Cavalié, Stephan E. Philipp, Michael X. Zhu, Volkhard Helms, Ulrich Wissenbach (+1 others)
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