Up-regulation of voltage-gated sodium channels by peptides mimicking S4-S5 linkers reveals a variation of the ligand-receptor mechanism.

ABSTRACT: Prokaryotic Na_V channels are tetramers and eukaryotic Na_V channels consist of a single subunit containing four domains. Each monomer/domain contains six transmembrane segments (S1-S6), S1-S4 being the voltage-sensor domain and S5-S6 the pore domain. A crystal structure of Na_VMs, a prokaryotic Na_V channel, suggests that the S4-S5 linker (S4-S5_L) interacts with the C-terminus of S6 (S6_T) to stabilize the gate in the open state. However, in several voltage-gated potassium channels, using specific S4-S5_L-mimicking peptides, we previously demonstrated that S4-S5_L/S6_T interaction stabilizes the gate in the closed state. Here, we used the same strategy on another prokaryotic Na_V channel,

SUBMITTER: Malak OA 

PROVIDER: S-EPMC7125111 | biostudies-literature | 2020 Apr

REPOSITORIES: biostudies-literature