Abstract:
:Voltage-sensor domains (VSDs) in voltage-gated ion channels are thought to regulate the probability that a channel adopts an open conformation by moving vertically in the lipid bilayer. Here we characterized the movement of the VSDs of the prokaryotic voltage-gated sodium channel, NaChBac. Substitution of residue T110, which is located on the extracellular side of the fourth transmembrane helix of the VSD, by cysteine resulted in the formation of a disulfide bond between adjacent subunits in the channel. Our results suggest that T110 residues in VSDs of adjacent subunits can come into close proximity, implying that the VSDs can move laterally in the membrane and constitute a mechanism that regulates channel activity.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Nagura H,Irie K,Imai T,Shimomura T,Hige T,Fujiyoshi Ydoi
10.1016/j.bbrc.2010.07.070subject
Has Abstractpub_date
2010-08-27 00:00:00pages
341-6issue
3eissn
0006-291Xissn
1090-2104pii
S0006-291X(10)01381-1journal_volume
399pub_type
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