TY - JOUR
T1 - New roles for a key glycine and its neighboring residue in potassium channel gating
AU - Rosenhouse-Dantsker, Avia
AU - Logothetis, Diomedes E.
N1 - Funding Information:
Confocal laser scanning microscopy was performed at the MSSM-Microscopy Shared Resource Facility, supported with funding from National Institutes of Health-National Cancer Institute shared resources grant (R24 CA095823) and National Science Foundation Major Research Instrumentation grant (DBI-9724504). This work was supported by a NIH grant (HL-54185) to D.E.L. D.E.L is an Established Investigator of the American Heart Association.
PY - 2006/10
Y1 - 2006/10
N2 - Potassium channel activation regulates cellular excitability in cells such as neurons and heart. Ion channel activity relies on a switching mechanism between two conformations, the open and closed states, known as gating. It has been suggested that potassium channels are gated via a pivoted mechanism of the pore-lining helix. Our analysis suggests that hinging occurs at the residue immediately preceding the central glycine of the inner helix. Furthermore, we show that the highly conserved central glycine is necessary to prevent constraining interactions with critical residues in its vicinity, including those located in the selectivity filter. We show that such interactions can impair channel function, and that upon their removal channel activity can be restored.
AB - Potassium channel activation regulates cellular excitability in cells such as neurons and heart. Ion channel activity relies on a switching mechanism between two conformations, the open and closed states, known as gating. It has been suggested that potassium channels are gated via a pivoted mechanism of the pore-lining helix. Our analysis suggests that hinging occurs at the residue immediately preceding the central glycine of the inner helix. Furthermore, we show that the highly conserved central glycine is necessary to prevent constraining interactions with critical residues in its vicinity, including those located in the selectivity filter. We show that such interactions can impair channel function, and that upon their removal channel activity can be restored.
UR - https://www.scopus.com/pages/publications/33749524201
U2 - 10.1529/biophysj.105.080242
DO - 10.1529/biophysj.105.080242
M3 - Article
C2 - 16877518
AN - SCOPUS:33749524201
SN - 0006-3495
VL - 91
SP - 2860
EP - 2873
JO - Biophysical Journal
JF - Biophysical Journal
IS - 8
ER -