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Biophys. J. BioFAST: First Published July 28, 2006. doi:10.1529/biophysj.105.080242
© 2006 by the Biophysical Society.

A more recent version of this article appeared on October 15, 2006.
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CHANNELS, RECEPTORS, AND ELECTRICAL SIGNALING

New roles for a key glycine and its neighboring residue in potassium channel gating

Avia Rosenhouse-Dantsker 1 and Diomedes E. Logothetis 1*

1 Mount Sinai School of Medicine

* To whom correspondence should be addressed. E-mail: diomedes.logothetis{at}mssm.edu.

Submitted on December 27, 2005
Revised on February 28, 2006
Accepted on 12 June 2006


  Abstract
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 in order 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.

Key Words: GIRK4, computer simulations, electrophysiology, gating, kir3.4, potassium channels




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Copyright © 2006 by the Biophysical Society.