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Biochem Biophys Res Commun. 2002 Mar 29;292(2):339-46.

Molecular basis of the voltage-dependent gating of TREK-1, a mechano-sensitive K(+) channel.

Author information

1
Institut de Pharmacologie Moléculaire et Cellulaire, CNRS, UMR 6097, Sophia Antipolis, Valbonne, France.

Abstract

TREK-1 is a member of the mammalian two P domain K(+) channel family. Mouse TREK-1 activity, in transiently transfected COS cells, is reduced at negative resting membrane potentials by both an external Mg(2+) block and an intrinsic voltage-dependent gating mechanism leading to a strong outward rectification. Deletional and chimeric analysis demonstrates that the carboxy terminal domain of TREK-1, but not the PKA phosphorylation site S333, is responsible for voltage-dependent gating. Since the same region is also critically required for TREK-1 mechano-gating, both mechanisms might be functionally linked. Preferential opening of TREK-1 at depolarized potentials will greatly affect action potential duration, recovery from inactivation and neuronal repetitive firing activity.

PMID:
11906167
DOI:
10.1006/bbrc.2002.6674
[Indexed for MEDLINE]

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