M-type KCNQ2–KCNQ3 potassium channels are modulated by the KCNE2 subunit

KCNQ2 and KCNQ3 subunits belong to the six transmembrane domain K + channel family and loss of function mutations are associated with benign familial neonatal convulsions. KCNE2 (MirP1) is a single transmembrane domain subunit first described to be a modulator of the HERG potassium channel in the he...

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Bibliographic Details
Published in:FEBS letters 2000-09, Vol.480 (2), p.137-141
Main Authors: Tinel, Norbert, Diochot, Sylvie, Lauritzen, Inger, Barhanin, Jacques, Lazdunski, Michel, Borsotto, Marc
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
BFNC, benign familial neonatal convulsions
Brain - metabolism
Brain - pathology
COS Cells
Electrophysiology
Epilepsy
Humans
Immunoprecipitation
In situ hybridization
In Situ Hybridization - methods
KCNQ2 Potassium Channel
KCNQ3 Potassium Channel
Molecular Sequence Data
PCR, polymerase chain reaction
Potassium channel
Potassium Channels - genetics
Potassium Channels - metabolism
Potassium Channels - physiology
Potassium Channels, Voltage-Gated
Precipitin Tests
Rats
Regulatory protein
Sequence Analysis, Protein
Sequence Homology, Amino Acid
Tissue Distribution
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Summary:KCNQ2 and KCNQ3 subunits belong to the six transmembrane domain K + channel family and loss of function mutations are associated with benign familial neonatal convulsions. KCNE2 (MirP1) is a single transmembrane domain subunit first described to be a modulator of the HERG potassium channel in the heart. Here, we show that KCNE2 is present in brain, in areas which also express KCNQ2 and KCNQ3 channels. We demonstrate that KCNE2 associates with KCNQ2 and/or KCNQ3 subunits. In transiently transfected COS cells, KCNE2 expression produces an acceleration of deactivation kinetics of KCNQ2 and of the KCNQ2–KCNQ3 complex. Effects of two previously identified arrhythmogenic mutations of KCNE2 have also been analyzed.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(00)01918-9