Identification of a protein-protein interaction between KCNE1 and the activation gate machinery of KCNQ1

KCNQ1 channels assemble with KCNE1 transmembrane (TM) peptides to form voltage-gated K(+) channel complexes with slow activation gate opening. The cytoplasmic C-terminal domain that abuts the KCNE1 TM segment has been implicated in regulating KCNQ1 gating, yet its interaction with KCNQ1 has not been...

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Veröffentlicht in:	The Journal of general physiology 2010-06, Vol.135 (6), p.607-618
Hauptverfasser:	Lvov, Anatoli, Gage, Steven D, Berrios, Virla M, Kobertz, William R
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals CHO Cells Cricetinae Cricetulus Cysteine Cytoplasm Disulfides - metabolism Humans Ion Channel Gating KCNQ1 Potassium Channel - genetics KCNQ1 Potassium Channel - metabolism Membrane Potentials Membranes Models, Molecular Mutation Peptides Physiology Potassium Potassium - metabolism Potassium Channels, Voltage-Gated - genetics Potassium Channels, Voltage-Gated - metabolism Protein Binding Protein Conformation Protein Interaction Domains and Motifs Protein Interaction Mapping Proteins Time Factors Transfection
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