Kv7 channels can function without constitutive calmodulin tethering

M-channels are voltage-gated potassium channels composed of Kv7.2-7.5 subunits that serve as important regulators of neuronal excitability. Calmodulin binding is required for Kv7 channel function and mutations in Kv7.2 that disrupt calmodulin binding cause Benign Familial Neonatal Convulsions (BFNC)...

Full description

Saved in:

Bibliographic Details
Published in:	PloS one Vol. 6; no. 9; p. e25508
Main Authors:	Gómez-Posada, Juan Camilo, Aivar, Paloma, Alberdi, Araitz, Alaimo, Alessandro, Etxeberría, Ainhoa, Fernández-Orth, Juncal, Zamalloa, Teresa, Roura-Ferrer, Meritxell, Villace, Patricia, Areso, Pilar, Casis, Oscar, Villarroel, Alvaro
Format:	Journal Article
Language:	English
Published:	United States Public Library of Science 28-09-2011 Public Library of Science (PLoS)
Subjects:	Amino Acid Sequence Animals Binding sites Biology Calcium-binding protein Calmodulin Calmodulin - metabolism Cell Membrane - metabolism Channels Convulsions Epilepsy Excitability Gene Expression Regulation HEK293 Cells Humans KCNQ2 Potassium Channel - chemistry KCNQ2 Potassium Channel - genetics KCNQ2 Potassium Channel - metabolism KCNQ3 Potassium Channel - chemistry KCNQ3 Potassium Channel - genetics KCNQ3 Potassium Channel - metabolism Kinases Medicine Molecular Sequence Data Mutants Mutation Neonates Neurons Phosphorylation Potassium Potassium channels Potassium channels (voltage-gated) Protein Structure, Secondary Protein Transport Regulators Rodents Tethering Xenopus San Francisco California California Spain
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!

Description
Summary:	M-channels are voltage-gated potassium channels composed of Kv7.2-7.5 subunits that serve as important regulators of neuronal excitability. Calmodulin binding is required for Kv7 channel function and mutations in Kv7.2 that disrupt calmodulin binding cause Benign Familial Neonatal Convulsions (BFNC), a dominantly inherited human epilepsy. On the basis that Kv7.2 mutants deficient in calmodulin binding are not functional, calmodulin has been defined as an auxiliary subunit of Kv7 channels. However, we have identified a presumably phosphomimetic mutation S511D that permits calmodulin-independent function. Thus, our data reveal that constitutive tethering of calmodulin is not required for Kv7 channel function.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Current address: Current address: Max Planck Institute for Experimental Medicine, Göttingen, Germany Conceived and designed the experiments: AV JCG-P P. Aivar A. Alaimo. Performed the experiments: JCG-P P. Aivar A. Alaimo A. Alberti AE JF-O OC TZ. Analyzed the data: JCG-P A. Alaimo A. Alberti TZ. Contributed reagents/materials/analysis tools: PV P. Areso. Wrote the paper: AV. Reviewed the design of experiments: PV. Assisted in the execution of imaging experiments: MR. Conceived experiments: P. Areso. Current address: Instituto Cajal, Av. Dr. Arce 37, Madrid, Spain Current address: Innoprot, Parque Tecnológico de Bizkaia, Derio, Spain Current address: Department of Neurology, University of California San Francisco, Genentech Hall, San Francisco, California, USA
ISSN:	1932-6203 1932-6203
DOI:	10.1371/journal.pone.0025508