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Potassium voltage-gated channel, KQT-like subfamily, member 2

KCNQ2, Kv7.2
The M channel is a slowly activating and deactivating potassium channel that plays a critical role in the regulation of neuronal excitability. The M channel is formed by the association of the protein encoded by this gene and a related protein encoded by the KCNQ3 gene, both integral membrane proteins. M channel currents are inhibited by M1 muscarinic acetylcholine receptors and activated by retigabine, a novel anti-convulsant drug. Defects in this gene are a cause of benign familial neonatal convulsions type 1 (BFNC), also known as epilepsy, benign neonatal type 1 (EBN1). At least five transcript variants encoding five different isoforms have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, HAD, KCNQ1, KCNQ4, ACID
Papers using KCNQ2 antibodies
Direct interaction of myosin regulatory light chain with the NMDA receptor.
Supplier
Amédée Thierry, In PLoS ONE, 2004
... The primary antibodies used were KCNQ2-C terminus, KCNQ3-C terminus (Alomone Labs, Jerusalem, Israel) and monoclonal ...
Papers on KCNQ2
Familial neonatal seizures in 36 families: Clinical and genetic features correlate with outcome.
New
Berkovic et al., Melbourne, Australia. In Epilepsia, 15 Jun 2015
Families were screened for KCNQ2, KCNQ3, SCN2A, and PRRT2 mutations, and linkage studies were performed in mutation-negative families to exclude known loci.
Protective role of Kv7 channels in oxygen and glucose deprivation-induced damage in rat caudate brain slices.
New
Davidson et al., London, United Kingdom. In J Cereb Blood Flow Metab, 13 Jun 2015
Quantitative-PCR experiments showed that OGD caused an ~6-fold decrease in Kv7.2 transcript, while levels of mRNAs encoding for other Kv7 subunits were unaffected; western blot experiments showed a parallel reduction in Kv7.2 protein levels.
Variable clinical expression in patients with mosaicism for KCNQ2 mutations.
New
Villard et al., Marseille, France. In Am J Med Genet A, 10 Jun 2015
UNASSIGNED: Mutations in the KCNQ2 gene, encoding a potassium channel subunit, were reported in patients presenting epileptic phenotypes of varying severity.
Functional analysis of potassium channels in Kv7.2 G271V mutant causing early onset familial epilepsy.
New
Zhou et al., Xi'an, China. In Brain Res, 07 Jun 2015
The First glycine (G) residue in the pore helix of Kv7.2 (KCNQ2) subunit is highly conserved among different classes of Kv7 channel family.
Discovery of a novel Kv7 channel opener as a treatment for epilepsy.
New
Lowe et al., Cambridge, United States. In Bioorg Med Chem Lett, 01 Jun 2015
In an effort to identify a compound with such properties, the structure-activity relationship (SAR) and in vitro ADME for a series of heterocyclic Kv7.2-7.5 channel openers was explored.
Celecoxib and ion channels: a story of unexpected discoveries.
Review
New
Singh et al., Oulu, Finland. In Eur J Pharmacol, Jun 2014
In experimental systems varying from Drosophila to primary mammalian and human cell lines, celecoxib inhibits many voltage-activated Na(+), Ca(2+), and K(+) channels, including NaV1.5, L- and T-type Ca(2+) channels, KV1.5, KV2.1, KV4.3, KV7.1, KV11.1 (hERG), while stimulating other K(+) channels-KV7.2-5
Biophysics, pathophysiology, and pharmacology of ion channel gating pores.
Review
Chahine et al., Québec, Canada. In Front Pharmacol, 2013
For example, gating pores in Nav1.5 and Kv7.2 channels may underlie mixed arrhythmias associated with dilated cardiomyopathy (DCM) phenotypes and peripheral nerve hyperexcitability (PNH), respectively.
Dynamic metabolic control of an ion channel.
Review
Falkenburger et al., Seattle, United States. In Prog Mol Biol Transl Sci, 2013
We are interested in the modulation of KCNQ2/3 potassium channels by the Gq-coupled M1 muscarinic (acetylcholine) receptor (M1R).
Structure activity relationships of novel antiepileptic drugs.
Review
Roberts et al., Los Angeles, United States. In Curr Med Chem, 2013
The synaptic vesicle glycoprotein 2A (SV2A), α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPA-R) and voltage-gated potassium channels (KCNQ2/Q3) are clinically validated as new molecular targets for epilepsy.
Potassium channel genes and benign familial neonatal epilepsy.
Review
Lerche et al., Tübingen, Germany. In Prog Brain Res, 2013
Among them, KCNQ2 and KCNQ3, coding for KV7.2 and KV7.3 voltage-gated potassium channels, present an example how genetic dissection of an epileptic disorder can lead not only to a better understanding of disease mechanisms but also broaden our knowledge about the physiological function of the affected proteins and enable novel approaches in the antiepileptic therapy design.
Neonatal seizures associated with a severe neonatal myoclonus like dyskinesia due to a familial KCNQ2 gene mutation.
GeneRIF
Lerman-Sagie et al., Tel Aviv-Yafo, Israel. In Eur J Paediatr Neurol, 2012
KCNQ2 mutations can present with a neonatal onset multifocal myoclonus-like dyskinesia
The Kv7.2/Kv7.3 heterotetramer assembles with a random subunit arrangement.
GeneRIF
Edwardson et al., Cambridge, United Kingdom. In J Biol Chem, 2012
the Kv7.2-Kv7.3 heteromer assembles as a tetramer with a predominantly 2:2 subunit stoichiometry and with a random subunit arrangement.
KCNQ2 encephalopathy: emerging phenotype of a neonatal epileptic encephalopathy.
GeneRIF
de Jonghe et al., Antwerp, Belgium. In Ann Neurol, 2012
KCNQ2 mutations are found in a substantial proportion of patients with neonatal epileptic encephalopathy with a potentially recognizable electroclinical and radiological phenotype.
Regulation of neuronal M-channel gating in an isoform-specific manner: functional interplay between calmodulin and syntaxin 1A.
GeneRIF
Lotan et al., Tel Aviv-Yafo, Israel. In J Neurosci, 2011
The existence of constitutive interactions between the N and C termini in homomeric KCNQ2 and KCNQ3 channels has been determined in living cells by means of optical, biochemical, electrophysiological, and molecular biology analyses.
Kv7 channels can function without constitutive calmodulin tethering.
GeneRIF
Villarroel et al., Leioa, Spain. In Plos One, 2010
constitutive tethering of calmodulin is not required for Kv7 channel function
Moderate loss of function of cyclic-AMP-modulated KCNQ2/KCNQ3 K+ channels causes epilepsy.
Impact
Jentsch et al., Hamburg, Germany. In Nature, 1999
Potassium channels are important regulators of electrical signalling, and benign familial neonatal convulsions (BFNC), an autosomal dominant epilepsy of infancy, is caused by mutations in the KCNQ2 or the KCNQ3 potassium channel genes.
KCNQ2 and KCNQ3 potassium channel subunits: molecular correlates of the M-channel.
Impact
McKinnon et al., Stony Brook, United States. In Science, 1999
The biophysical properties, sensitivity to pharmacological blockade, and expression pattern of the KCNQ2 and KCNQ3 potassium channels were determined.
A potassium channel mutation in neonatal human epilepsy.
Impact
Steinlein et al., Bonn, Germany. In Science, 1998
In a large pedigree with BFNC, a five-base pair insertion would delete more than 300 amino acids from the KCNQ2 carboxyl terminus.
A novel potassium channel gene, KCNQ2, is mutated in an inherited epilepsy of newborns.
Impact
Leppert et al., Salt Lake City, United States. In Nat Genet, 1998
Five other BFNC probands were shown to have KCNQ2 mutations, including two transmembrane missense mutations, two frameshifts and one splice-site mutation.
A pore mutation in a novel KQT-like potassium channel gene in an idiopathic epilepsy family.
Impact
Leppert et al., Salt Lake City, United States. In Nat Genet, 1998
By positional cloning, we recently identified the gene for EBN1 as KCNQ2 (ref.
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