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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, KCNQ1, HAD, 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
Oxidation Potentials of N-Modified Derivatives of the Analgesic Flupirtine Linked to Potassium KV 7 Channel Opening Activity But Not Hepatocyte Toxicity.
New
Link et al., Greifswald, Germany. In Chemmedchem, 12 Dec 2014
KV 7.2/3 (KCNQ2/3) opening activity was determined by an established assay with HEK293 cells overexpressing these channels.
Capturing distinct KCNQ2 channel resting states by metal ion bridges in the voltage-sensor domain.
New
Paas et al., Tel Aviv-Yafo, Israel. In J Gen Physiol, 10 Dec 2014
Here, we investigated the VSD resting state of KCNQ2, a K(+) channel subunit belonging to the KCNQ (Kv7) subfamily of Kv channels.
Clicked bis-PEG-peptide conjugates for studying calmodulin-Kv7.2 channel binding.
New
González-Muñiz et al., Madrid, Spain. In Org Biomol Chem, 21 Nov 2014
The recombinant Kv7.2 calmodulin (CaM) binding site (Q2AB CaMBD) shows a high tendency to aggregate, thus complicating biochemical and structural studies.
Abnormal gating of axonal slow potassium current in cramp-fasciculation syndrome.
New
Kaji et al., Tokushima, Japan. In Clin Neurophysiol, 28 Oct 2014
None of these patients had a mutation in the KCNQ2, 3, or 5 genes.
KCNQ/Kv7 channel activator flupirtine protects against acute stress-induced impairments of spatial memory retrieval and hippocampal LTP in rats.
New
Xu et al., Wuhan, China. In Neuroscience, 16 Oct 2014
Acute stress transiently decreased the expression of KCNQ2 and KCNQ3 in the hippocampus.
Structure activity relationships of novel antiepileptic drugs.
Review
New
Roberts et al., Los Angeles, United States. In Curr Med Chem, Dec 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.
Biophysics, pathophysiology, and pharmacology of ion channel gating pores.
Review
New
Chahine et al., Québec, Canada. In Front Pharmacol, Dec 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.
Video/EEG findings in a KCNQ2 epileptic encephalopathy: a case report and revision of literature data.
Review
New
Fusco et al., Roma, Italy. In Epileptic Disord, Jun 2013
We describe the EEG findings of an infant with early-onset epileptic encephalopathy with mutation of the KCNQ2 gene and a family history of neonatal seizures.
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.
The urinary safety profile and secondary renal effects of retigabine (ezogabine): a first-in-class antiepileptic drug that targets KCNQ (K(v)7) potassium channels.
Review
DeRossett et al., Fort Smith, United States. In Epilepsia, 2012
Retigabine (RTG; international nonproprietary name)/ezogabine (EZG; North American adopted name), a first-in-class antiepileptic drug (AED) that reduces neuronal excitability primarily by enhancing the activity of KCNQ2/3 (K(v)7.2/7.3)
The mechanism of action of retigabine (ezogabine), a first-in-class K+ channel opener for the treatment of epilepsy.
Review
Sankar et al., Harlow, United Kingdom. In Epilepsia, 2012
Its primary mechanism of action (MoA) as a positive allosteric modulator of KCNQ2-5 (K(v) 7.2-7.5)
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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