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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
Promiscuous gating modifiers target the voltage sensor of K(v)7.2, TRPV1, and H(v)1 cation channels.
New
Attali et al., Tel Aviv-Yafo, Israel. In Faseb J, Jun 2014
The effects of NH17 and NH29 were examined in Chinese hamster ovary cells transfected with transient receptor potential vanilloid 1 (TRPV1) or K(v)7.2 channels, as well as in dorsal root ganglia neurons, using the whole-cell patch-clamp technique.
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
Channel-anchored protein kinase CK2 and protein phosphatase 1 reciprocally regulate KCNQ2-containing M-channels via phosphorylation of calmodulin.
New
Hoshi et al., In J Biol Chem, May 2014
M-type potassium channels, encoded by the KCNQ family genes (KCNQ2-5), require calmodulin as an essential co-factor.
Heteromeric Kv7.2/7.3 channels differentially regulate action potential initiation and conduction in neocortical myelinated axons.
New
Kole et al., Melbourne, Australia. In J Neurosci, Apr 2014
Rapid energy-efficient signaling along vertebrate axons is achieved through intricate subcellular arrangements of voltage-gated ion channels and myelination.
The kick-in system: a novel rapid knock-in strategy.
New
Hirose et al., Fukuoka, Japan. In Plos One, Dec 2013
To demonstrate the functionality of the kick-in methodology, we generated two mouse lines with separate mutant versions of the voltage-dependent potassium channel Kv7.2 (Kcnq2): p.Tyr284Cys (Y284C) and p.Ala306Thr (A306T); both variations have been associated with benign familial neonatal epilepsy.
Simplified molecular input line entry system-based optimal descriptors: QSAR modelling for voltage-gated potassium channel subunit Kv7.2.
New
Achary, Bhubaneshwar, India. In Sar Qsar Environ Res, Dec 2013
CORAL software has been used to build quantitative structure-activity relationships (QSARs) for the prediction of binding affinities (pEC50, i.e., minus decimal logarithm of the 50% effective concentration) of 35 potent inhibitors towards the voltage-gated potassium channel subunit Kv7.2.
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.
[New antiepileptic drugs, and therapeutic considerations].
Review
Szupera, Hungary. In Ideggyogy Sz, 2011
Retigabine is a carbamic derivate, and its anticonvulsive properties are largely due to its ability to prolong the opening of neuronal voltage-gated potassium Kv7.2 and Kv7.3 channels.
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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