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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.
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
KCNQ Potassium Channels Modulate Sensitivity of Skin D-hair Mechanoreceptors.
Jentsch et al., Delbrück, Germany. In J Biol Chem, 05 Feb 2016
UNASSIGNED: M-current mediating KCNQ (Kv7) channels play an important role in regulating the excitability of neuronal cells, as highlighted by mutations in Kcnq2 and Kcnq3 that underlie certain forms of epilepsy.
Novel KCNQ2 channel activators discovered using fluorescence-based and automated patch-clamp-based high-throughput screening techniques.
Gao et al., Shanghai, China. In Acta Pharmacol Sin, 31 Jan 2016
AIM: To establish an improved, high-throughput screening techniques for identifying novel KCNQ2 channel activators.
Expression and function of Kv7.4 channels in Rat cardiac mitochondria: possible targets for cardioprotection.
Taglialatela et al., Pisa, Italy. In Cardiovasc Res, 29 Jan 2016
AIMS: Plasmalemmal Kv7.1 (KCNQ1) channels are critical players in cardiac excitability; however, little is known on the functional role of additional Kv7 family members (Kv7.2-5) in cardiac cells.
Characterization of the Functional Domains of a Mammalian Voltage-Sensitive Phosphatase.
Bajjalieh et al., Seattle, United States. In Biophys J, 15 Jan 2016
The Mm-VSP phosphatase domain, fused to the VSD of a nonmammalian VSP, was also functional: activation resulted in PI(4,5)P2 depletion that was sufficient to inhibit the PI(4,5)P2-regulated KCNQ2/3 channels.
The Sensorless Pore Module of Kv7 Channels Embodies the Target Site for the Anticonvulsant Retigabine.
Montal et al., San Diego, United States. In J Biol Chem, 01 Jan 2016
Here we show that the novel anti-epileptic drug Retigabine (RTG) modulates channel function of pore-only modules (PM) of the human Kv7.2 (6-10) and Kv7.3(7-9) homomeric channels, and of Kv7.2/3 (6-9, 11-15) heteromeric channels by prolonging the residence time in the open state (11-13).
Uncompacted Myelin Lamellae and Nodal Ion Channel Disruption in POEMS Syndrome.
Sobue et al., Nagoya, Japan. In J Neuropathol Exp Neurol, 31 Dec 2015
Indirect immunofluorescent studies revealed abnormalities of sodium (pan sodium) and potassium (KCNQ2) channels, even at nonwidened nodes of Ranvier.
Lower KV7.5 Potassium Channel Subunit Expression in an Animal Model of Paroxysmal Dystonia.
Richter et al., Berlin, Germany. In Cns Neurol Disord Drug Targets, 10 Dec 2015
In the dtsz hamster, a model of paroxysmal dystonia, pronounced antidystonic effects of the KV7.2-5 potassium channel opener retigabine and aggravation of dystonia by a selective KV7.2-5 blocker indicated a pathophysiological role of an abnormal expression of KV7 channels.
The Role of the Carboxyl Terminus Helix C-D Linker in Regulating KCNQ3 K+ Current Amplitudes by Controlling Channel Trafficking.
Shapiro et al., San Antonio, United States. In Plos One, 2014
In the central and peripheral nervous system, the assembly of KCNQ3 with KCNQ2 as mostly heteromers, but also homomers, underlies "M-type" currents, a slowly-activating voltage-gated K+ current that plays a dominant role in neuronal excitability.
Redistribution of Kv1 and Kv7 enhances neuronal excitability during structural axon initial segment plasticity.
Adachi et al., Nagoya, Japan. In Nat Commun, 2014
In the avian cochlear nucleus, depriving afferent inputs by removing cochlea elongated the AIS, and simultaneously switched the dominant Kv channels at the AIS from Kv1.1 to Kv7.2.
A New Regulatory Mechanism for Kv7.2 Protein During Neuropathy: Enhanced Transport from the Soma to Axonal Terminals of Injured Sensory Neurons.
López-García et al., Alcalá de Henares, Spain. In Front Cell Neurosci, 2014
Kv7.2 channel expression has been reported to decrease in dorsal root ganglia (DRG) following the induction of a peripheral neuropathy while other experiments show that Kv7.2 accumulates in peripheral neuromas.
Neonatal seizures associated with a severe neonatal myoclonus like dyskinesia due to a familial KCNQ2 gene mutation.
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.
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.
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.
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.
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.
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.
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.
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 pore mutation in a novel KQT-like potassium channel gene in an idiopathic epilepsy family.
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.
A novel potassium channel gene, KCNQ2, is mutated in an inherited epilepsy of newborns.
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.
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