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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
KCNQ Potassium Channels Modulate Sensitivity of Skin D-hair Mechanoreceptors.
New
Jentsch et al., Delbrück, Germany. In J Biol Chem, 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.
New
Gao et al., Shanghai, China. In Acta Pharmacol Sin, 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.
New
Taglialatela et al., Pisa, Italy. In Cardiovasc Res, 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.
Genetics of pediatric epilepsy.
Review
New
Mikati et al., Durham, United States. In Pediatr Clin North Am, Jun 2015
Examples of that include the need to avoid specific drugs in Dravet syndrome and the ongoing investigations of the potential use of new directed therapies such as retigabine in KCNQ2-related epilepsies, quinidine in KCNT1-related epilepsies, and memantine in GRIN2A-related epilepsies.
Eslicarbazepine acetate for the treatment of focal epilepsy: an update on its proposed mechanisms of action.
Review
New
Wright et al., São Mamede de Infesta, Portugal. In Pharmacol Res Perspect, Mar 2015
These preclinical findings may suggest the potential for antiepileptogenic effects; furthermore, the lack of effect upon KV7.2 outward currents may translate into a reduced potential for eslicarbazepine to facilitate repetitive firing.
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.
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.
Celecoxib and ion channels: a story of unexpected discoveries.
Review
Singh et al., Oulu, Finland. In Eur J Pharmacol, 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
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.
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.
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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