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Potassium voltage-gated channel, shaker-related subfamily, beta member 2

Kvbeta2, KCNAB2
voltage gated potassium channel beta subunit; modifies the inactivation kinetics of the channel [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: SF-1, Kv1.4, Kv1.1, Kvbeta1, Potassium Channel
Papers on Kvbeta2
Microarray analysis of 50 patients reveals the critical chromosomal regions responsible for 1p36 deletion syndrome-related complications.
Yamamoto et al., Tokyo, Japan. In Brain Dev, May 2015
Patients with deletions larger than 6.2 Mb showed no ambulation, indicating that severe neurodevelopmental prognosis may be modified by haploinsufficiencies of KCNAB2 and CHD5, located at 6.2 Mb away from the telomere.
1p36 deletion syndrome: an update.
Scott et al., Houston, United States. In Appl Clin Genet, 2014
In particular, we highlight evidence implicating MMP23B, GABRD, SKI, PRDM16, KCNAB2, RERE, UBE4B, CASZ1, PDPN, SPEN, ECE1, HSPG2, and LUZP1 in various 1p36 deletion phenotypes.
The Kvβ2 subunit of voltage-gated potassium channels is interacting with ProSAP2/Shank3 in the PSD.
Liebau et al., Ulm, Germany. In Neuroscience, 2014
KvBeta2 (Kvβ2) on the other hand serves as a regulatory subunit of voltage-gated potassium channels.
A pilot genome-scale profiling of DNA methylation in sporadic pituitary macroadenomas: association with tumor invasion and histopathological subtype.
Zada et al., Tianjin, China. In Plos One, 2013
Compared with hormonally-active PAs, nonfunctional PAs exhibited global DNA hypermethylation (mean beta-value 0.47 versus 0.42, P = 0.005); the most significant site of differential DNA methylation was within the promoter region of the potassium voltage-gated channel KCNAB2 (FDR = 5.11×10-10).
Genetic variation in KCNA5: impact on the atrial-specific potassium current IKur in patients with lone atrial fibrillation.
Schmitt et al., Copenhagen, Denmark. In Eur Heart J, 2013
KCNAB2 encodes KVβ2, a β-subunit of KV1.5, which increases IKur.
Similar cation channels mediate protection from cerebellar exitotoxicity by exercise and inheritance.
Shoham et al., Jerusalem, Israel. In J Cell Mol Med, 2012
Inherited protection and prior exercise were both accompanied by higher cerebellar expression levels of the Kir6.1 ATP-dependent potassium channel in adjacent Bergmann glia, and voltage-gated KVbeta2 and cyclic nucleotide-gated cation HCN1 channels in basket cells.
Catalytic reduction of carbonyl groups in oxidized PAPC by Kvβ2 (AKR6).
Tipparaju et al., Louisville, United States. In Chem Biol Interact, 2011
Kvbeta2 catalyzed the NADPH-dependent reduction of several products of oxPAPC
Deletion of the mouse homolog of KCNAB2, a gene linked to monosomy 1p36, results in associative memory impairments and amygdala hyperexcitability.
Murphy et al., Ann Arbor, United States. In J Neurosci, 2011
This study demonistrated that loss of Kvbeta2 likely contributes to the cognitive and neurological impairments observed in 1p36DS patients.
Stress-evoked tyrosine phosphorylation of signal regulatory protein α regulates behavioral immobility in the forced swim test.
Matozaki et al., Maebashi, Japan. In J Neurosci, 2010
Moreover, FS stress-induced tyrosine phosphorylation of both the NR2B subunit of the NMDA subtype of glutamate receptor and the K+-channel subunit Kvbeta2 was regulated by SIRPalpha.
Characterization of ion channels involved in the proliferative response of femoral artery smooth muscle cells.
López-López et al., Valladolid, Spain. In Arterioscler Thromb Vasc Biol, 2010
mRNA expression changes showed a good correlation between the 2 proliferative models, with only 2 genes, Kv1.3 and Kvbeta2, increasing their expression on proliferation.
Dynamics of Kv1 channel transport in axons.
Gu et al., Columbus, United States. In Plos One, 2009
Expressing Kvbeta2, a Kv1 accessory subunit, markedly increased the velocity, the travel distance, and the percentage of moving time of these puncta in both anterograde and retrograde directions.
Kinetics of nucleotide binding to the beta-subunit (AKR6A2) of the voltage-gated potassium (Kv) channel.
Bhatnagar et al., Louisville, United States. In Chem Biol Interact, 2009
Kinetic studies with rat Kvbeta2 revealed that the chemical step is largely responsible for the rate-limitation but nucleotide exchange could also contribute to the overall rate.
Gene expression profile of duodenal epithelial cells in response to chronic metabolic acidosis.
Charoenphandhu et al., Bangkok, Thailand. In Mol Cell Biochem, 2009
Interestingly, 27 upregulated transcripts (e.g., Aqp1, Cacnb1, Atp1a2, Kcnab2, and Slc2a1) and 13 downregulated transcripts (e.g., Slc17a7, Slc9a4, and Slc30a3) are involved in the absorption of water, ions, and nutrients.
Kv1 potassium channel complexes in vivo require Kvbeta2 subunits in dorsal spinal neurons.
Ribera et al., Aurora, United States. In J Neurophysiol, 2008
Whereas Kvbeta2 subunits modulate potassium current properties carried by Kv1 channel complexes in heterologous systems, little is known about the contributions of Kvbeta2 subunits to native potassium channel function.
Catalytic mechanism and substrate specificity of the beta-subunit of the voltage-gated potassium channel.
Bhatnagar et al., Louisville, United States. In Biochemistry, 2008
Here we report that recombinant rat Kvbeta2 catalyzes the reduction of a wide range of aldehydes and ketones.
Modulation of voltage-dependent Shaker family potassium channels by an aldo-keto reductase.
Zhou et al., New York City, United States. In J Biol Chem, 2006
identification of Kvbeta2 substrates and the demonstration that Kvbeta2 is a functional aldo-keto reductase
Genetic modifiers of the Kv beta2-null phenotype in mice.
Messing et al., Madison, United States. In Genes Brain Behav, 2005
strain differences significantly affected survival, body weight and thermoregulation in Kv beta2-null mice
Conformational changes in the C terminus of Shaker K+ channel bound to the rat Kvbeta2-subunit.
Grigorieff et al., Waltham, United States. In Proc Natl Acad Sci U S A, 2003
There is a possibility that the K+ voltage-gated channel function is modulated by its beta-subunit.
Differential stimulation of PKC phosphorylation of potassium channels by ZIP1 and ZIP2.
Li et al., Baltimore, United States. In Science, 1999
Two alternatively spliced ZIP1 and ZIP2 proteins are described, which bind to both Kvbeta2 subunits of potassium channel and protein kinase C (PKC) zeta, thereby acting as a physical link in the assembly of PKCzeta-ZIP-potassium channel complexes.
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