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Potassium voltage gated channel, Shab-related subfamily, member 1

Kv2.1, Shab, drk1
voltage gated potassium channel; involved in the excitability in nerve and muscle [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: Kv1.4, Potassium Channel, CAN, SF-1, Kv4.2
Papers using Kv2.1 antibodies
Three SNARE complexes cooperate to mediate membrane fusion.
Wenner Peter, In PLoS ONE, 2000
... The primary antibodies used were anti Kv1.1-C terminus and Kv2.1-C terminus (Alomone Labs Jerusalem, Israel), monoclonal anti ...
Papers on Kv2.1
Immunosuppressive evidence of Tityus serrulatus toxins Ts6 and Ts15: insights of a novel K(+) channel pattern in T cells.
Arantes et al., Ribeirão Preto, Brazil. In Immunology, Feb 2016
The voltage-gated potassium channel Kv1.3 is a novel target for immunomodulation of autoreactive effector memory T cells, which play a major role in the pathogenesis of autoimmune diseases.
A novel bipartite UNC-101/AP-1 μ1 binding signal mediates KVS-4/Kv2.1 somatodendritic distribution in Caenorhabditis elegans.
Shi et al., Wuhan, China. In Febs Lett, Jan 2016
Potassium channels such as Kv2.1 are targeted to specific subcellular compartments to fulfill various functions.
The Tau-Induced Reduction of mRNA Levels of Kv Channels in Human Neuroblastoma SK-N-SH Cells.
Li et al., Wuhan, China. In J Mol Neurosci, Dec 2015
In this report, transfection of tau plasmids into human neuroblastoma SK-N-SH cells caused a significant reduction in the messenger RNA (mRNA) levels of several Kv channels, including Kv2.1, Kv3.1, Kv5.1, Kv9.2, and KCNH4.
Distinct Cell- and Layer-Specific Expression Patterns and Independent Regulation of Kv2 Channel Subtypes in Cortical Pyramidal Neurons.
Trimmer et al., Antwerp, Belgium. In J Neurosci, Dec 2015
UNLABELLED: The Kv2 family of voltage-gated potassium channel α subunits, comprising Kv2.1 and Kv2.2, mediate the bulk of the neuronal delayed rectifier K(+) current in many mammalian central neurons.
Emerging potassium channel targets for the treatment of pain.
Tsantoulas, London, United Kingdom. In Curr Opin Support Palliat Care, Jun 2015
Importantly, preclinical studies confirm that K+ channel dysfunction can be a pain trigger in traumatic neuropathies (Kv9.1/Kv2.1,
Oxidative modulation of K+ channels in the central nervous system in neurodegenerative diseases and aging.
Boyle et al., Leeds, United Kingdom. In Antioxid Redox Signal, Mar 2015
RECENT ADVANCES: Oxidative regulation of the delayed rectifier Kv2.1 and the Ca(2+)- and voltage-sensitive BK channel are established, but recent studies contest how their redox sensitivity contributes to altered excitability, progression of neurodegenerative diseases, and healthy aging.
Effects of fluoxetine on protein expression of potassium ion channels in the brain of chronic mild stress rats.
Wang et al., Beijing, China. In Acta Pharm Sin B, 2015
CMS significantly increased the expression of Kv2.1 channel in frontal cortex but not in hippocampus, and the expression level was normalized after fluoxetine treatment.
Ionic mechanisms in pancreatic β cell signaling.
Berggren et al., Stockholm, Sweden. In Cell Mol Life Sci, 2014
K(+) efflux mediated by KV2.1 delayed rectifier K(+) channels, a predominant form of β cell KV channels, brings about the downstroke or repolarization phase of the action potential, which acts as a brake for insulin secretion owing to shutting down the CaV channel-mediated Ca(2+) entry.
Celecoxib and ion channels: a story of unexpected discoveries.
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
CXCL12 chemokine and its receptors as major players in the interactions between immune and nervous systems.
Guyon, Antibes, France. In Front Cell Neurosci, 2013
It can also act post-synaptically by activating a G protein activated inward rectifier K(+) (GIRK), a voltage-gated K channel Kv2.1 associated to neuronal survival, and by increasing high voltage activated Ca(2+) currents.
The C-terminus of neuronal Kv2.1 channels is required for channel localization and targeting but not for NMDA-receptor-mediated regulation of channel function.
O'Connell et al., Memphis, United States. In Neuroscience, 2012
the molecular determinants of Kv2.1 localization and modulation are distinct regions of the channel that function independently.
Expression and function of K(V)2-containing channels in human urinary bladder smooth muscle.
Petkov et al., Columbia, United States. In Am J Physiol Cell Physiol, 2012
stromatoxin-1 -sensitive KV2-containing channels are expressed in detrusor smooth muscle (DSM); they control DSM excitability, intracellular Ca2+ levels, and myogenic and nerve-evoked contractions
The voltage-dependent potassium channel subunit Kv2.1 regulates insulin secretion from rodent and human islets independently of its electrical function.
Macdonald et al., Edmonton, Canada. In Diabetologia, 2012
Direct interaction between syntaxin 1A and the Kv2.1 C-terminus is required for efficient insulin exocytosis and glucose-stimulated insulin secretion.
Toxic role of K+ channel oxidation in mammalian brain.
Sesti et al., United States. In J Neurosci, 2012
The results of this study that KCNB1 is a novel mechanism of toxicity in neurodegenerative disease.
Cholesterol enhances neuron susceptibility to apoptotic stimuli via cAMP/PKA/CREB-dependent up-regulation of Kv2.1.
Mei et al., Shanghai, China. In J Neurochem, 2012
The elevation of membrane cholesterol enhances susceptibility of cerebellar granule neurons to apoptotic stimuli via cyclic AMP/PKA/CREB-dependent up-regulation of Kv2.1.
Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment.
MacKinnon et al., New York City, United States. In Nature, 2007
Here we describe the structure of a chimaeric voltage-dependent K+ channel, which we call the 'paddle-chimaera channel', in which the voltage-sensor paddle has been transferred from Kv2.1 to Kv1.2.
SNAREing voltage-gated K+ and ATP-sensitive K+ channels: tuning beta-cell excitability with syntaxin-1A and other exocytotic proteins.
Gaisano et al., Taiwan. In Endocr Rev, 2007
We have obtained evidence that syntaxin-1A physically interacts with Kv2.1 (the predominant Kv in beta-cells) and the sulfonylurea receptor subunit of beta-cell K(ATP) channel to modify their gating behaviors.
Kv2.1 ablation alters glucose-induced islet electrical activity, enhancing insulin secretion.
Philipson et al., Chicago, United States. In Cell Metab, 2007
These results reveal the specific role of Kv2.1 in modulating glucose-stimulated action potentials of beta cells, exposing additional important currents involved in regulating physiological insulin secretion.
Graded regulation of the Kv2.1 potassium channel by variable phosphorylation.
Trimmer et al., Davis, United States. In Science, 2006
results show that variable phosphorylation of Kv2.1 at a large number of sites allows graded activity-dependent regulation of channel gating and neuronal firing properties
Permeation selectivity by competition in a delayed rectifier potassium channel.
Ikeda et al., United States. In Science, 1995
Permeation selectivity was studied in two human potassium channels, Kv2.1 and Kv1.5, expressed in a mouse cell line.
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