gopubmed logo
 
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 08 Dec 2016.

Potassium voltage-gated channel, Shal-related subfamily, member 3

Kv4.3, voltage-gated K+ channel
Voltage-gated potassium (Kv) channels represent the most complex class of voltage-gated ion channels from both functional and structural standpoints. Their diverse functions include regulating neurotransmitter release, heart rate, insulin secretion, neuronal excitability, epithelial electrolyte transport, smooth muscle contraction, and cell volume. Four sequence-related potassium channel genes - shaker, shaw, shab, and shal - have been identified in Drosophila, and each has been shown to have human homolog(s). This gene encodes a member of the potassium channel, voltage-gated, shal-related subfamily, members of which form voltage-activated A-type potassium ion channels and are prominent in the repolarization phase of the action potential. This member includes two isoforms with different sizes, which are encoded by alternatively spliced transcript variants of this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Kv1.4, CAN, ACID, Kv2.1, Potassium Channel
Papers on Kv4.3
Two novel Brugada syndrome-associated mutations increase KV4.3 membrane expression and function.
New
Xu et al., Suzhou, China. In Int J Mol Med, Jul 2015
The human cardiac fast transient outward K+ channel is composed of the KV4.3 α subunit encoded by KCND3 and the K+ channel‑interacting protein 2 (KChIP2) β subunit, and determines the early repolarization of the action potential (AP).
Oral administration of putrescine and proline during the suckling period improves epithelial restitution after early weaning in piglets.
New
Yin et al., In J Anim Sci, Apr 2015
The voltage-gated K+ channel (Kv) 1.1 protein expression in the jejunum of piglets administrated with putrescine and the Kv1.5 mRNA and Kv1.1 protein levels in the ileum of piglets administrated with proline were greater than those in control piglets (P < 0.05).
Voltage‑gated K+ channel blocker quinidine inhibits proliferation and induces apoptosis by regulating expression of microRNAs in human glioma U87‑MG cells.
New
Li et al., Wuhan, China. In Int J Oncol, Feb 2015
In the present study, we investigated the effect and mechanisms of quinidine, a commonly used voltage-gated K+ channel blocker, on cell proliferation and apoptosis of human glioma U87-MG cells.
SPAK and OSR1 sensitivity of voltage-gated K+ channel Kv1.5.
New
Lang et al., Tübingen, Germany. In J Membr Biol, Feb 2015
SPS1-related proline/alanine-rich kinase (SPAK) and oxidative stress-responsive kinase 1 (OSR1) are potent regulators of several transporters and ion channels.
Molecular Cloning and Functional Expression of the Equine K+ Channel KV11.1 (Ether à Go-Go-Related/KCNH2 Gene) and the Regulatory Subunit KCNE2 from Equine Myocardium.
Klaerke et al., Frederiksberg, Denmark. In Plos One, 2014
The KCNH2 and KCNE2 genes encode the cardiac voltage-gated K+ channel KV11.1 and its auxiliary β subunit KCNE2.
A direct interaction between the sigma-1 receptor and the hERG voltage-gated K+ channel revealed by atomic force microscopy and homogeneous time-resolved fluorescence (HTRF®).
Edwardson et al., Cambridge, United Kingdom. In J Biol Chem, 2014
The sigma-1 receptor is an endoplasmic reticulum chaperone protein, widely expressed in central and peripheral tissues, which can translocate to the plasma membrane and modulate the function of various ion channels.
Modulation of the voltage-gated potassium channel (Kv4.3) and the auxiliary protein (KChIP3) interactions by the current activator NS5806.
Miksovska et al., Miami, United States. In J Biol Chem, 2014
We further determined that the association between KChIP3 and the hydrophobic N terminus of Kv4.3 is calcium-dependent, with an equilibrium dissociation constant in the apo-state of 70 ± 3 μM and 2.7 ± 0.1 μM in the calcium-bound form.
Oxidative modulation of voltage-gated potassium channels.
Review
Heinemann et al., Jena, Germany. In Antioxid Redox Signal, 2014
In vivo documentation of oxidative modifications of specific amino-acid residues of various voltage-gated K+ channel proteins, including the target specificity issue, is largely absent.
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
Novel mutations in the KCND3-encoded Kv4.3 K+ channel associated with autopsy-negative sudden unexplained death.
GeneRIF
Ackerman et al., Rochester, United States. In Hum Mutat, 2012
KCND3 may serve as a rare genetic substrate in the pathogenesis of autopsy-negative sudden unexplained death (SUD) but not sudden infant death syndrome (SIDS) cases.
Delayed endosome-dependent CamKII and p38 kinase signaling in cardiomyocytes destabilizes Kv4.3 mRNA.
GeneRIF
Levitan et al., Pittsburgh, United States. In J Mol Cell Cardiol, 2012
cardiomyocyte endosomes control channel kv4.3 mRNA expression by mediating delayed oxidative CamKII-p38K signaling.
Single cell analysis of voltage-gated potassium channels that determines neuronal types of rat hypothalamic paraventricular nucleus neurons.
GeneRIF
Lee et al., Seoul, South Korea. In Neuroscience, 2012
The expression densities of Kv4.2 and Kv4.3 channels are significantly higher in type I neurons than in type II neurons.
Modulation of human cardiac transient outward potassium current by EGFR tyrosine kinase and Src-family kinases.
GeneRIF
Li et al., Hong Kong, Hong Kong. In Cardiovasc Res, 2012
Human atrial I(to) and cloned hKv4.3 channels are modulated by EGFR kinase via phosphorylation of the Y136 residue and by Src-family kinases via phosphorylation of the Y108 residue.
Involvement of C-type inactivation gating in the actions of voltage-gated K+ channel inhibitors.
Review
Leung, Taiwan. In Pharmacol Ther, 2012
Voltage-gated K(+) (Kv) channels serve multiple functions.
Kv4 potassium channels modulate hippocampal EPSP-spike potentiation and spatial memory in rats.
GeneRIF
Mourre et al., Marseille, France. In Learn Mem, 2011
This study showed that Significant differences in Kv4.2 and Kv4.3 mRNA levels in conditioned rats. and up regulation in the brain.
Tethering chemistry and K+ channels.
Review
Kobertz et al., Worcester, United States. In J Biol Chem, 2008
This Minireview examines the synthesis and utilization of chemical tethering agents to probe and manipulate the assembly, structure, function, and molecular movements of voltage-gated K+ channel protein complexes.
Neonatal epilepsy syndromes and GEFS+: mechanistic considerations.
Review
Burgess, Houston, United States. In Epilepsia, 2004
These genes encode voltage-gated Na+ channel subunits (SCN1A, SCN2A, SCN1B), voltage-gated K+ channel subunits (KCNQ2, KCNQ3), and a ligand-gated neurotransmitter receptor subunit (GABRG2).
Molecular mechanism of cAMP modulation of HCN pacemaker channels.
Impact
Tibbs et al., New York City, United States. In Nature, 2001
Homologous CNBDs are responsible for the direct activation of cyclic nucleotide-gated channels and for modulation of the HERG voltage-gated K+ channel--important for visual and olfactory signalling and for cardiac repolarization, respectively.
Blocker protection in the pore of a voltage-gated K+ channel and its structural implications.
Impact
Yellen et al., Boston, United States. In Nature, 2000
The structure of the bacterial potassium channel KcsA has provided a framework for understanding the related voltage-gated potassium channels (Kv channels) that are used for signalling in neurons.
Evidence that the S6 segment of the Shaker voltage-gated K+ channel comprises part of the pore.
Impact
Jan et al., San Francisco, United States. In Nature, 1994
Potassium channels are highly selective and allow the rapid flux of potassium ions through their pore.
share on facebooktweetadd +1mail to friends