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Potassium voltage gated channel, shaker related subfamily, member 6

Kv1.6, KCNA6, RCK2
voltage-gated potassium channel [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: Kv1.1, SF-1, Kv1.4, Kv1.3, Potassium Channel
Papers on Kv1.6
α-dendrotoxin sensitive Kv1 channels contribute to conduction failure of polymodal nociceptive C-fibers from rat coccygeal nerve.
Duan et al., In J Neurophysiol, Dec 2015
Expression of Kv channel subunits Kv1.2 and Kv1.6 were down-regulated in both small dorsal root ganglion neurons and peripheral C-fibers.
Development of highly selective Kv1.3-blocking peptides based on the sea anemone peptide ShK.
Beeton et al., Louisville, United States. In Mar Drugs, 2015
Other potentially important Kv channels such as Kv1.4 and Kv1.6 were only partially blocked at 100 nM concentrations of each of the ShK analogs.
Expression of RCK2 MAPKAP (MAPK-activated protein kinase) rescues yeast cells sensitivity to osmotic stress.
Greetham et al., Nottingham, United Kingdom. In Microb Cell Fact, 2014
RESULTS: RCK2 encodes for a MAPKAP (MAPK-activated protein kinase) enzyme and was identified on a locus by QTL analysis in yeast cells under osmotic stress, RCK2 expression was placed under a tetracycline regulatable vector and rescued glucose, sorbitol or glycerol induced osmotic stress in an rck2 null strain.
Identification of Region-Specific Myocardial Gene Expression Patterns in a Chronic Swine Model of Repaired Tetralogy of Fallot.
Rooryck et al., Pessac, France. In Plos One, 2014
Moreover, calcium handling and contractile function genes (SLN, ACTC1, PLCD4, PLCZ), potential arrhythmia-related genes (MYO5B, KCNA5), and cytoskeleton and cellular organization-related genes (XIRP2, COL8A1, KCNA6) were among the most deregulated genes in rTOF ventricles.
Differential expression of the Kv1 voltage-gated potassium channel family in the rat nephron.
Escobar et al., Mexico. In J Mol Histol, 2014
Kv1.3 and Kv1.6 channels in collecting ducts of the rat inner medulla.
A family of excitatory peptide toxins from venomous crassispirine snails: using Constellation Pharmacology to assess bioactivity.
Olivera et al., Salt Lake City, United States. In Toxicon, 2014
We demonstrate that two of these crassipeptides, cce9a and cce9b, elicited an excitatory phenotype in a subset of small-diameter capsaicin-sensitive mouse DRG neurons that were also affected by κJ-conotoxin PlXIVA (pl14a), a blocker of Kv1.6 channels.
The Kv1.3 potassium channel is localized to the cis-Golgi and Kv1.6 is localized to the endoplasmic reticulum in rat astrocytes.
Thornhill et al., United States. In Febs J, 2014
Kv1.1, Kv1.3 and Kv1.6 are endogenously expressed in C6 astrocytoma cells, but their trafficking and subcellular localization have not been well studied.
The genetic basis of variation in clean lineages of Saccharomyces cerevisiae in response to stresses encountered during bioethanol fermentations.
Smart et al., Loughborough, United Kingdom. In Plos One, 2013
We tested candidate genes within loci identified by QTL using reciprocal hemizygosity analysis to ascertain their contribution to the observed phenotypic variation; this approach validated a gene (COX20) for weak acid stress and a gene (RCK2) for osmotic stress.
Shaker-related potassium channels in the central medial nucleus of the thalamus are important molecular targets for arousal suppression by volatile general anesthetics.
Alkire et al., Irvine, United States. In J Neurosci, 2013
The modulation of Kv1 channels by volatiles is network specific as microinfusion of ShK, a potent inhibitor of Kv1.1, Kv1.3, and Kv1.6 channels, into the CMT awakened sevoflurane-anesthetized rodents.
Activation of lysophosphatidic Acid receptor is coupled to enhancement of ca(2+)-activated potassium channel currents.
Nah et al., Seoul, South Korea. In Korean J Physiol Pharmacol, 2013
In addition, mutations in RCK1 and RCK2 also attenuated LPA-mediated BKCa channel activation.
SLO-2 isoforms with unique Ca(2+) - and voltage-dependence characteristics confer sensitivity to hypoxia in C. elegans.
Logothetis et al., Richmond, United States. In Channels (austin), 2013
Most importantly, SLO-2 provides a unique case in the Slo family for sensing Ca ( 2+) with the high-affinity Ca ( 2+) regulatory site in the RCK1 but not the RCK2 domain, formed through interactions with residues E319 and E487 (that correspond to D362 and E535 of Slo1, respectively).
Biochemical and electrophysiological characterization of two sea anemone type 1 potassium toxins from a geographically distant population of Bunodosoma caissarum.
Tytgat et al., São Paulo, Brazil. In Mar Drugs, 2013
Their functional characterization was performed by means of a wide electrophysiological screening on 12 different subtypes of KV channels (KV1.1-KV1.6;
Developmental changes in the expression of Κv1 potassium channels in rat vestibular ganglion cells.
Yamasoba et al., Tokyo, Japan. In Brain Res, 2012
down-regulation of the Kv1.6 protein and mRNA may be associated with maturation of excitable properties of primary vestibular neurons
Position-dependent attenuation by Kv1.6 of N-type inactivation of Kv1.4-containing channels.
Dolly et al., Dublin, Ireland. In Biochem J, 2011
N-type inactivation prevention (NIP) domain function was shown to require positioning of Kv1.6 adjacent to the Kv1.4 subunit.
Clinical spectrum of voltage-gated potassium channel autoimmunity.
Pittock et al., Rochester, United States. In Neurology, 2008
The spectrum of neurologic manifestations and neoplasms associated with voltage-gated potassium channel (VGKC) autoimmunity is broader than previously recognized
The RCK2 domain of the human BKCa channel is a calcium sensor.
Olcese et al., Los Angeles, United States. In Proc Natl Acad Sci U S A, 2008
analysis of how the RCK2 domain of the human BKCa channel is a calcium sensor
Two opposing roles of 4-AP-sensitive K+ current in initiation and invasion of spikes in rat mesencephalic trigeminal neurons.
Kang et al., Suita, Japan. In J Neurophysiol, 2006
Consistent with these findings, strong immunoreactivities for Kv1.1 and Kv1.6, among 4-AP-sensitive and low-voltage-activated Kv1 family examined, were detected in the soma but not in the stem axon of MTN neurons.
Dendrotoxins: structure-activity relationships and effects on potassium ion channels.
Robertson et al., Glasgow, United Kingdom. In Curr Med Chem, 2004
Alpha-dendrotoxin from green mamba Dendroaspis angusticeps and toxin I from the black mamba Dendroaspis polylepis block cloned Kv1.1, Kv1.2 and Kv1.6 channels in the low nanomolar range; toxin K, also from the black mamba Dendroaspis polylepis, preferentially blocks Kv1.1 channels and is active at picomolar concentrations.
Twenty years of dendrotoxins.
Harvey, Glasgow, United Kingdom. In Toxicon, 2001
Studies with cloned K(+) channels indicate that alpha-dendrotoxin from green mamba Dendroaspis angusticeps blocks Kv1.1, Kv1.2 and Kv1.6 channels in the nanomolar range, whereas toxin K from the black mamba Dendroaspis polylepis preferentially blocks Kv1.1 channels.
NIP domain prevents N-type inactivation in voltage-gated potassium channels.
Pongs et al., Hamburg, Germany. In Nature, 1998
These heteromultimers mediate non-inactivating currents because of the dominant-negative activity of a new type of N-type inactivation-prevention (NIP) domain present in the Kv1.6 amino terminus.
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