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Potassium voltage-gated channel, shaker-related subfamily, member 5

Potassium Channel, Kv1.5
Potassium channels represent the most complex class of voltage-gated ino 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, shaker-related subfamily. This member contains six membrane-spanning domains with a shaker-type repeat in the fourth segment. It belongs to the delayed rectifier class, the function of which could restore the resting membrane potential of beta cells after depolarization and thereby contribute to the regulation of insulin secretion. This gene is intronless, and the gene is clustered with genes KCNA1 and KCNA6 on chromosome 12. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, V1a, HAD, KCNQ2, HERG
Papers on Potassium Channel
Environment-Sensitive Fluorescent Probe for the Human Ether-a-go-go-Related Gene Potassium Channel.
New
Li et al., Jinan, China. In Anal Chem, Feb 2016
UNASSIGNED: A novel environment-sensitive probe S2 with turn-on switch for Human Ether-a-go-go-Related Gene (hERG) potassium channel was developed herein.
The Molecular Basis of Polyunsaturated Fatty Acid Interactions with the Shaker Voltage-Gated Potassium Channel.
New
Lindahl et al., Magdeburg, Germany. In Plos Comput Biol, Jan 2016
Voltage-gated potassium (KV) channels are membrane proteins that respond to changes in membrane potential by enabling K+ ion flux across the membrane.
Kv7.5 Potassium Channel Subunits are the Primary Targets for PKA-Dependent Enhancement of Vascular Smooth Muscle Kv7 Currents.
New
Byron et al., Chicago, United States. In Mol Pharmacol, Jan 2016
UNASSIGNED: Kv7 (KCNQ) channels, formed as homo- or hetero-tetramers of Kv7.4 and Kv7.5 α-subunits, are important regulators of vascular smooth muscle cell (VSMC) membrane voltage.
Slack Sodium-activated Potassium Channel Membrane Expression Requires p38 Mitogen-Activated Protein Kinase Phosphorylation.
New
Bhattacharjee et al., Buffalo, United States. In Neuropharmacology, Jan 2016
UNASSIGNED: p38 MAPK has long been understood as an inducible kinase under conditions of cellular stress, but there is now increasing evidence to support its role in the regulation of neuronal function.
Perspectives on the Two-Pore Domain Potassium Channel TREK-1 (TWIK-Related K(+) Channel 1). A Novel Therapeutic Target?
New
Ducki et al., Clermont-Ferrand, France. In J Med Chem, Jan 2016
UNASSIGNED: Potassium (K(+)) channels are membrane proteins expressed in most living cells that selectively control the flow of K(+) ions.
Structural Dynamics of the Potassium Channel Blocker ShK: SRLS Analysis of (15)N Relaxation.
New
Chill et al., Ramat Gan, Israel. In J Phys Chem B, Jan 2016
The 35-residue ShK peptide binds with high affinity to voltage-gated potassium channels.
Opening of Adenosine Triphosphate-Sensitive Potassium Channel Attenuates Morphine Tolerance by Inhibiting JNK and Astrocyte Activation in the Spinal Cord.
New
Liu et al., Nanjing, China. In Clin J Pain, Dec 2015
OBJECTIVES: In the present study we investigated the role of adenosine triphosphate (ATP)-sensitive potassium (KATP) channel in chronic morphine tolerance.
Lower KV7.5 Potassium Channel Subunit Expression in an Animal Model of Paroxysmal Dystonia.
New
Richter et al., Berlin, Germany. In Cns Neurol Disord Drug Targets, Dec 2015
In the dtsz hamster, a model of paroxysmal dystonia, pronounced antidystonic effects of the KV7.2-5 potassium channel opener retigabine and aggravation of dystonia by a selective KV7.2-5 blocker indicated a pathophysiological role of an abnormal expression of KV7 channels.
Modulation of Potassium Channel Activity in the Balance of ROS and ATP Production by Durum Wheat Mitochondria-An Amazing Defense Tool Against Hyperosmotic Stress.
Review
Pastore et al., Foggia, Italy. In Front Plant Sci, 2014
In plants, the existence of a mitochondrial potassium channel was firstly demonstrated about 15 years ago in durum wheat as an ATP-dependent potassium channel (PmitoKATP).
Correction: Ocular Hypotensive Effects of the ATP-Sensitive Potassium Channel Opener Cromakalim in Human and Murine Experimental Model Systems.
Fautsch et al., In Plos One, 2014
UNASSIGNED: [This corrects the article DOI: 10.1371/journal.pone.0141783.].
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
Cardiac potassium channel subtypes: new roles in repolarization and arrhythmia.
Review
Impact
Olesen et al., In Physiol Rev, 2014
Three main K+ channels drive the late repolarization of the ventricle with some redundancy, and in atria this repolarization reserve is supplemented by the fairly atrial-specific KV1.5, Kir3, KCa, and K2P channels.
Minireview: potassium channels and aldosterone dysregulation: is primary aldosteronism a potassium channelopathy?
Review
Oki et al., Hiroshima, Japan. In Endocrinology, 2014
Under basal conditions, the adrenal zona glomerulosa cells are hyperpolarized with negative resting potentials determined by membrane permeability to K(+) mediated through various K(+) channels, including the leak K(+) channels TASK-1, TASK-3, and Twik-Related Potassium Channel 1, and G protein inward rectifying potassium channel Kir3.4.
ML365: Development of Bis-Amides as Selective Inhibitors of the KCNK3/TASK1 Two Pore Potassium Channel
Review
Li et al., Bethesda, United States. In Unknown Journal, 2013
ML365 was identified as a novel selective small molecule inhibitor of the TASK1 or potassium channel, subfamily K, member 9 (KCNK3) two-pore domain potassium channel following a high throughput fluorescent screen of the Molecular Libraries Small Molecule Repository (MLSMR) library and structure activity relationship (SAR) analysis of active compounds.
Protein kinase C (PKC) activity regulates functional effects of Kvβ1.3 subunit on KV1.5 channels: identification of a cardiac Kv1.5 channelosome.
GeneRIF
Valenzuela et al., Madrid, Spain. In J Biol Chem, 2012
and immunocytochemistry experiments revealed an association between K(v)1.5, K(v)beta1.3, the receptor for activated C kinase (RACK1), PKCbetaI, PKCbetaII, and PKCtheta.
Differential expression of Kv1.3 and Kv1.5 voltage-dependent K+ channels in human skeletal muscle sarcomas.
GeneRIF
Felipe et al., Barcelona, Spain. In Cancer Invest, 2012
expression of Kv1.5 and Kv1.3 increased in skeletal muscle tumorigenesis in a close relationship with malignancy.
Activation of voltage gated K⁺ channel Kv1.5 by β-catenin.
GeneRIF
Lang et al., Tübingen, Germany. In Biochem Biophys Res Commun, 2012
The experiments disclose a completely novel function of beta-catenin, i.e. the regulation of Kv1.5 channel activity.
Multistep ion channel remodeling and lethal arrhythmia precede heart failure in a mouse model of inherited dilated cardiomyopathy.
GeneRIF
Kurebayashi et al., Tokyo, Japan. In Plos One, 2011
The combined down-regulation of Kv4.2, Kv1.5 and KChIP2 prior to the onset of HF may play an important role in the premature sudden death in this DCM model.
Four and a half LIM protein 1C (FHL1C): a binding partner for voltage-gated potassium channel K(v1.5).
GeneRIF
Malle et al., Graz, Austria. In Plos One, 2010
In order to substantiate a possible relation between K(v1.5) and FHL1C, a pull-down assay was performed.
De novo Folding of Two-Helix Potassium Channel Blockers with Free-Energy Models and Molecular Dynamics.
Wenzel et al., Karlsruhe, Germany. In J Chem Theory Comput, 2007
We report the predictive de novo folding of three two-helix proteins using the free-energy protein forcefield PFF01.
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