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Potassium channel, subfamily K, member 1

This gene encodes one of the members of the superfamily of potassium channel proteins containing two pore-forming P domains. The product of this gene has not been shown to be a functional channel, however, it may require other non-pore-forming proteins for activity. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: TREK-1, ACID, K2P, TWIK-2, TASK-2
Papers on TWIK-1
mGluR3 Activation Recruits Cytoplasmic TWIK-1 Channels to Membrane that Enhances Ammonium Uptake in Hippocampal Astrocytes.
Zhou et al., Columbus, United States. In Mol Neurobiol, Dec 2015
UNASSIGNED: TWIK-1 two-pore domain K(+) channels are highly expressed in mature hippocampal astrocytes.
A genome-wide analysis of the response to inhaled β2-agonists in chronic obstructive pulmonary disease.
COPDGene Investigators-clinical centers et al., Boston, United States. In Pharmacogenomics J, Nov 2015
In the meta-analysis, single-nucleotide polymorphisms (SNPs) in the genes KCNK1 (P=2.02 × 10(-7)) and KCNJ2 (P=1.79 × 10(-7)) were the top associations with BDR.
Role of leak potassium channels in pain signaling.
Toyoda et al., China. In Brain Res Bull, Oct 2015
Furthermore, we describe the possible involvement of TASK2 and TWIK1 channels in pain.
KCNK1 inhibits osteoclastogenesis by blocking the Ca2+ oscillation and JNK-NFATc1 signaling axis.
Choi et al., Sunch'ŏn, South Korea. In J Cell Sci, Oct 2015
KCNK1 (K(+) channel, subfamily K, member 1) is a member of the inwardly rectifying K(+) channel family, which drives the membrane potential towards the K(+) balance potential.
The family of K2P channels: salient structural and functional properties.
Lesage et al., Antibes, France. In J Physiol, Jul 2015
Since the cloning of TWIK1, the prototypical member of this family, a lot of work has been carried out on their structure and biology.
Two-pore domain potassium channels: potential therapeutic targets for the treatment of pain.
Veale et al., Chatham, United Kingdom. In Pflugers Arch, May 2015
Expression of several different K2P channel subunits has been detected in nociceptive dorsal root ganglion neurons and trigeminal ganglion neurons, in particular, TREK1, TREK2, TRESK, TRAAK, TASK3 and TWIK1 channels.
The role of acid-sensitive two-pore domain potassium channels in cardiac electrophysiology: focus on arrhythmias.
Rinné et al., Marburg an der Lahn, Germany. In Pflugers Arch, May 2015
The role of TWIK-1 in the heart is also discussed since, after successful expression, an extracellular pH dependence, similar to that of TASK-1, was described as a hallmark of TWIK-1.
Silent but not dumb: how cellular trafficking and pore gating modulate expression of TWIK1 and THIK2.
Lesage et al., Antibes, France. In Pflugers Arch, May 2015
For TWIK1 and THIK2 channels, silence is related to a combination of intracellular retention and low intrinsic activity.
Molecular simulation studies of hydrophobic gating in nanopores and ion channels.
Sansom et al., Oxford, United Kingdom. In Biochem Soc Trans, Apr 2015
Simulations of both the nicotinic acetylcholine receptor and of TWIK-1 potassium channels (the latter alongside experimental studies) suggest hydrophobic gating may occur in some biological ion channels.
Influence of lipids on the hydrophobic barrier within the pore of the TWIK-1 K2P channel.
Tucker et al., Oxford, United Kingdom. In Channels (austin), 2014
In a recent study we demonstrated that functional activity of the TWIK-1 K2P channel is influenced by the presence of hydrophobic residues deep within the inner pore.
Differential expression of two-pore domain potassium channels in rat cerebellar granule neurons.
Zúñiga et al., Talca, Chile. In Biochem Biophys Res Commun, 2014
The presence of the major K2P subunits expressed was then confirmed by Western blot and immunofluorescence analysis, demonstrating robust expression of K2P1 (TWIK-1), K2P3 (TASK-1), K2P9 (TASK-3) and K2P18 (TRESK) channel protein.
Chronic periodontitis genome-wide association studies: gene-centric and gene set enrichment analyses.
Offenbacher et al., Chapel Hill, United States. In J Dent Res, 2014
Six genes showed evidence of statistically significant association: 4 with severe CP (NIN, p = 1.6 × 10(-7); ABHD12B, p = 3.6 × 10(-7); WHAMM, p = 1.7 × 10(-6); AP3B2, p = 2.2 × 10(-6)) and 2 with high periodontal pathogen colonization (red complex-KCNK1, p = 3.4 × 10(-7); Porphyromonas gingivalis-DAB2IP, p = 1.0 × 10(-6)).
TWIK-1 contributes to the intrinsic excitability of dentate granule cells in mouse hippocampus.
Park et al., Seoul, South Korea. In Mol Brain, 2013
However, physiological function of TWIK-1, the first identified member of the mammalian K2P channel family, in neuronal cells is largely unknown.
Crystal structure of the human two-pore domain potassium channel K2P1.
Long et al., New York City, United States. In Science, 2012
study presents the 3.4 angstrom resolution crystal structure of a human K2P channel, K2P1; an extracellular cap domain located above the selectivity filter forms an ion pathway in which K(+) ions flow through side portals
A role for two-pore K⁺ channels in modulating Na⁺ absorption and Cl⁻ secretion in normal human bronchial epithelial cells.
Kreindler et al., Shanghai, China. In Am J Physiol Lung Cell Mol Physiol, 2012
Potassium channels, in particular K2P channels, are expressed and functional in the apical membrane of airway epithelial cells
TWIK-1 two-pore domain potassium channels change ion selectivity and conduct inward leak sodium currents in hypokalemia.
Chen et al., Albany, United States. In Sci Signal, 2010
ion selectivity of TWIK-1 K+ channels during pathological hypokalemia; a molecular basis for inward leak Na+ currents that could trigger or contribute to cardiac paradoxical depolarization in lowered [K+]o; mechanism for regulating cardiac excitability.
Potassium channel silencing by constitutive endocytosis and intracellular sequestration.
Lesage et al., Antibes, France. In J Biol Chem, 2010
TWIK1 is internalized via a dynamin-dependent mechanism and addressed to the recycling endosomal compartment. Mutation in its cytoplasmic C terminus (I293A,I294A) stabilizes TWIK1 at the plasma membrane, resulting in robust currents.
TWIK-1 and TREK-1 are potassium channels contributing significantly to astrocyte passive conductance in rat hippocampal slices.
Chen et al., Albany, United States. In J Neurosci, 2009
support TWIK-1 and TREK-1 as being the major components of the long-sought K(+) channels underlying the passive conductance of mature hippocampal astrocytes
Does sumoylation control K2P1/TWIK1 background K+ channels?
Lesage et al., France. In Cell, 2007
It originates from the observation that the background K(+) channel K2P1 (TWIK1) may be silenced by sumoylation in Xenopus oocytes and that inactivation of the putative sumoylation site (mutation K274E) gives rise to robust current expression in transfected COS-7 cells.
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