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    KCNT2 potassium sodium-activated channel subfamily T member 2 [ Homo sapiens (human) ]

    Gene ID: 343450, updated on 2-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    KCNT2-Related Disorders: Phenotypes, Functional, and Pharmacological Properties.

    KCNT2-Related Disorders: Phenotypes, Functional, and Pharmacological Properties.
    Cioclu MC, Mosca I, Ambrosino P, Puzo D, Bayat A, Wortmann SB, Koch J, Strehlow V, Shirai K, Matsumoto N, Sanders SJ, Michaud V, Legendre M, Riva A, Striano P, Muhle H, Pendziwiat M, Lesca G, Mangano GD, Nardello R, KCNT2-study group, Lemke JR, Møller RS, Soldovieri MV, Rubboli G, Taglialatela M.

    07/28/2023
    Recurrent KCNT2 missense variants affecting p.Arg190 result in a recognizable phenotype.

    Recurrent KCNT2 missense variants affecting p.Arg190 result in a recognizable phenotype.
    Jackson A, Banka S, Stewart H, Genomics England Research Consortium, Robinson H, Lovell S, Clayton-Smith J.

    01/22/2022
    New mutations in KCNT2 gene causing early infantile epileptic encephalopathy type 57: Case study and literature review.

    New mutations in KCNT2 gene causing early infantile epileptic encephalopathy type 57: Case study and literature review.
    Alagoz M, Kherad N, Bozkurt S, Yuksel A.

    09/25/2021
    In silico and in vitro analysis of cation-activated potassium channels in human corneal endothelial cells.

    In silico and in vitro analysis of cation-activated potassium channels in human corneal endothelial cells.
    Amador-Muñoz D, Gutiérrez ÁM, Payán-Gómez C, Matheus LM.

    01/16/2021
    An inducible circular RNA circKcnt2 inhibits ILC3 activation to facilitate colitis resolution.

    An inducible circular RNA circKcnt2 inhibits ILC3 activation to facilitate colitis resolution.
    Liu B, Ye B, Zhu X, Yang L, Li H, Liu N, Zhu P, Lu T, He L, Tian Y, Fan Z., Free PMC Article

    09/12/2020
    The expression of three genes (STK26, KCNT2, CASP12) was correlated with the prognosis of skin cutaneous melanoma (SCM). STK26 and KCNT2 were significantly different between normal skin and SCM. These three hub genes have potential value as predictors for accurate diagnosis and prognosis of SCM in the future.

    Common Nevus and Skin Cutaneous Melanoma: Prognostic Genes Identified by Gene Co-Expression Network Analysis.
    Yang L, Xu Y, Yan Y, Luo P, Chen S, Zheng B, Yan W, Chen Y, Wang C., Free PMC Article

    03/21/2020
    Pathogenic Phe240Leu mutation in KCNT2 channel changes ion selectivity.

    A De Novo Mutation in the Sodium-Activated Potassium Channel KCNT2 Alters Ion Selectivity and Causes Epileptic Encephalopathy.
    Gururaj S, Palmer EE, Sheehan GD, Kandula T, Macintosh R, Ying K, Morris P, Tao J, Dias KR, Zhu Y, Dinger ME, Cowley MJ, Kirk EP, Roscioli T, Sachdev R, Duffey ME, Bye A, Bhattacharjee A., Free PMC Article

    06/16/2018
    In the present study, we evaluated two other potential mechanisms for stabilization of Slo2 channels in a closed state: (1) dewetting and collapse of the inner pore (hydrophobic gating) and (2) constriction of the inner pore by tight criss-crossing of the cytoplasmic ends of the S6 alpha-helical segments.

    Molecular mechanisms of Slo2 K(+) channel closure.
    Giese MH, Gardner A, Hansen A, Sanguinetti MC., Free PMC Article

    09/23/2017
    mRNA of aquaporin 1 was co-expressed in Xenopus oocytes with homomeric or heteromeric Slick and Slack alpha-subunits. Hypotonic or hypertonic buffers caused changes in current. The heteromeric channel had a characteristic graded sensitivity to small and fast changes in cell volume. This the cell volume sensitivity is dependent on the number of volume sensitive Slick alpha-subunits in the tetrameric channels.

    Heteromeric Slick/Slack K+ channels show graded sensitivity to cell volume changes.
    Tejada MA, Hashem N, Calloe K, Klaerke DA., Free PMC Article

    08/26/2017
    KCNT2 SNPs were associated with lifetime cannabis use, but the association did not reach genome-wide significance. [Meta-Analysis]

    Genome-wide association study of lifetime cannabis use based on a large meta-analytic sample of 32 330 subjects from the International Cannabis Consortium.
    Stringer S, Minică CC, Verweij KJ, Mbarek H, Bernard M, Derringer J, van Eijk KR, Isen JD, Loukola A, Maciejewski DF, Mihailov E, van der Most PJ, Sánchez-Mora C, Roos L, Sherva R, Walters R, Ware JJ, Abdellaoui A, Bigdeli TB, Branje SJ, Brown SA, Bruinenberg M, Casas M, Esko T, Garcia-Martinez I, Gordon SD, Harris JM, Hartman CA, Henders AK, Heath AC, Hickie IB, Hickman M, Hopfer CJ, Hottenga JJ, Huizink AC, Irons DE, Kahn RS, Korhonen T, Kranzler HR, Krauter K, van Lier PA, Lubke GH, Madden PA, Mägi R, McGue MK, Medland SE, Meeus WH, Miller MB, Montgomery GW, Nivard MG, Nolte IM, Oldehinkel AJ, Pausova Z, Qaiser B, Quaye L, Ramos-Quiroga JA, Richarte V, Rose RJ, Shin J, Stallings MC, Stiby AI, Wall TL, Wright MJ, Koot HM, Paus T, Hewitt JK, Ribasés M, Kaprio J, Boks MP, Snieder H, Spector T, Munafò MR, Metspalu A, Gelernter J, Boomsma DI, Iacono WG, Martin NG, Gillespie NA, Derks EM, Vink JM., Free PMC Article

    02/18/2017
    Together these results suggest that hydrophobic interactions between residues in S5 and the C-terminal end of the pore helix stabilize Slo2.1 channels in a closed state.

    Hydrophobic interactions between the S5 segment and the pore helix stabilizes the closed state of Slo2.1 potassium channels.
    Suzuki T, Hansen A, Sanguinetti MC., Free PMC Article

    06/28/2016
    Charge reversal of Asp757 of Slo2.1 prevented activation of channels by intracellular Na+, whereas activation by niflumic acid was unaffected.

    Identification of the Intracellular Na+ Sensor in Slo2.1 Potassium Channels.
    Thomson SJ, Hansen A, Sanguinetti MC., Free PMC Article

    08/29/2015
    Slick channels, in contrast to the similar Slack channels, are the only high-conductance K+ channels strongly sensitive to small changes in cell volume.

    Cell volume changes regulate slick (Slo2.1), but not slack (Slo2.2) K+ channels.
    Tejada MA, Stople K, Hammami Bomholtz S, Meinild AK, Poulsen AN, Klaerke DA., Free PMC Article

    06/27/2015
    Together these findings suggest that (1) the selectivity filter and not the bundle crossing gates ion permeation and (2) dynamic coupling between the pore helix and the S5 and S6 segments mediates Slo2.1 channel activation.

    Structural basis of ion permeation gating in Slo2.1 K+ channels.
    Garg P, Gardner A, Garg V, Sanguinetti MC., Free PMC Article

    06/14/2014
    Cloning and regulation of slick channel activity.

    Slick (Slo2.1), a rapidly-gating sodium-activated potassium channel inhibited by ATP.
    Bhattacharjee A, Joiner WJ, Wu M, Yang Y, Sigworth FJ, Kaczmarek LK., Free PMC Article

    01/21/2010
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