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    Kcnb1 potassium voltage gated channel, Shab-related subfamily, member 1 [ Mus musculus (house mouse) ]

    Gene ID: 16500, updated on 27-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Integrin-KCNB1 potassium channel complexes regulate neocortical neuronal development and are implicated in epilepsy.

    Integrin-KCNB1 potassium channel complexes regulate neocortical neuronal development and are implicated in epilepsy.
    Bortolami A, Yu W, Forzisi E, Ercan K, Kadakia R, Murugan M, Fedele D, Estevez I, Boison D, Rasin MR, Sesti F., Free PMC Article

    03/13/2023
    Cdyl Deficiency Brakes Neuronal Excitability and Nociception through Promoting Kcnb1 Transcription in Peripheral Sensory Neurons.

    Cdyl Deficiency Brakes Neuronal Excitability and Nociception through Promoting Kcnb1 Transcription in Peripheral Sensory Neurons.
    Sun ZW, Waybright JM, Beldar S, Chen L, Foley CA, Norris-Drouin JL, Lyu TJ, Dong A, Min J, Wang YP, James LI, Wang Y., Free PMC Article

    04/16/2022
    Kv2.1 expression in giant reticular neurons of the postnatal mouse brain.

    Kv2.1 expression in giant reticular neurons of the postnatal mouse brain.
    Ding T, Magarinos AM, Kow LM, Milner TA, Pfaff DW., Free PMC Article

    03/5/2022
    Molecular, Cellular and Functional Changes in the Retinas of Young Adult Mice Lacking the Voltage-Gated K(+) Channel Subunits Kv8.2 and K2.1.

    Molecular, Cellular and Functional Changes in the Retinas of Young Adult Mice Lacking the Voltage-Gated K(+) Channel Subunits Kv8.2 and K2.1.
    Jiang X, Rashwan R, Voigt V, Nerbonne J, Hunt DM, Carvalho LS., Free PMC Article

    06/19/2021
    Site-specific contacts enable distinct modes of TRPV1 regulation by the potassium channel Kvbeta1 subunit.

    Site-specific contacts enable distinct modes of TRPV1 regulation by the potassium channel Kvβ1 subunit.
    Wang Y, Mo X, Ping C, Huang Q, Zhang H, Xie C, Zhong B, Li D, Yao J., Free PMC Article

    03/20/2021
    Kv2.1 plays a canonical conductive role but found it also has a structural role in arterial myocytes to enhance clustering of CaV1.2 channels.

    Kv2.1 channels play opposing roles in regulating membrane potential, Ca(2+) channel function, and myogenic tone in arterial smooth muscle.
    O'Dwyer SC, Palacio S, Matsumoto C, Guarina L, Klug NR, Tajada S, Rosati B, McKinnon D, Trimmer JS, Santana LF., Free PMC Article

    07/11/2020
    the VAP-interacting membrane-associated phosphatidylinositol (PtdIns) transfer proteins PYK2 N-terminal domain-interacting receptor 2 (Nir2) and Nir3 specifically associate with Kv2.1 complexes.

    Neuronal ER-plasma membrane junctions organized by Kv2-VAP pairing recruit Nir proteins and affect phosphoinositide homeostasis.
    Kirmiz M, Gillies TE, Dickson EJ, Trimmer JS., Free PMC Article

    06/13/2020
    results suggest that Kv2.1 clusters exert a spatially discrete homeostatic braking mechanism on dopamine transporter by inducing a relative increase in inward-facing transporters

    Clustered Kv2.1 decreases dopamine transporter activity and internalization.
    Lebowitz JJ, Pino JA, Mackie PM, Lin M, Hurst C, Divita K, Collins AT, Koutzoumis DN, Torres GE, Khoshbouei H., Free PMC Article

    01/11/2020
    Expression of Kv2.1 recruits VAPB and VAPA to ER-PM junctions. Knocking out VAPA expression disrupts Kv2.1 clustering.The domains of VAPs and Kv2.1 necessary and sufficient for their association at ER-PM junctions were identified. Kv2.1 expression in the plasma membrane can affect ER-PM junctions via its phosphorylation-dependent association to ER-localized VAPA and VAPB.

    Identification of VAPA and VAPB as Kv2 Channel-Interacting Proteins Defining Endoplasmic Reticulum-Plasma Membrane Junctions in Mammalian Brain Neurons.
    Kirmiz M, Vierra NC, Palacio S, Trimmer JS., Free PMC Article

    10/19/2019
    Kv8.2 knock-out (KO) mice show many similarities to human cone dystrophy with a supernormal rod response, including a depressed a-wave and an elevated b-wave response with bright light stimulation. Optical coherence tomography imaging and immunohistochemistry indicate that the changes in six-month-old Kv8.2 KO retinae are largely limited to the outer nuclear layer, while outer segments appear intact.

    The Role of the Voltage-Gated Potassium Channel Proteins Kv8.2 and Kv2.1 in Vision and Retinal Disease: Insights from the Study of Mouse Gene Knock-Out Mutations.
    Hart NS, Mountford JK, Voigt V, Fuller-Carter P, Barth M, Nerbonne JM, Hunt DM, Carvalho LS., Free PMC Article

    05/25/2019
    these findings demonstrate a conserved in vivo function for Kv2 family members in remodeling neuronal endoplasmic reticulum-plasma membrane junctions.

    Remodeling neuronal ER-PM junctions is a conserved nonconducting function of Kv2 plasma membrane ion channels.
    Kirmiz M, Palacio S, Thapa P, King AN, Sack JT, Trimmer JS., Free PMC Article

    05/11/2019
    The results of this study shown the disruption of KV2.1 somato-dendritic clusters prevents the apoptogenic increase of potassium currents.

    Disruption of K(V)2.1 somato-dendritic clusters prevents the apoptogenic increase of potassium currents.
    Justice JA, Schulien AJ, He K, Hartnett KA, Aizenman E, Shah NH., Free PMC Article

    03/17/2018
    KCNB1 oxidation may favor integrin clustering, thereby facilitating the recruitment and activation of FAK and Src/Fyn kinases.

    Oxidation of KCNB1 potassium channels triggers apoptotic integrin signaling in the brain.
    Yu W, Gowda M, Sharad Y, Singh SA, Sesti F., Free PMC Article

    11/25/2017
    Spinal Musculature Atrophy motor neurons showed a lower surface expression of Kv2.1 potassium channels and reduced spiking ability.

    Reduced sensory synaptic excitation impairs motor neuron function via Kv2.1 in spinal muscular atrophy.
    Fletcher EV, Simon CM, Pagiazitis JG, Chalif JI, Vukojicic A, Drobac E, Wang X, Mentis GZ., Free PMC Article

    09/2/2017
    This study provides the first experimental evidence that oxidation of a K(+) channel constitutes a mechanism of neuronal and cognitive impairment in vertebrates. Specifically, the interaction of KCNB1 channels with reactive oxygen species plays a major role in the etiology of mouse model of traumatic brain injury (TBI), a condition associated with extensive oxidative stress. In addition, a Food and Drug Administration-app

    Oxidation of KCNB1 Potassium Channels Causes Neurotoxicity and Cognitive Impairment in a Mouse Model of Traumatic Brain Injury.
    Yu W, Parakramaweera R, Teng S, Gowda M, Sharad Y, Thakker-Varia S, Alder J, Sesti F., Free PMC Article

    07/15/2017
    The AMIGO1-KCNB1 complex is involved in schizophrenia-related behavioral domains in mice.

    AMIGO-Kv2.1 Potassium Channel Complex Is Associated With Schizophrenia-Related Phenotypes.
    Peltola MA, Kuja-Panula J, Liuhanen J, Võikar V, Piepponen P, Hiekkalinna T, Taira T, Lauri SE, Suvisaari J, Kulesskaya N, Paunio T, Rauvala H., Free PMC Article

    09/24/2016
    major finding from this study is the novel region- and cell-specific relationship between the localization of the plasma membrane Kv2.1 channel and intracellular RyR Ca2+ release channels

    Cell type-specific spatial and functional coupling between mammalian brain Kv2.1 K+ channels and ryanodine receptors.
    Mandikian D, Bocksteins E, Parajuli LK, Bishop HI, Cerda O, Shigemoto R, Trimmer JS., Free PMC Article

    11/7/2015
    study supports the concept that transcriptional suppression of KV2.1 by activation of the AKAP150-CaN/NFATc3 signaling axis contributes to enhanced arterial tone during diabetes

    Selective down-regulation of KV2.1 function contributes to enhanced arterial tone during diabetes.
    Nieves-Cintrón M, Nystoriak MA, Prada MP, Johnson K, Fayer W, Dell'Acqua ML, Scott JD, Navedo MF., Free PMC Article

    07/4/2015
    High temperature sensitivity is intrinsic to voltage-gated potassium channels.

    High temperature sensitivity is intrinsic to voltage-gated potassium channels.
    Yang F, Zheng J., Free PMC Article

    05/16/2015
    These results showed that a modest suppression of Kv2.1 channels dramatically raises insulinotropic potency of GLP-1-based drugs.

    Partial blockade of Kv2.1 channel potentiates GLP-1's insulinotropic effects in islets and reduces its dose required for improving glucose tolerance in type 2 diabetic male mice.
    Sukma Rita R, Dezaki K, Kurashina T, Kakei M, Yada T.

    03/21/2015
    Kv2.1 knockout mice are strikingly hyperactive, defective in spatial learning and hypersensitive to convulsants.

    Deletion of the Kv2.1 delayed rectifier potassium channel leads to neuronal and behavioral hyperexcitability.
    Speca DJ, Ogata G, Mandikian D, Bishop HI, Wiler SW, Eum K, Wenzel HJ, Doisy ET, Matt L, Campi KL, Golub MS, Nerbonne JM, Hell JW, Trainor BC, Sack JT, Schwartzkroin PA, Trimmer JS., Free PMC Article

    01/3/2015
    the accumulation of KCNB1 oligomers in the membrane disrupts planar lipid raft integrity and causes apoptosis via activating the c-Src/JNK signaling pathway.

    Molecular mechanisms underlying the apoptotic effect of KCNB1 K+ channel oxidation.
    Wu X, Hernandez-Enriquez B, Banas M, Xu R, Sesti F., Free PMC Article

    04/20/2013
    Kv2.1 regulates insulin secretion in beta-cells

    The role of voltage-gated potassium channels Kv2.1 and Kv2.2 in the regulation of insulin and somatostatin release from pancreatic islets.
    Li XN, Herrington J, Petrov A, Ge L, Eiermann G, Xiong Y, Jensen MV, Hohmeier HE, Newgard CB, Garcia ML, Wagner M, Zhang BB, Thornberry NA, Howard AD, Kaczorowski GJ, Zhou YP.

    03/30/2013
    Direct interaction between syntaxin 1A and the Kv2.1 C-terminus is required for efficient insulin exocytosis and glucose-stimulated insulin secretion.

    The voltage-dependent potassium channel subunit Kv2.1 regulates insulin secretion from rodent and human islets independently of its electrical function.
    Dai XQ, Manning Fox JE, Chikvashvili D, Casimir M, Plummer G, Hajmrle C, Spigelman AF, Kin T, Singer-Lahat D, Kang Y, Shapiro AM, Gaisano HY, Lotan I, Macdonald PE.

    09/1/2012
    stromatoxin-1 -sensitive KV2-containing channels are expressed in detrusor smooth muscle (DSM); they control DSM excitability, intracellular Ca2+ levels, and myogenic and nerve-evoked contractions

    Expression and function of K(V)2-containing channels in human urinary bladder smooth muscle.
    Hristov KL, Chen M, Afeli SA, Cheng Q, Rovner ES, Petkov GV., Free PMC Article

    08/11/2012
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