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    Kpna2 karyopherin subunit alpha 2 [ Mus musculus (house mouse) ]

    Gene ID: 16647, updated on 14-Oct-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Karyopherin alpha2 is a maternal effect gene required for early embryonic development and female fertility in mice.

    Karyopherin α2 is a maternal effect gene required for early embryonic development and female fertility in mice.
    Rother F, Depping R, Popova E, Huegel S, Heiler A, Hartmann E, Bader M.

    04/26/2024
    Nuclear ERK1/2 signaling potentiation enhances neuroprotection and cognition via Importinalpha1/KPNA2.

    Nuclear ERK1/2 signaling potentiation enhances neuroprotection and cognition via Importinα1/KPNA2.
    Indrigo M, Morella I, Orellana D, d'Isa R, Papale A, Parra R, Gurgone A, Lecca D, Cavaccini A, Tigaret CM, Cagnotto A, Jones K, Brooks S, Ratto GM, Allen ND, Lelos MJ, Middei S, Giustetto M, Carta AR, Tonini R, Salmona M, Hall J, Thomas K, Brambilla R, Fasano S., Free PMC Article

    11/14/2023
    KPNA2 promotes angiogenesis by regulating STAT3 phosphorylation.

    KPNA2 promotes angiogenesis by regulating STAT3 phosphorylation.
    Jia Y, Wang Q, Liang M, Huang K., Free PMC Article

    01/11/2023
    Importin alpha2 association with chromatin: Direct DNA binding via a novel DNA-binding domain.

    Importin α2 association with chromatin: Direct DNA binding via a novel DNA-binding domain.
    Jibiki K, Kodama TS, Suenaga A, Kawase Y, Shibazaki N, Nomoto S, Nagasawa S, Nagashima M, Shimodan S, Kikuchi R, Okayasu M, Takashita R, Mehmood R, Saitoh N, Yoneda Y, Akagi KI, Yasuhara N.

    01/22/2022
    USP22 promotes IRF3 nuclear translocation and antiviral responses by deubiquitinating the importin protein KPNA2.

    USP22 promotes IRF3 nuclear translocation and antiviral responses by deubiquitinating the importin protein KPNA2.
    Cai Z, Zhang MX, Tang Z, Zhang Q, Ye J, Xiong TC, Zhang ZD, Zhong B., Free PMC Article

    12/26/2020
    NLRP3 interacted with Kpna2 and translocated to the nucleus from the cytoplasm under regulatory T cells-polarizing conditions.

    NLRP3 negatively regulates Treg differentiation through Kpna2-mediated nuclear translocation.
    Park SH, Ham S, Lee A, Möller A, Kim TS., Free PMC Article

    06/13/2020
    upregulation of KPNA2 seemed to be correlated with progression of the degree of atypia in pancreatic ductal cells in aged diabetic C414A-mutant-CRY1 transgenic mice

    Karyopherin Alpha 2-Expressing Pancreatic Duct Glands and Intra-Islet Ducts in Aged Diabetic C414A-Mutant-CRY1 Transgenic Mice.
    Okano S, Yasui A, Kanno SI, Satoh K, Igarashi M, Nakajima O., Free PMC Article

    01/18/2020
    Results demonstrated that radiation-induced dying colorectal cancer cells released considerable amounts of KPNA2 that induce the maturation and activation of DCs for synergistic antitumor effect of radiation.

    Induction of immunogenic cell death by radiation-upregulated karyopherin alpha 2 in vitro.
    Song KH, Jung SY, Kang SM, Kim MH, Ahn J, Hwang SG, Lee JH, Lim DS, Nam SY, Song JY.

    02/18/2017
    mTORC1 positively regulated the importer protein KPNA2, which participated in glycolysis regulation downstream of mTORC1 in a HIF1alpha-independent manner, indicating that mTORC1 regulates glycolysis through multiple ways.

    mTORC1 alters the expression of glycolytic genes by regulating KPNA2 abundances.
    Chen X, Zhu Y, Wang Z, Zhu H, Pan Q, Su S, Dong Y, Li L, Zhang H, Wu L, Lou X, Liu S.

    12/17/2016
    provided support for a link between autophagy and epithelial-to-mesenchymal (-like) transition status in WT TP53 glioblastoma cells and provided evidence for the signaling pathway (MIR517C-KPNA2-cytoplasmic TP53) involved in attenuating autophagy

    MIR517C inhibits autophagy and the epithelial-to-mesenchymal (-like) transition phenotype in human glioblastoma through KPNA2-dependent disruption of TP53 nuclear translocation.
    Lu Y, Xiao L, Liu Y, Wang H, Li H, Zhou Q, Pan J, Lei B, Huang A, Qi S., Free PMC Article

    11/5/2016
    Structure of importin-alpha bound to a non-classical nuclear localization signal of the influenza A virus nucleoprotein has been reported.

    Structure of importin-α bound to a non-classical nuclear localization signal of the influenza A virus nucleoprotein.
    Nakada R, Hirano H, Matsuura Y., Free PMC Article

    08/27/2016
    Specific interaction with the nuclear transporter importin alpha2 can modulate paraspeckle protein 1 delivery to nuclear paraspeckles.

    Specific interaction with the nuclear transporter importin α2 can modulate paraspeckle protein 1 delivery to nuclear paraspeckles.
    Major AT, Hogarth CA, Miyamoto Y, Sarraj MA, Smith CL, Koopman P, Kurihara Y, Jans DA, Loveland KL., Free PMC Article

    02/6/2016
    constitutive expression of Kpna2 during the differentiation culture of ESCs significantly impairs clock development, and KPNA2 facilitates cytoplasmic localization of PER1/

    Transcriptional program of Kpna2/Importin-α2 regulates cellular differentiation-coupled circadian clock development in mammalian cells.
    Umemura Y, Koike N, Matsumoto T, Yoo SH, Chen Z, Yasuhara N, Takahashi JS, Yagita K., Free PMC Article

    04/25/2015
    a significant correlation of KPNA2 expression and tumour aggressiveness in a large variety of other solid tumour entities

    KPNA2 is overexpressed in human and mouse endometrial cancers and promotes cellular proliferation.
    Ikenberg K, Valtcheva N, Brandt S, Zhong Q, Wong CE, Noske A, Rechsteiner M, Rueschoff JH, Caduff R, Dellas A, Obermann E, Fink D, Fuchs T, Krek W, Moch H, Frew IJ, Wild PJ.

    11/22/2014
    study reports a cell-fate determination mechanism in which importin alpha2 negatively regulates the nuclear import of certain transcription factors to maintain embryonic stem cell properties

    Importin alpha subtypes determine differential transcription factor localization in embryonic stem cells maintenance.
    Yasuhara N, Yamagishi R, Arai Y, Mehmood R, Kimoto C, Fujita T, Touma K, Kaneko A, Kamikawa Y, Moriyama T, Yanagida T, Kaneko H, Yoneda Y.

    11/2/2013
    importin alpha binds to Nup153

    The interaction between importin-α and Nup153 promotes importin-α/β-mediated nuclear import.
    Ogawa Y, Miyamoto Y, Oka M, Yoneda Y.

    10/6/2012
    results collectively reveal that nuclear-localized importin alpha2 influences gene expression and contributes directly to cell fate outcomes including non-apoptotic cell death.

    Nuclear retention of importin α coordinates cell fate through changes in gene expression.
    Yasuda Y, Miyamoto Y, Yamashiro T, Asally M, Masui A, Wong C, Loveland KL, Yoneda Y., Free PMC Article

    04/28/2012
    Chrp, Arip3, and Hop2 are binding partners of IMPalpha2 in the developmental context of germ line development.

    Importin alpha2-interacting proteins with nuclear roles during mammalian spermatogenesis.
    Ly-Huynh JD, Lieu KG, Major AT, Whiley PA, Holt JE, Loveland KL, Jans DA.

    04/14/2012
    Overexpression of a dominant-negative IMPalpha2 isoform, when assessed against adjacent untransfected or IMPalpha2 transfected cells, led to both a significant reduction in endogenous Oct3/4 protein levels and inhibition of Oct3/4 nuclear localization.

    Distinct effects of importin α2 and α4 on Oct3/4 localization and expression in mouse embryonic stem cells.
    Young JC, Major AT, Miyamoto Y, Loveland KL, Jans DA.

    12/31/2011
    knockdown of KPNA2 decreased myotube growth.

    Distinct roles for classical nuclear import receptors in the growth of multinucleated muscle cells.
    Hall MN, Griffin CA, Simionescu A, Corbett AH, Pavlath GK., Free PMC Article

    11/5/2011
    The results suggest that Klf2 and Klf4 function redundantly to drive high level of Kpna2 expression in ES cells.

    Cell type-specific transcriptional regulation of the gene encoding importin-α1.
    Kamikawa Y, Yasuhara N, Yoneda Y.

    09/24/2011
    Data show that MRTF-A contains an unusually long bipartite nuclear localisation signal embedded within the RPEL domain, that uses the importin (Imp)alpha/beta-dependent import pathway, and that import is inhibited by G-actin.

    An actin-regulated importin α/β-dependent extended bipartite NLS directs nuclear import of MRTF-A.
    Pawłowski R, Rajakylä EK, Vartiainen MK, Treisman R., Free PMC Article

    11/27/2010
    Study identified the sequences KKKRR, KKKRK, and KKRKK as the optimal sequences for binding to this site for mouse importin-alpha2, human importin-alpha1, and human importin-alpha5, respectively.

    Probing the specificity of binding to the major nuclear localization sequence-binding site of importin-alpha using oriented peptide library screening.
    Yang SN, Takeda AA, Fontes MR, Harris JM, Jans DA, Kobe B., Free PMC Article

    08/30/2010
    Karyopherin alpha2: a control step of glucose-sensitive gene expression in hepatic cells

    Karyopherin alpha2: a control step of glucose-sensitive gene expression in hepatic cells.
    Guillemain G, Muñoz-Alonso MJ, Cassany A, Loizeau M, Faussat AM, Burnol AF, Leturque A., Free PMC Article

    01/21/2010
    Results suggest that the importin alpha/beta system is involved in nuclear entry of mammalian clock components Cry2 and Per2, which is indispensable to transcriptional oscillation of clock genes

    Importin alpha/beta mediates nuclear transport of a mammalian circadian clock component, mCRY2, together with mPER2, through a bipartite nuclear localization signal.
    Sakakida Y, Miyamoto Y, Nagoshi E, Akashi M, Nakamura TJ, Mamine T, Kasahara M, Minami Y, Yoneda Y, Takumi T.

    01/21/2010
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