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    NXF1 nuclear RNA export factor 1 [ Homo sapiens (human) ]

    Gene ID: 10482, updated on 27-Aug-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Association between TAP gene polymorphisms and tuberculosis susceptibility in a Han Chinese population in Guangdong.

    Association between TAP gene polymorphisms and tuberculosis susceptibility in a Han Chinese population in Guangdong.
    Luo F, Zou P, Liao Y, Luo J, Luo D, Hu K, Zhang K, Wang B., Free PMC Article

    06/11/2022
    The Ebola Virus Nucleoprotein Recruits the Nuclear RNA Export Factor NXF1 into Inclusion Bodies to Facilitate Viral Protein Expression.

    The Ebola Virus Nucleoprotein Recruits the Nuclear RNA Export Factor NXF1 into Inclusion Bodies to Facilitate Viral Protein Expression.
    Wendt L, Brandt J, Bodmer BS, Reiche S, Schmidt ML, Traeger S, Hoenen T., Free PMC Article

    03/13/2021
    Using iCLIP, we show that the export receptor Nxf1 and two TREX subunits, Alyref and Chtop, are recruited to the whole mRNA co-transcriptionally via splicing but before 3' end processing.

    Co-transcriptional Loading of RNA Export Factors Shapes the Human Transcriptome.
    Viphakone N, Sudbery I, Griffith L, Heath CG, Sims D, Wilson SA., Free PMC Article

    01/25/2020
    NXF1 is involved in coordinating transcriptional dynamics, 3' end processing, and nuclear export of long 3' UTR transcripts, implicating NXF1 as a nexus of gene regulation.

    The mRNA Export Receptor NXF1 Coordinates Transcriptional Dynamics, Alternative Polyadenylation, and mRNA Export.
    Chen S, Wang R, Zheng D, Zhang H, Chang X, Wang K, Li W, Fan J, Tian B, Cheng H., Free PMC Article

    07/20/2019
    Gain or loss-of-function experiments revealed NXF1 selectively regulates TLR7-driven IRF5 transcriptional activity, suggesting a new role for NXF1 in the IRF5 signaling pathway.

    RNAi Screen and Proteomics Reveal NXF1 as a Novel Regulator of IRF5 Signaling.
    Fu B, Zhao M, Wang L, Patil G, Smith JA, Juncadella IJ, Zuvela-Jelaska L, Dorf ME, Li S., Free PMC Article

    12/22/2018
    repeat RNA-sequestration of SRSF1 triggers the NXF1-dependent nuclear export of C9ORF72 transcripts retaining expanded hexanucleotide repeats

    SRSF1-dependent nuclear export inhibition of C9ORF72 repeat transcripts prevents neurodegeneration and associated motor deficits.
    Hautbergue GM, Castelli LM, Ferraiuolo L, Sanchez-Martinez A, Cooper-Knock J, Higginbottom A, Lin YH, Bauer CS, Dodd JE, Myszczynska MA, Alam SM, Garneret P, Chandran JS, Karyka E, Stopford MJ, Smith EF, Kirby J, Meyer K, Kaspar BK, Isaacs AM, El-Khamisy SF, De Vos KJ, Ning K, Azzouz M, Whitworth AJ, Shaw PJ., Free PMC Article

    12/22/2018
    small hairpin RNA-mediated down-regulation of TAP or Aly reduced nuclear export of HDAg-L and assembly of HDV virions. Furthermore, a peptide, TAT-HDAg-L(198-210), containing the 10-amino acid TAT peptide and HDAg-L(198-210), inhibited the interaction between HDAg-L and TAP and blocked HDV virion assembly and secretion.

    Cellular Nuclear Export Factors TAP and Aly Are Required for HDAg-L-mediated Assembly of Hepatitis Delta Virus.
    Huang HC, Lee CP, Liu HK, Chang MF, Lai YH, Lee YC, Huang C., Free PMC Article

    05/27/2017
    Hepatitis B virus core protein associates with the cellular NXF1-p15 complex via the nuclear export signal motif of hepatitis B virus core protein.Nuclear export of human hepatitis B virus core protein and pregenomic RNA depends on the NXF1-p15 machinery.

    Nuclear export of human hepatitis B virus core protein and pregenomic RNA depends on the cellular NXF1-p15 machinery.
    Yang CC, Huang EY, Li HC, Su PY, Shih C., Free PMC Article

    09/26/2015
    Complementary structural, biochemical and cellular techniques indicated that the formation of a symmetric RNA binding platform generated by dimerization of NXF1:NXT1 facilitates the recognition of CTE-RNA and promotes its nuclear export

    The principal mRNA nuclear export factor NXF1:NXT1 forms a symmetric binding platform that facilitates export of retroviral CTE-RNA.
    Aibara S, Katahira J, Valkov E, Stewart M., Free PMC Article

    06/20/2015
    Gag polyprotein synthesis was decreased by NXF1 knockdown.

    Gammaretroviral pol sequences act in cis to direct polysome loading and NXF1/NXT-dependent protein production by gag-encoded RNA.
    Bartels H, Luban J., Free PMC Article

    03/7/2015
    a spatial map is produced in living cells of the sites for the interaction of two TREX subunits, Alyref and Chtop, with Nxf1.

    Mapping interactions between mRNA export factors in living cells.
    Teng IF, Wilson SA., Free PMC Article

    02/8/2014
    TREX is the major complex used to recruit Nxf1 to mRNA in human cells.

    TREX exposes the RNA-binding domain of Nxf1 to enable mRNA export.
    Viphakone N, Hautbergue GM, Walsh M, Chang CT, Holland A, Folco EG, Reed R, Wilson SA., Free PMC Article

    02/9/2013
    the organization of the NXF1 proline-tyrosine nuclear localization signal reveal unexpected redundancy in the nuclear import pathways used by NXF1.

    Evolutionary development of redundant nuclear localization signals in the mRNA export factor NXF1.
    Zhang ZC, Satterly N, Fontoura BM, Chook YM., Free PMC Article

    04/14/2012
    The U2AF65 protein served as an adaptor to link expanded CAG RNA to NXF1 for RNA export.

    Perturbation of U2AF65/NXF1-mediated RNA nuclear export enhances RNA toxicity in polyQ diseases.
    Tsoi H, Lau CK, Lau KF, Chan HY.

    01/21/2012
    The crystal structure of the RNA recognition and leucine-rich repeat motifs of TAP bound to one symmetrical half of the CTE RNA is solved.

    Structure-function studies of nucleocytoplasmic transport of retroviral genomic RNA by mRNA export factor TAP.
    Teplova M, Wohlbold L, Khin NW, Izaurralde E, Patel DJ., Free PMC Article

    11/12/2011
    these data revealed a redox-regulated chaperone function of PDI in delivering antigenic peptides from TAP to MHC-I.

    Redox-regulated peptide transfer from the transporter associated with antigen processing to major histocompatibility complex class I molecules by protein disulfide isomerase.
    Cho K, Cho S, Lee SO, Oh C, Kang K, Ryoo J, Lee S, Kang S, Ahn K.

    10/29/2011
    Tpr plays an important role in quality control of mRNA trafficked on the Nxf1 pathway.

    The Tpr protein regulates export of mRNAs with retained introns that traffic through the Nxf1 pathway.
    Coyle JH, Bor YC, Rekosh D, Hammarskjold ML., Free PMC Article

    09/3/2011
    These results showed that the interaction between herpes simplex virus type 1 ICP27 and human TAP/NXF1 occurred in living cells upon head-to-tail intramolecular association of ICP27.

    Head-to-tail intramolecular interaction of herpes simplex virus type 1 regulatory protein ICP27 is important for its interaction with cellular mRNA export receptor TAP/NXF1.
    Hernandez FP, Sandri-Goldin RM., Free PMC Article

    08/27/2011
    Varicella-zoster virus IE4 protein interacts with SR proteins and exports mRNAs through the TAP/NXF1 pathway

    Varicella-zoster virus IE4 protein interacts with SR proteins and exports mRNAs through the TAP/NXF1 pathway.
    Ote I, Lebrun M, Vandevenne P, Bontems S, Medina-Palazon C, Manet E, Piette J, Sadzot-Delvaux C., Free PMC Article

    05/3/2010
    Depletion of NXF1 or 5,6-dichloro-1-beta-d-ribofuranosyl-benzimidazole treatment had similar effects, inhibiting the nuclear export of several of the H5N1 influenza virus mRNAs.

    Individual influenza A virus mRNAs show differential dependence on cellular NXF1/TAP for their nuclear export.
    Read EK, Digard P., Free PMC Article

    05/3/2010
    Results describe the subcellular localization of ICP27 and its colocalization with cellular RNA export factors Aly/REF and TAP/NXF1.

    ICP27 phosphorylation site mutants display altered functional interactions with cellular export factors Aly/REF and TAP/NXF1 but are able to bind herpes simplex virus 1 RNA.
    Corbin-Lickfett KA, Rojas S, Li L, Cocco MJ, Sandri-Goldin RM., Free PMC Article

    03/22/2010
    The RNA-binding motif protein 15B (RBM15B/OTT3) acts as cofactor of the nuclear export receptor NXF1.

    The RNA-binding motif protein 15B (RBM15B/OTT3) acts as cofactor of the nuclear export receptor NXF1.
    Uranishi H, Zolotukhin AS, Lindtner S, Warming S, Zhang GM, Bear J, Copeland NG, Jenkins NA, Pavlakis GN, Felber BK., Free PMC Article

    01/21/2010
    TAP/NXF1, but not Aly/REF, is required for RNA export during HSV-1 infection.

    The cellular RNA export receptor TAP/NXF1 is required for ICP27-mediated export of herpes simplex virus 1 RNA, but the TREX complex adaptor protein Aly/REF appears to be dispensable.
    Johnson LA, Li L, Sandri-Goldin RM., Free PMC Article

    01/21/2010
    ICP27 is the major export adaptor for HSV-1 mRNA and that it links bound transcripts to the TAP/NXF1 export receptor

    Efficient nuclear export of herpes simplex virus 1 transcripts requires both RNA binding by ICP27 and ICP27 interaction with TAP/NXF1.
    Johnson LA, Sandri-Goldin RM., Free PMC Article

    01/21/2010
    The efficiency and stability of the approach are demonstrated by reconstructing the structure of a two domain region of the 31 kDa nuclear export factor TAP (TIP-associated protein).

    A structure refinement protocol combining NMR residual dipolar couplings and small angle scattering restraints.
    Gabel F, Simon B, Nilges M, Petoukhov M, Svergun D, Sattler M.

    01/21/2010
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