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    EIF4ENIF1 eukaryotic translation initiation factor 4E nuclear import factor 1 [ Homo sapiens (human) ]

    Gene ID: 56478, updated on 3-Apr-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    An intramolecular disulphide bond in human 4E-T affects its binding to eIF4E1a protein.

    An intramolecular disulphide bond in human 4E-T affects its binding to eIF4E1a protein.
    Zuberek J, Warzecha M, Dobrowolski M, Modrak-Wojcik A., Free PMC Article

    11/1/2023
    EIF4ENIF1 variants in two patients with non-syndromic premature ovarian insufficiency.

    EIF4ENIF1 variants in two patients with non-syndromic premature ovarian insufficiency.
    Shang L, Ren S, Yang X, Zhang F, Jin L, Zhang X, Wu Y.

    10/22/2022
    we demonstrate that joint deletion of two short conserved motifs that bind UNR and DDX6 relieves repression of 4E-T-bound mRNA, in part reliant on the 4E-T-DDX6-CNOT1 axis.

    The DDX6-4E-T interaction mediates translational repression and P-body assembly.
    Kamenska A, Simpson C, Vindry C, Broomhead H, Bénard M, Ernoult-Lange M, Lee BP, Harries LW, Weil D, Standart N., Free PMC Article

    06/24/2017
    our data support a model where 4E-T promotes mRNA turnover by physically linking the 3'-terminal mRNA decay machinery to the 5' cap

    The eIF4E-Binding Protein 4E-T Is a Component of the mRNA Decay Machinery that Bridges the 5' and 3' Termini of Target mRNAs.
    Nishimura T, Padamsi Z, Fakim H, Milette S, Dunham WH, Gingras AC, Fabian MR.

    04/16/2016
    neural precursors are transcriptionally primed to generate neurons, but an eIF4E/4E-T complex sequesters and represses translation of proneurogenic proteins to determine appropriate neurogenesis.

    An eIF4E1/4E-T complex determines the genesis of neurons from precursors by translationally repressing a proneurogenic transcription program.
    Yang G, Smibert CA, Kaplan DR, Miller FD.

    02/14/2015
    that while both eIF4E1 and eIF4E2 bind 4E-T via the canonical YX 4Lvarphi sequence, nearby downstream sequences also influence eIF4E:4E-T interactions

    Investigating the consequences of eIF4E2 (4EHP) interaction with 4E-transporter on its cellular distribution in HeLa cells.
    Kubacka D, Kamenska A, Broomhead H, Minshall N, Darzynkiewicz E, Standart N., Free PMC Article

    06/21/2014
    This work has demonstrated the conserved yet unpredicted and surprising translational control of bound mRNAs by 4E-T, which does not involve eIF4E, nor P-body components.

    Human 4E-T represses translation of bound mRNAs and enhances microRNA-mediated silencing.
    Kamenska A, Lu WT, Kubacka D, Broomhead H, Minshall N, Bushell M, Standart N., Free PMC Article

    05/24/2014
    Data demonstrate that EIF4ENIF1 is associated with dominantly inherited primary ovarian insufficiency.

    Mutations in eIF4ENIF1 are associated with primary ovarian insufficiency.
    Kasippillai T, MacArthur DG, Kirby A, Thomas B, Lambalk CB, Daly MJ, Welt CK., Free PMC Article

    11/16/2013
    The c-Jun N-terminal kinase (JNK) is targeted to processing bodies in response to oxidative stress and promotes the phosphorylation of 4E-T.

    Phosphorylation of the eukaryotic translation initiation factor 4E-transporter (4E-T) by c-Jun N-terminal kinase promotes stress-dependent P-body assembly.
    Cargnello M, Tcherkezian J, Dorn JF, Huttlin EL, Maddox PS, Gygi SP, Roux PP., Free PMC Article

    01/5/2013
    Hsp90 probably contributes to the correct localization of eIF4E and 4E-T to stress granules and also to the interaction between eIF4E and eIF4G, both of which may be needed for eIF4E to acquire the physiological functionality

    The Hsp90 inhibitor geldanamycin abrogates colocalization of eIF4E and eIF4E-transporter into stress granules and association of eIF4E with eIF4G.
    Suzuki Y, Minami M, Suzuki M, Abe K, Zenno S, Tsujimoto M, Matsumoto K, Minami Y., Free PMC Article

    01/21/2010
    Overexpression of eIF4E-T triggers the movement of eIF4E into the processing bodies.

    Ectopic expression of eIF4E-transporter triggers the movement of eIF4E into P-bodies, inhibiting steady-state translation but not the pioneer round of translation.
    Lee HC, Cho H, Kim YK.

    01/21/2010
    A role for the eIF4E-binding protein 4E-T in P-body formation and mRNA decay is described.

    A role for the eIF4E-binding protein 4E-T in P-body formation and mRNA decay.
    Ferraiuolo MA, Basak S, Dostie J, Murray EL, Schoenberg DR, Sonenberg N., Free PMC Article

    01/21/2010
    human P bodies contain the cap-binding protein eIF4E and the related factor eIF4E-transporter (eIF4E-T), suggesting novel roles for these proteins in targeting mRNAs for 5' --> 3' degradation

    A role for eIF4E and eIF4E-transporter in targeting mRNPs to mammalian processing bodies.
    Andrei MA, Ingelfinger D, Heintzmann R, Achsel T, Rivera-Pomar R, Lührmann R., Free PMC Article

    01/21/2010
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