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    EIF4E2 eukaryotic translation initiation factor 4E family member 2 [ Homo sapiens (human) ]

    Gene ID: 9470, updated on 6-Oct-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    METTL16 promotes translation and lung tumorigenesis by sequestering cytoplasmic eIF4E2.

    METTL16 promotes translation and lung tumorigenesis by sequestering cytoplasmic eIF4E2.
    Wang F, Zhang J, Lin X, Yang L, Zhou Q, Mi X, Li Q, Wang S, Li D, Liu XM, Zhou J.

    04/7/2023
    Translational repression of NMD targets by GIGYF2 and EIF4E2.

    Translational repression of NMD targets by GIGYF2 and EIF4E2.
    Zinshteyn B, Sinha NK, Enam SU, Koleske B, Green R., Free PMC Article

    12/4/2021
    4EHP and GIGYF1/2 Mediate Translation-Coupled Messenger RNA Decay.

    4EHP and GIGYF1/2 Mediate Translation-Coupled Messenger RNA Decay.
    Weber R, Chung MY, Keskeny C, Zinnall U, Landthaler M, Valkov E, Izaurralde E, Igreja C., Free PMC Article

    09/25/2021
    High EIF4E2 expression is an independent prognostic risk factor for poor overall survival and recurrence-free survival in uveal melanoma.

    High EIF4E2 expression is an independent prognostic risk factor for poor overall survival and recurrence-free survival in uveal melanoma.
    Yang B, Gu A, Wu Y.

    09/18/2021
    microRNA-induced translational control of antiviral immunity by the cap-binding protein 4EHP.

    microRNA-induced translational control of antiviral immunity by the cap-binding protein 4EHP.
    Zhang X, Chapat C, Wang P, Choi JH, Li Q, Luo J, Wiebe S, Kim SH, Robichaud N, Karam IF, Dai D, Hackett AP, Lin R, Alain T, Yang L, Jafarnejad SM, Sonenberg N.

    04/3/2021
    GIGYF2 and 4EHP Inhibit Translation Initiation of Defective Messenger RNAs to Assist Ribosome-Associated Quality Control.

    GIGYF2 and 4EHP Inhibit Translation Initiation of Defective Messenger RNAs to Assist Ribosome-Associated Quality Control.
    Hickey KL, Dickson K, Cogan JZ, Replogle JM, Schoof M, D'Orazio KN, Sinha NK, Hussmann JA, Jost M, Frost A, Green R, Weissman JS, Kostova KK., Free PMC Article

    10/3/2020
    The authors that the Dusp6 mRNA, which encodes an ERK1/2 phosphatase, is translationally repressed by 4EHP and a specific miRNA, miR-145.

    Translational control of ERK signaling through miRNA/4EHP-directed silencing.
    Jafarnejad SM, Chapat C, Matta-Camacho E, Gelbart IA, Hesketh GG, Arguello M, Garzia A, Kim SH, Attig J, Shapiro M, Morita M, Khoutorsky A, Alain T, Gkogkas CG, Stern-Ginossar N, Tuschl T, Gingras AC, Duchaine TF, Sonenberg N., Free PMC Article

    08/10/2019
    cadherin-22 is upregulated in hypoxia via mTORC1-independent translational control by the initiation factor eIF4E2 functioning as a hypoxia-specific cell-surface molecule involved in cancer cell migration, invasion and adhesion.

    Hypoxia activates cadherin-22 synthesis via eIF4E2 to drive cancer cell migration, invasion and adhesion.
    Kelly NJ, Varga JFA, Specker EJ, Romeo CM, Coomber BL, Uniacke J., Free PMC Article

    10/13/2018
    cap-binding activity contributes to the translational silencing by miRNAs through the CCR4-NOT complex

    Cap-binding protein 4EHP effects translation silencing by microRNAs.
    Chapat C, Jafarnejad SM, Matta-Camacho E, Hesketh GG, Gelbart IA, Attig J, Gkogkas CG, Alain T, Stern-Ginossar N, Fabian MR, Gingras AC, Duchaine TF, Sonenberg N., Free PMC Article

    05/19/2018
    We performed bioinformatics analyses of ESTs and the 3'UTRs of the main transcript splice variants of the translational initiation factor eIF4E1 and its family members, eIF4E2 and eIF4E3. We propose to elucidate the minor splice variants of eIF4E2 and eIF4E3 in great detail because they might produce proteins with modified features that fulfill different cellular roles from their major counterparts.

    Major splice variants and multiple polyadenylation site utilization in mRNAs encoding human translation initiation factors eIF4E1 and eIF4E3 regulate the translational regulators?
    Mrvová S, Frydrýšková K, Pospíšek M, Vopálenský V, Mašek T.

    02/17/2018
    miRNA enhances eIF4E2 association with the target mRNA

    MicroRNAs recruit eIF4E2 to repress translation of target mRNAs.
    Chen S, Gao G., Free PMC Article

    12/2/2017
    Following heat shock, eIF4E2 is found in both processing bodies and stress granules, whereas eIF4E3_A relocates only to stress granules.

    Distinct recruitment of human eIF4E isoforms to processing bodies and stress granules.
    Frydryskova K, Masek T, Borcin K, Mrvova S, Venturi V, Pospisek M., Free PMC Article

    09/16/2017
    Tristetraprolin recruits eukaryotic initiation factor 4E2 (eIF4E2) to repress target mRNA translation.

    Tristetraprolin Recruits Eukaryotic Initiation Factor 4E2 To Repress Translation of AU-Rich Element-Containing mRNAs.
    Tao X, Gao G., Free PMC Article

    02/6/2016
    DNA damage induces an increase in ARIH1 protein levels and association of ARIH1 with 4EHP. In turn, this causes 4EHP recruitment to the mRNA cap, where it is known to compete with eIF4E.

    The E3 ubiquitin ligase ARIH1 protects against genotoxic stress by initiating a 4EHP-mediated mRNA translation arrest.
    von Stechow L, Typas D, Carreras Puigvert J, Oort L, Siddappa R, Pines A, Vrieling H, van de Water B, Mullenders LH, Danen EH., Free PMC Article

    05/30/2015
    provide evidence that eIF4E2 binds 4E-T in the yeast two hybrid assay, as well as in pull-down assays and by recruitment to P-bodies in mammalian cells

    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
    Activation of eIF4E2-directed translation is essential for cancer cells.

    Cancer cells exploit eIF4E2-directed synthesis of hypoxia response proteins to drive tumor progression.
    Uniacke J, Perera JK, Lachance G, Francisco CB, Lee S.

    06/7/2014
    GIGYF2 and the zinc finger protein 598 (ZNF598) are identified as components of the 4EHP complex.

    A novel 4EHP-GIGYF2 translational repressor complex is essential for mammalian development.
    Morita M, Ler LW, Fabian MR, Siddiqui N, Mullin M, Henderson VC, Alain T, Fonseca BD, Karashchuk G, Bennett CF, Kabuta T, Higashi S, Larsson O, Topisirovic I, Smith RJ, Gingras AC, Sonenberg N., Free PMC Article

    11/3/2012
    Observational study and genome-wide association study of gene-disease association. (HuGE Navigator)

    Genome-wide association study on overall survival of advanced non-small cell lung cancer patients treated with carboplatin and paclitaxel.
    Sato Y, Yamamoto N, Kunitoh H, Ohe Y, Minami H, Laird NM, Katori N, Saito Y, Ohnami S, Sakamoto H, Sawada J, Saijo N, Yoshida T, Tamura T.

    12/5/2010
    Clinical trial of gene-disease association and gene-environment interaction. (HuGE Navigator)

    Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score.
    Rose JE, Behm FM, Drgon T, Johnson C, Uhl GR., Free PMC Article

    06/30/2010
    ISGylation of 4EHP may play an important role in cap structure-dependent translation control in immune responses.

    ISG15 modification of the eIF4E cognate 4EHP enhances cap structure-binding activity of 4EHP.
    Okumura F, Zou W, Zhang DE., Free PMC Article

    01/21/2010
    4EHP binds cap analogs m(7)GpppG and m(7)GTP with low affinity

    Weak binding affinity of human 4EHP for mRNA cap analogs.
    Zuberek J, Kubacka D, Jablonowska A, Jemielity J, Stepinski J, Sonenberg N, Darzynkiewicz E., Free PMC Article

    01/21/2010
    4EHP over-expression instigates a negative feedback loop that inhibits upstream signaling to 4E-BP1 and ribosomal protein S6 kinase 1 (S6K1) whereas the 4E-BP1-binding-deficient mutant of 4EHP(W95A) was unable to trigger this feedback loop

    Characterizing the interaction of the mammalian eIF4E-related protein 4EHP with 4E-BP1.
    Tee AR, Tee JA, Blenis J.

    01/21/2010
    4EHP plays a physiological role utilizing both cap-binding and protein-binding functions but which is distinct from eIF4E.

    Structures of the human eIF4E homologous protein, h4EHP, in its m7GTP-bound and unliganded forms.
    Rosettani P, Knapp S, Vismara MG, Rusconi L, Cameron AD.

    01/21/2010
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