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    EIF4A2 eukaryotic translation initiation factor 4A2 [ Homo sapiens (human) ]

    Gene ID: 1974, updated on 12-Sep-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Dystonia Linked to EIF4A2 Haploinsufficiency: A Disorder of Protein Translation Dysfunction.

    Dystonia Linked to EIF4A2 Haploinsufficiency: A Disorder of Protein Translation Dysfunction.
    Harrer P, Škorvánek M, Kittke V, Dzinovic I, Borngräber F, Thomsen M, Mandel V, Svorenova T, Ostrozovicova M, Kulcsarova K, Berutti R, Busch H, Ott F, Kopajtich R, Prokisch H, Kumar KR, Mencacci NE, Kurian MA, Di Fonzo A, Boesch S, Kühn AA, Blümlein U, Lohmann K, Haslinger B, Weise D, Jech R, Winkelmann J, Zech M.

    11/1/2023
    Monitoring RNA restructuring in a human cell-free extract reveals eIF4A-dependent and eIF4A-independent unwinding activity.

    Monitoring RNA restructuring in a human cell-free extract reveals eIF4A-dependent and eIF4A-independent unwinding activity.
    O'Sullivan MH, Fraser CS., Free PMC Article

    08/3/2023
    Rare EIF4A2 variants are associated with a neurodevelopmental disorder characterized by intellectual disability, hypotonia, and epilepsy.

    Rare EIF4A2 variants are associated with a neurodevelopmental disorder characterized by intellectual disability, hypotonia, and epilepsy.
    Paul MS, Duncan AR, Genetti CA, Pan H, Jackson A, Grant PE, Shi J, Pinelli M, Brunetti-Pierri N, Garza-Flores A, Shahani D, Saneto RP, Zampino G, Leoni C, Agolini E, Novelli A, Blümlein U, Haack TB, Heinritz W, Matzker E, Alhaddad B, Abou Jamra R, Bartolomaeus T, AlHamdan S, Carapito R, Isidor B, Bahram S, Ritter A, Izumi K, Shakked BP, Barel O, Ben Zeev B, Begtrup A, Carere DA, Mullegama SV, Palculict TB, Calame DG, Schwan K, Aycinena ARP, Traberg R, Genomics England Research Consortium, Douzgou S, Pirt H, Ismayilova N, Banka S, Chao HT, Agrawal PB., Free PMC Article

    01/14/2023
    exerts its repressive effect on translation initiation by binding purine-rich motifs which are enriched in the 5'UTR of target mRNAs directly upstream of the AUG start codon

    eIF4A2 drives repression of translation at initiation by Ccr4-Not through purine-rich motifs in the 5'UTR.
    Wilczynska A, Gillen SL, Schmidt T, Meijer HA, Jukes-Jones R, Langlais C, Kopra K, Lu WT, Godfrey JD, Hawley BR, Hodge K, Zanivan S, Cain K, Le Quesne J, Bushell M., Free PMC Article

    03/21/2020
    Data show that incorporation of ATP-dependent RNA helicase eIF4A-2 (eIF4A2) into the CCR4-NOT complex inhibits CCR4-NOT transcription complex subunit 7 (CNOT7) deadenylation activity.

    DEAD-box helicase eIF4A2 inhibits CNOT7 deadenylation activity.
    Meijer HA, Schmidt T, Gillen SL, Langlais C, Jukes-Jones R, de Moor CH, Cain K, Wilczynska A, Bushell M., Free PMC Article

    12/14/2019
    high EIF4A2 expression predicts poor prognosis of CRC patients and is associated with distant metastasis and poor response to oxaliplatin. Knocking-down EIF4A2 inhibits sphere formation and experimental metastasis, as well as oxaliplatin resistance in CRC.

    Eukaryotic initiation factor 4A2 promotes experimental metastasis and oxaliplatin resistance in colorectal cancer.
    Chen ZH, Qi JJ, Wu QN, Lu JH, Liu ZX, Wang Y, Hu PS, Li T, Lin JF, Wu XY, Miao L, Zeng ZL, Xie D, Ju HQ, Xu RH, Wang F., Free PMC Article

    11/16/2019
    EIF4A2 was confirmed as a potential target of miR-5195-3p. MicroRNA-5195-3p enhances the chemosensitivity of triple-negative breast cancer (TNBC) to paclitaxel (PTX) by downregulating EIF4A2.

    MicroRNA-5195-3p enhances the chemosensitivity of triple-negative breast cancer to paclitaxel by downregulating EIF4A2.
    Liu M, Gong C, Xu R, Chen Y, Wang X., Free PMC Article

    08/31/2019
    Eukaryotic translation initiation factor 4A2 (eIF4A2) is necessary for efficient HIV-1 replication in human lymphoid cell line. eIF4A2 depletion reduces the efficiency of viral cDNA synthesis with virion entry into target cells being unaffected. Depletion of eIF4A2 also inhibits HIV-1 spreading infection in a knockdown level-dependent manner.

    eIF4A2 is a host factor required for efficient HIV-1 replication.
    Ndzinu JK, Takeuchi H, Saito H, Yoshida T, Yamaoka S.

    05/4/2019
    eIF4A2 is recruited to stress granules, suggesting sumoylation of eIF4A2 correlates with its recruitment to stress granules.

    Sumoylation of eIF4A2 affects stress granule formation.
    Jongjitwimol J, Baldock RA, Morley SJ, Watts FZ., Free PMC Article

    08/5/2017
    Studies indicate a developing focus on targeting eukaryotic initiation factor 4A eIF4A1 and eIF4A2 as cancer therapy.

    Translational dysregulation in cancer: eIF4A isoforms and sequence determinants of eIF4A dependence.
    Raza F, Waldron JA, Quesne JL.

    09/17/2016
    expression is an independent prognostic factor for patients with non-small-cell lung cancer for both overall survival and disease-free survival

    Downregulation of EIF4A2 in non-small-cell lung cancer associates with poor prognosis.
    Shaoyan X, Juanjuan Y, Yalan T, Ping H, Jianzhong L, Qinian W.

    07/19/2014
    These data support a linear model for miRNA-mediated gene regulation in which translational repression via eIF4A2 is required first, followed by mRNA destabilization.

    Translational repression and eIF4A2 activity are critical for microRNA-mediated gene regulation.
    Meijer HA, Kong YW, Lu WT, Wilczynska A, Spriggs RV, Robinson SW, Godfrey JD, Willis AE, Bushell M.

    04/20/2013
    The results indicated that eIF4AI and eIF4AII expression are linked and that the two protein isoforms exhibit functional differences.

    A cellular response linking eIF4AI activity to eIF4AII transcription.
    Galicia-Vázquez G, Cencic R, Robert F, Agenor AQ, Pelletier J., Free PMC Article

    09/1/2012
    A protein encoded by this locus was found to be differentially expressed in postmortem brains from patients with atypical frontotemporal lobar degeneration.

    Proteomic analysis identifies dysfunction in cellular transport, energy, and protein metabolism in different brain regions of atypical frontotemporal lobar degeneration.
    Martins-de-Souza D, Guest PC, Mann DM, Roeber S, Rahmoune H, Bauder C, Kretzschmar H, Volk B, Baborie A, Bahn S.

    04/26/2012
    Studies indicate that eIF4A (DDX2), together with its accessory proteins eIF4B and eIF4H, is thought to act as a helicase that unwinds secondary structures in the mRNA 5' UTR.

    mRNA helicases: the tacticians of translational control.
    Parsyan A, Svitkin Y, Shahbazian D, Gkogkas C, Lasko P, Merrick WC, Sonenberg N.

    06/18/2011
    subcellular distribution of eIF4F components may potentiate the complex assembly

    Eukaryotic translation initiation factor 4F architectural alterations accompany translation initiation factor redistribution in poxvirus-infected cells.
    Walsh D, Arias C, Perez C, Halladin D, Escandon M, Ueda T, Watanabe-Fukunaga R, Fukunaga R, Mohr I., Free PMC Article

    01/21/2010
    This protein has been found differentially expressed in the temporal lobe from patients with schizophrenia.

    Alterations in oligodendrocyte proteins, calcium homeostasis and new potential markers in schizophrenia anterior temporal lobe are revealed by shotgun proteome analysis.
    Martins-de-Souza D, Gattaz WF, Schmitt A, Rewerts C, Marangoni S, Novello JC, Maccarrone G, Turck CW, Dias-Neto E.

    12/15/2008
    A feedforward loop involving c-Myc and eIF4F that serves to link transcription and translation and that could contribute to the effects of c-Myc on cell proliferation and neoplastic growth.

    c-Myc and eIF4F are components of a feedforward loop that links transcription and translation.
    Lin CJ, Cencic R, Mills JR, Robert F, Pelletier J.

    01/21/2010
    interacted with NS5B protein, and the two proteins were shown to be partially colocalized in the perinuclear region

    Human eukaryotic initiation factor 4AII associates with hepatitis C virus NS5B protein in vitro.
    Kyono K, Miyashiro M, Taguchi I.

    01/21/2010
    Single nucleotide polymorphisms in two relevant candidate genes for glucose homeostasis, kininogen (KNG1), and eukaryotic translation initiation factor 4alpha2 (EIF4A2) linked to type 2 diabetes.

    EIF4A2 is a positional candidate gene at the 3q27 locus linked to type 2 diabetes in French families.
    Cheyssac C, Dina C, Leprêtre F, Vasseur-Delannoy V, Dechaume A, Lobbens S, Balkau B, Ruiz J, Charpentier G, Pattou F, Joly E, Prentki M, Hansen T, Pedersen O, Vaxillaire M, Froguel P.

    01/21/2010
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