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    RBFOX2 RNA binding fox-1 homolog 2 [ Homo sapiens (human) ]

    Gene ID: 23543, updated on 10-Oct-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    RBFOX proteins can facilitate the splicing of micro-exons. We also found that PTBP1 likely regulates the inclusion of micro-exons, possibly by repressing the inclusion of micro-exons that are enhanced by RBFOX proteins and other splicing factors.[RBFOX]

    RBFOX and PTBP1 proteins regulate the alternative splicing of micro-exons in human brain transcripts.
    Li YI, Sanchez-Pulido L, Haerty W, Ponting CP., Free PMC Article

    03/2/2016
    CPSF2 and SYMPK, are RBFOX2 cofactors for both inclusion and exclusion of internal exons.

    Global Promotion of Alternative Internal Exon Usage by mRNA 3' End Formation Factors.
    Misra A, Ou J, Zhu LJ, Green MR., Free PMC Article

    08/22/2015
    RBFOX2 SNPs showed evidence for effects across multiple reading and language traits.

    Genome-wide screening for DNA variants associated with reading and language traits.
    Gialluisi A, Newbury DF, Wilcutt EG, Olson RK, DeFries JC, Brandler WM, Pennington BF, Smith SD, Scerri TS, Simpson NH, SLI Consortium, Luciano M, Evans DM, Bates TC, Stein JF, Talcott JB, Monaco AP, Paracchini S, Francks C, Fisher SE., Free PMC Article

    05/23/2015
    Results show that the conserved Rbfox2 RNA binding protein regulates 30% of the splicing transitions observed during myogenesis and is required for the specific step of myoblast fusion.

    Rbfox2-coordinated alternative splicing of Mef2d and Rock2 controls myoblast fusion during myogenesis.
    Singh RK, Xia Z, Bland CS, Kalsotra A, Scavuzzo MA, Curk T, Ule J, Li W, Cooper TA., Free PMC Article

    10/25/2014
    MBNL1 and RBFOX2 cooperate to establish a splicing programme involved in pluripotent stem cell differentiation.

    MBNL1 and RBFOX2 cooperate to establish a splicing programme involved in pluripotent stem cell differentiation.
    Venables JP, Lapasset L, Gadea G, Fort P, Klinck R, Irimia M, Vignal E, Thibault P, Prinos P, Chabot B, Abou Elela S, Roux P, Lemaitre JM, Tazi J.

    04/26/2014
    RBFOX2 polymorphism is associated with breast cancer.

    Associations of polymorphisms in the genes of FGFR2, FGF1, and RBFOX2 with breast cancer risk by estrogen/progesterone receptor status.
    Cen YL, Qi ML, Li HG, Su Y, Chen LJ, Lin Y, Chen WQ, Xie XM, Tang LY, Ren ZF.

    12/21/2013
    RBFOX2 drives mesenchymal tissue-specific splicing in both normal and cancer tissues.

    RBFOX2 is an important regulator of mesenchymal tissue-specific splicing in both normal and cancer tissues.
    Venables JP, Brosseau JP, Gadea G, Klinck R, Prinos P, Beaulieu JF, Lapointe E, Durand M, Thibault P, Tremblay K, Rousset F, Tazi J, Abou Elela S, Chabot B., Free PMC Article

    02/23/2013
    FOX-2 is involved in splicing of ataxin-2 transcripts and that this splicing event is altered by overexpression of ataxin-1

    FOX-2 dependent splicing of ataxin-2 transcript is affected by ataxin-1 overexpression.
    Welzel F, Kaehler C, Isau M, Hallen L, Lehrach H, Krobitsch S., Free PMC Article

    11/3/2012
    functional significance of EMT-associated alternative splicing depletion of RBFOX2 in mesenchymal cells

    An EMT-driven alternative splicing program occurs in human breast cancer and modulates cellular phenotype.
    Shapiro IM, Cheng AW, Flytzanis NC, Balsamo M, Condeelis JS, Oktay MH, Burge CB, Gertler FB., Free PMC Article

    03/31/2012
    This study characterizes the mechanism by which RBFOX2 regulates protein 4.1R exon 16 splicing through the downstream intronic element UGCAUG.

    RBFOX2 promotes protein 4.1R exon 16 selection via U1 snRNP recruitment.
    Huang SC, Ou AC, Park J, Yu F, Yu B, Lee A, Yang G, Zhou A, Benz EJ Jr., Free PMC Article

    02/25/2012
    the negative regulation of Rbfox2 by Rbfox3 through a novel mechanism

    NeuN/Rbfox3 nuclear and cytoplasmic isoforms differentially regulate alternative splicing and nonsense-mediated decay of Rbfox2.
    Dredge BK, Jensen KB., Free PMC Article

    11/5/2011
    Fox-2 plays an integral role in the regulation of LH2 splicing and knockdown of Fox-2 may suggest a novel approach to strategies directed against scleroderma.

    Fox-2 protein regulates the alternative splicing of scleroderma-associated lysyl hydroxylase 2 messenger RNA.
    Seth P, Yeowell HN., Free PMC Article

    05/10/2010
    These findings suggest that FOX2 functions as a critical regulator of a splicing network, and that FOX2 is important for the survival of human embryonic stem cells.

    An RNA code for the FOX2 splicing regulator revealed by mapping RNA-protein interactions in stem cells.
    Yeo GW, Coufal NG, Liang TY, Peng GE, Fu XD, Gage FH., Free PMC Article

    01/21/2010
    predict thousands of Fox-1/2 targets with conserved binding sites, at a false discovery rate of approximately 24%, including many validated experimentally, suggesting a surprisingly extensive splicing regulatory networks

    Defining the regulatory network of the tissue-specific splicing factors Fox-1 and Fox-2.
    Zhang C, Zhang Z, Castle J, Sun S, Johnson J, Krainer AR, Zhang MQ., Free PMC Article

    01/21/2010
    These results establish hnRNP H and hnRNP F as being repressors of exon inclusion and suggest that Fox proteins enhance their ability to antagonize ASF/SF2.

    hnRNP H and hnRNP F complex with Fox2 to silence fibroblast growth factor receptor 2 exon IIIc.
    Mauger DM, Lin C, Garcia-Blanco MA., Free PMC Article

    01/21/2010
    Fox-1/Fox-2 proteins block prespliceosome complex formation at two distinct steps through binding to two functionally important UGCAUG elements.

    Repression of prespliceosome complex formation at two distinct steps by Fox-1/Fox-2 proteins.
    Zhou HL, Lou H., Free PMC Article

    01/21/2010
    Fox-1 and Fox-2 isoforms specifically activate splicing of neuronally regulated exons, which requires UGCAUG enhancer elements

    Homologues of the Caenorhabditis elegans Fox-1 protein are neuronal splicing regulators in mammals.
    Underwood JG, Boutz PL, Dougherty JD, Stoilov P, Black DL., Free PMC Article

    01/21/2010
    Fox-1 and Fox-2 splicing factors have roles in alternative splicing of protein 4.1R

    Fox-2 splicing factor binds to a conserved intron motif to promote inclusion of protein 4.1R alternative exon 16.
    Ponthier JL, Schluepen C, Chen W, Lersch RA, Gee SL, Hou VC, Lo AJ, Short SA, Chasis JA, Winkelmann JC, Conboy JG.

    01/21/2010
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