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    BRD3 bromodomain containing 3 [ Homo sapiens (human) ]

    Gene ID: 8019, updated on 4-Aug-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Tumor suppressive role of the epigenetic master regulator BRD3 in colorectal cancer.

    Tumor suppressive role of the epigenetic master regulator BRD3 in colorectal cancer.
    Hashimoto M, Masuda T, Nakano Y, Tobo T, Saito H, Koike K, Takahashi J, Abe T, Ando Y, Ozato Y, Hosoda K, Higuchi S, Hisamatsu Y, Toshima T, Yonemura Y, Hata T, Uemura M, Eguchi H, Doki Y, Mori M, Mimori K., Free PMC Article

    07/7/2024
    Targeting BRD3 eradicates nuclear TYRO3-induced colorectal cancer metastasis.

    Targeting BRD3 eradicates nuclear TYRO3-induced colorectal cancer metastasis.
    Hsu PL, Chien CW, Tang YA, Lin BW, Lin SC, Lin YS, Chen SY, Sun HS, Tsai SJ., Free PMC Article

    04/14/2023
    Kinome-wide screening uncovers a role for Bromodomain Protein 3 in DNA double-stranded break repair.

    Kinome-wide screening uncovers a role for Bromodomain Protein 3 in DNA double-stranded break repair.
    Wang C, Chan DW, Hendrickson EA., Free PMC Article

    02/4/2023
    Epigenetic readers and lung cancer: the rs2427964C>T variant of the bromodomain and extraterminal domain gene BRD3 is associated with poorer survival outcome in NSCLC.

    Epigenetic readers and lung cancer: the rs2427964C>T variant of the bromodomain and extraterminal domain gene BRD3 is associated with poorer survival outcome in NSCLC.
    Lee JH, Yoo SS, Hong MJ, Choi JE, Kang HG, Do SK, Lee WK, Choi SH, Lee YH, Seo H, Lee J, Lee SY, Cha SI, Kim CH, Lee EB, Cho S, Jheon S, Park JY., Free PMC Article

    04/16/2022
    A common binding motif in the ET domain of BRD3 forms polymorphic structural interfaces with host and viral proteins.

    A common binding motif in the ET domain of BRD3 forms polymorphic structural interfaces with host and viral proteins.
    Aiyer S, Swapna GVT, Ma LC, Liu G, Hao J, Chalmers G, Jacobs BC, Montelione GT, Roth MJ., Free PMC Article

    01/15/2022
    BCL6 confers KRAS-mutant non-small-cell lung cancer resistance to BET inhibitors.

    BCL6 confers KRAS-mutant non-small-cell lung cancer resistance to BET inhibitors.
    Guo J, Liu Y, Lv J, Zou B, Chen Z, Li K, Feng J, Cai Z, Wei L, Liu M, Pang X., Free PMC Article

    09/11/2021
    Comparative structure-function analysis of bromodomain and extraterminal motif (BET) proteins in a gene-complementation system.

    Comparative structure-function analysis of bromodomain and extraterminal motif (BET) proteins in a gene-complementation system.
    Werner MT, Wang H, Hamagami N, Hsu SC, Yano JA, Stonestrom AJ, Behera V, Zong Y, Mackay JP, Blobel GA., Free PMC Article

    10/24/2020
    BRD3 is recruited to and controls the activity of a subset ERa transcriptional enhancers, providing a therapeutic opportunity to target BRD3 with BET inhibitors in ERa-positive breast cancers.

    Distinct Roles for BET Family Members in Estrogen Receptor α Enhancer Function and Gene Regulation in Breast Cancer Cells.
    Murakami S, Li R, Nagari A, Chae M, Camacho CV, Kraus WL., Free PMC Article

    06/27/2020
    This study presents the first co-crystal structure of SPOP and a bromodomain containing protein (BRD3).

    Structural Insights into BET Client Recognition of Endometrial and Prostate Cancer-Associated SPOP Mutants.
    Ostertag MS, Hutwelker W, Plettenburg O, Sattler M, Popowicz GM.

    04/4/2020
    The BET proteins Brd3 and Brd4 were shown to bind to the NOX4 promoter and drive TGF-beta-induced NOX4 expression. Our data indicate a critical role of BET proteins in promoting redox imbalance and pulmonary myofibroblast activation and support BET bromodomain inhibitors as a potential therapy for fibrotic lung disease.

    Bromodomain and Extraterminal (BET) Protein Inhibition Restores Redox Balance and Inhibits Myofibroblast Activation.
    Stock CJW, Michaeloudes C, Leoni P, Durham AL, Mumby S, Wells AU, Chung KF, Adcock IM, Renzoni EA, Lindahl GE., Free PMC Article

    11/16/2019
    Results provide evidence that both BRD3 and BRD4 are repressors of epithelial-to-mesenchymal transition in breast cancer cells.

    BET Proteins Exhibit Transcriptional and Functional Opposition in the Epithelial-to-Mesenchymal Transition.
    Andrieu GP, Denis GV., Free PMC Article

    08/3/2019
    Recruitment of Brd3 (and Brd4) to chromatin is essential for inflammation mediator-induced matrix-degrading enzyme expression.

    Recruitment of Brd3 and Brd4 to acetylated chromatin is essential for proinflammatory cytokine-induced matrix-degrading enzyme expression.
    Dai J, Zhou S, Ge Q, Qin J, Li J, Ju H, Cao Y, Zheng M, Li C, Gao X, Teng H, Jiang Q., Free PMC Article

    06/22/2019
    data provide insight into the mechanisms by which BET family proteins might link chromatin acetylation to transcriptional outcomes and uncover an unexpected functional similarity between BET and YEATS family proteins

    The BRD3 ET domain recognizes a short peptide motif through a mechanism that is conserved across chromatin remodelers and transcriptional regulators.
    Wai DCC, Szyszka TN, Campbell AE, Kwong C, Wilkinson-White LE, Silva APG, Low JKK, Kwan AH, Gamsjaeger R, Chalmers JD, Patrick WM, Lu B, Vakoc CR, Blobel GA, Mackay JP., Free PMC Article

    01/26/2019
    conclude that BRD3/4 and the FLT3-TAK1/NF-kB pathways collectively control a set of targets that are critically important for the survival of human MLL-AF9 cells

    BRD3/4 inhibition and FLT3-ligand deprivation target pathways that are essential for the survival of human MLL-AF9+ leukemic cells.
    Carretta M, Brouwers-Vos AZ, Bosman M, Horton SJ, Martens JHA, Vellenga E, Schuringa JJ., Free PMC Article

    01/20/2018
    The bromodomain and extraterminal domain (BET) family consists of BRDT, BRD2, BRD3, and BRD4, each containing 2 bromodomains located N-terminal to extraterminal domain, which is located near C-terminus. Data suggest that 10 distinct acylations participate in binding of BET family proteins to histone 4 (oligopeptide fragments used here); C-terminal bromodomains do not cooperatively bind multiple acylation sites.

    Metabolically Derived Lysine Acylations and Neighboring Modifications Tune the Binding of the BET Bromodomains to Histone H4.
    Olp MD, Zhu N, Smith BC., Free PMC Article

    10/28/2017
    Ewing sarcoma may be susceptible to treatment with epigenetic inhibitors blocking BRD3/4 activity and the associated pathognomonic EWS-FLT1 transcriptional program.

    Targeting the EWS-ETS transcriptional program by BET bromodomain inhibition in Ewing sarcoma.
    Hensel T, Giorgi C, Schmidt O, Calzada-Wack J, Neff F, Buch T, Niggli FK, Schäfer BW, Burdach S, Richter GH., Free PMC Article

    12/17/2016
    An isoform of BRD3, BRD3R (BRD3 with Reprogramming activity) is a reprogramming factor.

    The acetyllysine reader BRD3R promotes human nuclear reprogramming and regulates mitosis.
    Shao Z, Zhang R, Khodadadi-Jamayran A, Chen B, Crowley MR, Festok MA, Crossman DK, Townes TM, Hu K., Free PMC Article

    09/24/2016
    Here, we identify NCT, a complex comprising the Nrc1 BET-family tandem bromodomain protein (SPAC631.02), casein kinase II (CKII), and several TAFs, as a regulator of condensin function.

    Identification of a BET family bromodomain/casein kinase II/TAF-containing complex as a regulator of mitotic condensin function.
    Kim HS, Mukhopadhyay R, Rothbart SB, Silva AC, Vanoosthuyse V, Radovani E, Kislinger T, Roguev A, Ryan CJ, Xu J, Jahari H, Hardwick KG, Greenblatt JF, Krogan NJ, Fillingham JS, Strahl BD, Bouhassira EE, Edelmann W, Keogh MC., Free PMC Article

    01/10/2015
    BRD2, BRD3, and BRD4 interact with gammaretroviral INs and serve as cofactors for murine leukemia virus integration.

    Bromo- and extraterminal domain chromatin regulators serve as cofactors for murine leukemia virus integration.
    Gupta SS, Maetzig T, Maertens GN, Sharif A, Rothe M, Weidner-Glunde M, Galla M, Schambach A, Cherepanov P, Schulz TF., Free PMC Article

    01/11/2014
    The BRDT gene was not expressed in testicular tissue from patients with Sertoli cells only, whereas the other three genes of the BET family retained expression in all the sperm pathologies.

    Expression of BET genes in testis of men with different spermatogenic impairments.
    Barda S, Paz G, Yogev L, Yavetz H, Lehavi O, Hauser R, Botchan A, Breitbart H, Kleiman SE.

    02/18/2012
    the structural basis for GATA1 and Brd3 interaction was described.

    Structural basis and specificity of acetylated transcription factor GATA1 recognition by BET family bromodomain protein Brd3.
    Gamsjaeger R, Webb SR, Lamonica JM, Billin A, Blobel GA, Mackay JP., Free PMC Article

    08/27/2011
    BRD-NUT fusion proteins contribute to carcinogenesis by associating with chromatin and interfering with epithelial differentiation.

    BRD-NUT oncoproteins: a family of closely related nuclear proteins that block epithelial differentiation and maintain the growth of carcinoma cells.
    French CA, Ramirez CL, Kolmakova J, Hickman TT, Cameron MJ, Thyne ME, Kutok JL, Toretsky JA, Tadavarthy AK, Kees UR, Fletcher JA, Aster JC.

    01/21/2010
    Results report that the double bromodomain proteins Brd2 and Brd3 associate preferentially in vivo with hyperacetylated chromatin along the entire lengths of transcribed genes.

    The double bromodomain proteins Brd2 and Brd3 couple histone acetylation to transcription.
    LeRoy G, Rickards B, Flint SJ., Free PMC Article

    01/21/2010
    Activated lymphocytes induced by mitogens or antigens express various sets of genes, including those involved in the expression of cytokines, surface molecules, and nuclear proteins.

    Detection of the genes induced in activated lymphocytes by modified differential display.
    Kaneko H, Inoue R, Teramoto T, Morimoto W, Isogai K, Kasahara K, Kondo N.

    01/21/2010
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