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    NRBF2 nuclear receptor binding factor 2 [ Homo sapiens (human) ]

    Gene ID: 29982, updated on 2-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    NRBF2-mediated autophagy contributes to metabolite replenishment and radioresistance in glioblastoma.

    NRBF2-mediated autophagy contributes to metabolite replenishment and radioresistance in glioblastoma.
    Kim J, Kang H, Son B, Kim MJ, Kang J, Park KH, Jeon J, Jo S, Kim HY, Youn H, Youn B., Free PMC Article

    12/17/2022
    PI3KC3 complex subunit NRBF2 is required for apoptotic cell clearance to restrict intestinal inflammation.

    PI3KC3 complex subunit NRBF2 is required for apoptotic cell clearance to restrict intestinal inflammation.
    Wu MY, Liu L, Wang EJ, Xiao HT, Cai CZ, Wang J, Su H, Wang Y, Tan J, Zhang Z, Wang J, Yao M, Ouyang DF, Yue Z, Li M, Chen Y, Bian ZX, Lu JH., Free PMC Article

    12/4/2021
    implicates NRBF2 deficiency as a risk factor for cognitive impairment associated with AD, but also support the idea of NRBF2 as a potential therapeutic target for Alzheimer's Disease

    Autophagy protein NRBF2 has reduced expression in Alzheimer's brains and modulates memory and amyloid-beta homeostasis in mice.
    Lachance V, Wang Q, Sweet E, Choi I, Cai CZ, Zhuang XX, Zhang Y, Jiang JL, Blitzer RD, Bozdagi-Gunal O, Zhang B, Lu JH, Yue Z., Free PMC Article

    06/27/2020
    NRBF2 plays an important role in regulating degradation of APP-C-terminal fragments through modulating autophagy.

    NRBF2 is involved in the autophagic degradation process of APP-CTFs in Alzheimer disease models.
    Yang C, Cai CZ, Song JX, Tan JQ, Durairajan SSK, Iyaswamy A, Wu MY, Chen LL, Yue Z, Li M, Lu JH., Free PMC Article

    07/6/2019
    Here we show that a putative fifth subunit, nuclear receptor binding factor 2 (NRBF2), is a tightly bound component of the class III phosphatidylinositol 3-kinase complex I that profoundly affects its activity and architecture. NRBF2 is a homodimer and drives the dimerization of the larger PI3KC3-C1 complex, with implications for the higher-order organization of the preautophagosomal structure.

    Dynamics and architecture of the NRBF2-containing phosphatidylinositol 3-kinase complex I of autophagy.
    Young LN, Cho K, Lawrence R, Zoncu R, Hurley JH., Free PMC Article

    12/2/2017
    This study reveals NRBF2 as a critical molecular switch of PtdIns3K and autophagy activation, and its on/off state is precisely controlled by MTORC1 through phosphorylation.

    MTORC1-mediated NRBF2 phosphorylation functions as a switch for the class III PtdIns3K and autophagy.
    Ma X, Zhang S, He L, Rong Y, Brier LW, Sun Q, Liu R, Fan W, Chen S, Yue Z, Kim J, Guan KL, Li D, Zhong Q., Free PMC Article

    11/26/2017
    Atg38 and its human ortholog NRBF2, accessory components of complex I consisting of Vps15-Vps34-Vps30/Atg6-Atg14 (yeast) and PIK3R4/VPS15-PIK3C3/VPS34-BECN1/Beclin 1-ATG14 (human), were characterized.

    Characterization of Atg38 and NRBF2, a fifth subunit of the autophagic Vps34/PIK3C3 complex.
    Ohashi Y, Soler N, García Ortegón M, Zhang L, Kirsten ML, Perisic O, Masson GR, Burke JE, Jakobi AJ, Apostolakis AA, Johnson CM, Ohashi M, Ktistakis NT, Sachse C, Williams RL., Free PMC Article

    11/18/2017
    Polymorphisms in a putative enhancer at the 10q21.2 Breast Cancer Risk Locus regulate NRBF2 expression, implicating this gene in the etiology of breast cancer.

    Polymorphisms in a Putative Enhancer at the 10q21.2 Breast Cancer Risk Locus Regulate NRBF2 Expression.
    Darabi H, McCue K, Beesley J, Michailidou K, Nord S, Kar S, Humphreys K, Thompson D, Ghoussaini M, Bolla MK, Dennis J, Wang Q, Canisius S, Scott CG, Apicella C, Hopper JL, Southey MC, Stone J, Broeks A, Schmidt MK, Scott RJ, Lophatananon A, Muir K, Beckmann MW, Ekici AB, Fasching PA, Heusinger K, Dos-Santos-Silva I, Peto J, Tomlinson I, Sawyer EJ, Burwinkel B, Marme F, Guénel P, Truong T, Bojesen SE, Flyger H, Benitez J, González-Neira A, Anton-Culver H, Neuhausen SL, Arndt V, Brenner H, Engel C, Meindl A, Schmutzler RK, German Consortium of Hereditary Breast and Ovarian Cancer, Arnold N, Brauch H, Hamann U, Chang-Claude J, Khan S, Nevanlinna H, Ito H, Matsuo K, Bogdanova NV, Dörk T, Lindblom A, Margolin S, kConFab/AOCS Investigators, Kosma VM, Mannermaa A, Tseng CC, Wu AH, Floris G, Lambrechts D, Rudolph A, Peterlongo P, Radice P, Couch FJ, Vachon C, Giles GG, McLean C, Milne RL, Dugué PA, Haiman CA, Maskarinec G, Woolcott C, Henderson BE, Goldberg MS, Simard J, Teo SH, Mariapun S, Helland Å, Haakensen V, Zheng W, Beeghly-Fadiel A, Tamimi R, Jukkola-Vuorinen A, Winqvist R, Andrulis IL, Knight JA, Devilee P, Tollenaar RA, Figueroa J, García-Closas M, Czene K, Hooning MJ, Tilanus-Linthorst M, Li J, Gao YT, Shu XO, Cox A, Cross SS, Luben R, Khaw KT, Choi JY, Kang D, Hartman M, Lim WY, Kabisch M, Torres D, Jakubowska A, Lubinski J, McKay J, Sangrajrang S, Toland AE, Yannoukakos D, Shen CY, Yu JC, Ziogas A, Schoemaker MJ, Swerdlow A, Borresen-Dale AL, Kristensen V, French JD, Edwards SL, Dunning AM, Easton DF, Hall P, Chenevix-Trench G., Free PMC Article

    09/26/2015
    Nrbf2 may interact with the Atg14L-containing Beclin 1-Vps34 protein complex to modulate protein-protein interactions within the complex.

    Nrbf2 protein suppresses autophagy by modulating Atg14L protein-containing Beclin 1-Vps34 complex architecture and reducing intracellular phosphatidylinositol-3 phosphate levels.
    Zhong Y, Morris DH, Jin L, Patel MS, Karunakaran SK, Fu YJ, Matuszak EA, Weiss HL, Chait BT, Wang QJ., Free PMC Article

    02/7/2015
    NRBF2 regulates macroautophagy as a component of Vps34 Complex I.

    NRBF2 regulates macroautophagy as a component of Vps34 Complex I.
    Cao Y, Wang Y, Abi Saab WF, Yang F, Pessin JE, Backer JM., Free PMC Article

    08/23/2014
    The activation domain, their small size (COPR1, 26.9 kDa; COPR2, 32.4 kDa), and strict dependence on AF-2 for interaction distinguish COPR1 and COPR2 from the SMRT/NCoR type of corepressor and may dampen rather than repress NR-mediated gene expression.

    Isolation and functional analysis of a keratinocyte-derived, ligand-regulated nuclear receptor comodulator.
    Flores AM, Li L, Aneskievich BJ.

    01/21/2010
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