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    CPEB1 cytoplasmic polyadenylation element binding protein 1 [ Homo sapiens (human) ]

    Gene ID: 64506, updated on 4-Jan-2025

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    CPEB1 Controls NRF2 Proteostasis and Ferroptosis Susceptibility in Pancreatic Cancer.

    CPEB1 Controls NRF2 Proteostasis and Ferroptosis Susceptibility in Pancreatic Cancer.
    Zhang S, Huang J, Lan Z, Xiao Y, Liao Y, Basnet S, Huang P, Li Y, Yan J, Sheng Y, Zhou W, Liu Q, Tan H, Tan Y, Yuan L, Wang L, Dai L, Zhang W, Du C., Free PMC Article

    10/29/2024
    DNA hypermethylation contributes to colorectal cancer metastasis by regulating the binding of CEBPB and TFCP2 to the CPEB1 promoter.

    DNA hypermethylation contributes to colorectal cancer metastasis by regulating the binding of CEBPB and TFCP2 to the CPEB1 promoter.
    Shao K, Pu W, Zhang J, Guo S, Qian F, Glurich I, Jin Q, Ma Y, Ju S, Zhang Z, Ding W., Free PMC Article

    01/22/2022
    CPEB alteration and aberrant transcriptome-polyadenylation lead to a treatable SLC19A3 deficiency in Huntington's disease.

    CPEB alteration and aberrant transcriptome-polyadenylation lead to a treatable SLC19A3 deficiency in Huntington's disease.
    Picó S, Parras A, Santos-Galindo M, Pose-Utrilla J, Castro M, Fraga E, Hernández IH, Elorza A, Anta H, Wang N, Martí-Sánchez L, Belloc E, Garcia-Esparcia P, Garrido JJ, Ferrer I, Macías-García D, Mir P, Artuch R, Pérez B, Hernández F, Navarro P, López-Sendón JL, Iglesias T, Yang XW, Méndez R, Lucas JJ.

    11/6/2021
    Estrogen promotes increased breast cancer cell proliferation and migration through downregulation of CPEB1 expression.

    Estrogen promotes increased breast cancer cell proliferation and migration through downregulation of CPEB1 expression.
    Sovijit W, Sovijit W, Ishii Y, Kambe J, Fujita T, Watanabe G, Yamaguchi H, Nagaoka K.

    04/24/2021
    CPEB1 deletion is not a common explanation for premature ovarian insufficiency in a Chinese cohort.

    CPEB1 deletion is not a common explanation for premature ovarian insufficiency in a Chinese cohort.
    Jiao W, Zhao S, Liu R, Guo T, Qin Y., Free PMC Article

    01/2/2021
    CPEB1 and CPEB4 are involved in the regulation of the TAK1 and Smad signalings in human macrophages and dermal fibroblasts

    CPEB1 or CPEB4 knockdown suppresses the TAK1 and Smad signalings in THP-1 macrophage-like cells and dermal fibroblasts.
    Cui HS, Joo SY, Cho YS, Kim JB, Seo CH.

    07/25/2020
    Study revealed that CPEB1 depletion might play an anti-inflammatory and antiapoptotic role in Ox-LDL-induced apoptosis and inflammation though SIRT1/LOX-1 signalling pathway.

    Depletion of CPEB1 protects against oxidized LDL-induced endothelial apoptosis and inflammation though SIRT1/LOX-1 signalling pathway.
    Xu K, Xiwen Liu, Ren G, Yin D, Guo S, Zhao Y.

    02/15/2020
    study identifies CPEB1 as a potential regulator of disease progression of Posttraumatic Ankle Osteoarthritis

    CPEB1 Expression Correlates with Severity of Posttraumatic Ankle Osteoarthritis and Aggravates Catabolic Effect of IL-1β on Chondrocytes.
    Li L, Lan J, Ye Y, Yang B, Yang X, Cai Z.

    08/3/2019
    These findings indicated that the overexpression of miR4543p inhibited cell proliferation, migration and invasion by downregulating CPEB1.

    miR‑454‑3p suppresses cell migration and invasion by targeting CPEB1 in human glioblastoma.
    Hui X, Zhang S, Wang Y.

    12/22/2018
    Upon binding to p27(Kip1) 3'UTR, CPEB1 promotes elongation of poly-A tail and the subsequent translation of p27(Kip1) mRNA. This leads to higher levels of p27(Kip1) in the cell, in turn significantly inhibiting cell proliferation, and confers to CPEB1 a potential value as a tumor suppressor in Glioblastoma.

    CPEB1 restrains proliferation of Glioblastoma cells through the regulation of p27(Kip1) mRNA translation.
    Galardi S, Petretich M, Pinna G, D'Amico S, Loreni F, Michienzi A, Groisman I, Ciafrè SA., Free PMC Article

    01/27/2018
    CPEB1 regulation of MMP9 mRNA expression mediates metastasis of breast cancer cells

    CPEB1 mediates epithelial-to-mesenchyme transition and breast cancer metastasis.
    Nagaoka K, Fujii K, Zhang H, Usuda K, Watanabe G, Ivshina M, Richter JD., Free PMC Article

    09/2/2017
    The host RNA-binding protein CPEB1 was highly induced after cytomegalovirus infection and ectopic expression of CPEB1 in non-infected cells recapitulated infection-related post-transcriptional changes. CPEB1 was also required for poly(A)-tail lengthening of viral RNAs important for productive infection.

    RNA-binding protein CPEB1 remodels host and viral RNA landscapes.
    Batra R, Stark TJ, Clark AE, Belzile JP, Wheeler EC, Yee BA, Huang H, Gelboin-Burkhart C, Huelga SC, Aigner S, Roberts BT, Bos TJ, Sathe S, Donohue JP, Rigo F, Ares M Jr, Spector DH, Yeo GW., Free PMC Article

    05/20/2017
    Expression levels of CPEB4 and CPEB1 genes are correlated with overall survival in patients with glioma.

    Somatic CPEB4 and CPEB1 genes mutations spectrum on the prognostic predictive accuracy in patients with high-grade glioma and their clinical significance.
    Boustani MR, Mehrabi F, Yahaghi E, Khoshnood RJ, Shahmohammadi M, Darian EK, Goudarzi PK.

    12/31/2016
    WEE1 is regulated at the translational level by CPEB1 and miR-15b in a coordinated and cell-cycle-dependent manner.

    The WEE1 regulators CPEB1 and miR-15b switch from inhibitor to activators at G2/M.
    Kratassiouk G, Pritchard LL, Cuvellier S, Vislovukh A, Meng Q, Groisman R, Degerny C, Deforzh E, Harel-Bellan A, Groisman I., Free PMC Article

    12/17/2016
    This mechanical catalysis makes possible a positive feedback loop that would help localize the formation of CPEB fibers to active synapse areas and mark those synapses for forming a long-term memory after the prion form is established. The functional role of the CPEB helical oligomers in this mechanism carries with it implications for targeting such species in neurodegenerative diseases.

    Energy landscapes of a mechanical prion and their implications for the molecular mechanism of long-term memory.
    Chen M, Zheng W, Wolynes PG., Free PMC Article

    12/17/2016
    Structural Analysis of the Pin1-CPEB1 interaction and its potential role in CPEB1 degradation has been described.

    Structural Analysis of the Pin1-CPEB1 interaction and its potential role in CPEB1 degradation.
    Schelhorn C, Martín-Malpartida P, Suñol D, Macias MJ., Free PMC Article

    08/27/2016
    Identify a mechanism of VEGF overexpression in liver and mesentery that promotes pathologic, but not physiologic, angiogenesis, via sequential and nonredundant functions of CPEB1 and CPEB4.

    Sequential Functions of CPEB1 and CPEB4 Regulate Pathologic Expression of Vascular Endothelial Growth Factor and Angiogenesis in Chronic Liver Disease.
    Calderone V, Gallego J, Fernandez-Miranda G, Garcia-Pras E, Maillo C, Berzigotti A, Mejias M, Bava FA, Angulo-Urarte A, Graupera M, Navarro P, Bosch J, Fernandez M, Mendez R.

    08/13/2016
    CPEB1, 2, and 4, are essential to successful mitotic cell division.

    Global Analysis of CPEBs Reveals Sequential and Non-Redundant Functions in Mitotic Cell Cycle.
    Giangarrà V, Igea A, Castellazzi CL, Bava FA, Mendez R., Free PMC Article

    06/4/2016
    Results suggest that CPEB1-mediated translational control is essential for the differentiation of GSCs.

    CPEB1 modulates differentiation of glioma stem cells via downregulation of HES1 and SIRT1 expression.
    Yin J, Park G, Lee JE, Park JY, Kim TH, Kim YJ, Lee SH, Yoo H, Kim JH, Park JB., Free PMC Article

    06/6/2015
    CPEB accelerates deadenylation and decay of the c-myc mRNA by recruiting the Tob-Caf1 complex.

    Antiproliferative protein Tob directly regulates c-myc proto-oncogene expression through cytoplasmic polyadenylation element-binding protein CPEB.
    Ogami K, Hosoda N, Funakoshi Y, Hoshino S.

    03/8/2014
    Downregulation of CPEB1 induces senescence of glioma cells in a p53-dependent manner.

    CPEB1, a histone-modified hypomethylated gene, is regulated by miR-101 and involved in cell senescence in glioma.
    Xiaoping L, Zhibin Y, Wenjuan L, Zeyou W, Gang X, Zhaohui L, Ying Z, Minghua W, Guiyuan L., Free PMC Article

    03/1/2014
    FMRP and CPEB1, an activator of translation, are present in neuronal dendrites, are predicted to bind many of the same mRNAs and may mediate a translational homeostasis that, when imbalanced, results in fragile X syndrome.

    Genetic and acute CPEB1 depletion ameliorate fragile X pathophysiology.
    Udagawa T, Farny NG, Jakovcevski M, Kaphzan H, Alarcon JM, Anilkumar S, Ivshina M, Hurt JA, Nagaoka K, Nalavadi VC, Lorenz LJ, Bassell GJ, Akbarian S, Chattarji S, Klann E, Richter JD., Free PMC Article

    01/25/2014
    The structural similarity to other ZZ domains suggests that the CPEB1-ZZ domain recruits sumoylated proteins during assembly of the ribonucleoprotein complex prior to mRNA export from the nucleus.

    The C-terminal region of cytoplasmic polyadenylation element binding protein is a ZZ domain with potential for protein-protein interactions.
    Merkel DJ, Wells SB, Hilburn BC, Elazzouzi F, Pérez-Alvarado GC, Lee BM.

    07/13/2013
    results reveal a novel function of CPEB1 in mediating alternative 3'-UTR processing, which is coordinated with regulation of mRNA translation, through its dual nuclear and cytoplasmic functions

    CPEB1 coordinates alternative 3'-UTR formation with translational regulation.
    Bava FA, Eliscovich C, Ferreira PG, Miñana B, Ben-Dov C, Guigó R, Valcárcel J, Méndez R.

    03/30/2013
    poly(A) polymerase Gld2, deadenylase PARN, and translation inhibitory factor neuroguidin (Ngd) are components of a dendritic CPEB-associated polyadenylation apparatus

    Bidirectional control of mRNA translation and synaptic plasticity by the cytoplasmic polyadenylation complex.
    Udagawa T, Swanger SA, Takeuchi K, Kim JH, Nalavadi V, Shin J, Lorenz LJ, Zukin RS, Bassell GJ, Richter JD., Free PMC Article

    10/13/2012
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