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    Pabpc1 poly(A) binding protein, cytoplasmic 1 [ Mus musculus (house mouse) ]

    Gene ID: 18458, updated on 27-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    De novo variants in the PABP domain of PABPC1 lead to developmental delay.

    De novo variants in the PABP domain of PABPC1 lead to developmental delay.
    Wegler M, Jia X, Alders M, Bouman A, Chen J, Duan X, Lauzon JL, Mathijssen IB, Sticht H, Syrbe S, Tan S, Guo H, Abou Jamra R.

    08/20/2022
    Translation of insulin granule proteins are regulated by PDI and PABP.

    Translation of insulin granule proteins are regulated by PDI and PABP.
    Sarwade RD, Khalique A, Kulkarni SD, Pandey PR, Gaikwad N, Seshadri V.

    12/5/2020
    in the diabetic retinopathy environment, TTR might affect the lncRNA MEG3/miR-223-3p axis by the direct binding with PABPC1, and finally repress retinal vessel proliferation.

    Transthyretin Upregulates Long Non-Coding RNA MEG3 by Affecting PABPC1 in Diabetic Retinopathy.
    Fan G, Gu Y, Zhang J, Xin Y, Shao J, Giampieri F, Battino M., Free PMC Article

    05/2/2020
    The findings suggest that EPAB in cooperation with PABPC1 implicate in the translational control of maternal mRNAs during oogenesis and early embryo development.

    Embryonic poly(A)-binding protein is differently expressed and interacts with the messenger RNAs in the mouse oocytes and early embryos.
    Uysal F, Ozturk S.

    03/21/2020
    PIWIL1 augments protein translation with PABPC1 in the presence of 3'-UTRs of post-meiotic mRNAs. While both the N-terminal RNA recognition motif (RRM) domain and the central linker region of PABPC1 stimulate translation, only the PIWI Argonaute and Zwille (PAZ) domain of PIWIL1 positively affects translation of reporter mRNAs.

    Domain-functional analyses of PIWIL1 and PABPC1 indicate their synergistic roles in protein translation via 3'-UTRs of meiotic mRNAs.
    Wu Y, Xu K, Qi H.

    09/28/2019
    The nicotinamide adenine dinucleotide (NAD)-dependent deacetylase SIRT1 acts as an energy sensor and negatively regulates poly(A)RNA transport via deacetylating a poly(A)-binding protein, PABP1.

    SIRT1 Functions as a Negative Regulator of Eukaryotic Poly(A)RNA Transport.
    Shan P, Fan G, Sun L, Liu J, Wang W, Hu C, Zhang X, Zhai Q, Song X, Cao L, Cui Y, Zhang S, Wang C.

    07/28/2018
    These results suggest that PABP interacts with HuD in basal glucose conditions making translation inhibitory complex, however upon glucose stimulation this association is affected and PABP is acted upon by PDI resulting in stimulation of insulin translation.

    Interaction of HuDA and PABP at 5'UTR of mouse insulin2 regulates insulin biosynthesis.
    Pandey PR, Sarwade RD, Khalique A, Seshadri V., Free PMC Article

    07/14/2018
    These results demonstrate that EPAB is important for oocyte-somatic communication by maintaining transzonal processes and gap junctions at the preantral stage of folliculogenesis.

    Embryonic poly(A)-binding protein is required at the preantral stage of mouse folliculogenesis for oocyte-somatic communication.
    Lowther KM, Favero F, Yang CR, Taylor HS, Seli E.

    06/30/2018
    The authors found that the endogenous Zfp36 directly interacts with the cytoplasmic poly(A)-binding protein. Importantly, this interaction is required for the translational repression of Zfp36's target mRNAs in resolving inflammation.

    Translation repression via modulation of the cytoplasmic poly(A)-binding protein in the inflammatory response.
    Zhang X, Chen X, Liu Q, Zhang S, Hu W., Free PMC Article

    03/10/2018
    Data suggest that hnRNPLL specifically associates with cytoplasmic PABPC1 in both T-lymphocytes and plasma cells; PABPC1 promotes binding of hnRNPLL to immunoglobulin H (IgH, heavy chain) mRNA and regulates switching from mIgH (membrane isoform) to sIgH (secreted isoform) in plasma cells. (hnRNPLL = heterogeneous nuclear ribonucleoprotein L-like protein; PABPC1 = cytoplasmic poly[A]-binding protein 1)

    Cytoplasmic poly(A)-binding protein 1 (PABPC1) interacts with the RNA-binding protein hnRNPLL and thereby regulates immunoglobulin secretion in plasma cells.
    Peng Y, Yuan J, Zhang Z, Chang X., Free PMC Article

    08/12/2017
    Superovulation with low or high doses of gonadotropins significantly altered Epab and Pabpc1 mRNA levels in GV oocytes, MII oocytes and 1- and 2-cell embryos compared with their respective controls. These changes most likely lead to variations in expression of EPAB- and PABPC1-regulated genes, which may adversely influence the quality of oocytes and early embryos retrieved using superovulation.

    Superovulation alters embryonic poly(A)-binding protein (Epab) and poly(A)-binding protein, cytoplasmic 1 (Pabpc1) gene expression in mouse oocytes and early embryos.
    Ozturk S, Yaba-Ucar A, Sozen B, Mutlu D, Demir N.

    04/15/2017
    Data (including data from studies in knockout mice) suggest that Epab (embryonic poly(A)-binding protein), which is oocyte specific, is required for ability of cumulus cells and granulosa cells to exhibit responsiveness to Egf/Egfr signaling.

    Embryonic Poly(A)-Binding Protein (EPAB) Is Required for Granulosa Cell EGF Signaling and Cumulus Expansion in Female Mice.
    Yang CR, Lowther KM, Lalioti MD, Seli E., Free PMC Article

    05/21/2016
    Epab(-/-) oocytes are smaller in size, contain peripheral germinal vesicles, and are loosely associated with cumulus cells

    Embryonic Poly(A)-Binding Protein Is Required During Early Stages of Mouse Oocyte Development for Chromatin Organization, Transcriptional Silencing, and Meiotic Competence.
    Lowther KM, Mehlmann LM., Free PMC Article

    05/21/2016
    These findings suggest that EPAB may predominantly play roles in translational regulation of the mRNAs during early oogenesis and folliculogenesis, but PABPC1 most likely perform these roles in the later terms of ovarian development along with EPAB

    Epab and Pabpc1 are differentially expressed in the postnatal mouse ovaries.
    Ozturk S, Sozen B, Demir N., Free PMC Article

    09/26/2015
    Epab is dispensable for mouse spermatogenesis and male fertility.

    Epab is dispensable for mouse spermatogenesis and male fertility.
    Ozturk S, Guzeloglu-Kayisli O, Lowther KM, Lalioti MD, Sakkas D, Seli E., Free PMC Article

    02/14/2015
    We analyzed the expression of sperm-specific Akap3 and the potential regulatory factors of its protein synthesis during mouse spermiogenesis.

    AKAP3 synthesis is mediated by RNA binding proteins and PKA signaling during mouse spermiogenesis.
    Xu K, Yang L, Zhao D, Wu Y, Qi H.

    01/24/2015
    Both Epab and Pabpc1 expression increase during early postnatal life and reach their peak at D32 testis.

    Epab and Pabpc1 are differentially expressed during male germ cell development.
    Ozturk S, Guzeloglu-Kayisli O, Demir N, Sozen B, Ilbay O, Lalioti MD, Seli E., Free PMC Article

    04/19/2014
    our data support the concept that expanded ATXN2 undergoes progressive insolubility and affects PABPC1 by a toxic gain-of-function mechanism with tissue-specific effects, which may be partially alleviated by the induction of FBXW8.

    ATXN2-CAG42 sequesters PABPC1 into insolubility and induces FBXW8 in cerebellum of old ataxic knock-in mice.
    Damrath E, Heck MV, Gispert S, Azizov M, Nowock J, Seifried C, Rüb U, Walter M, Auburger G., Free PMC Article

    01/5/2013
    EPAB is necessary for oogenesis, folliculogenesis and female fertility in mice.

    Embryonic poly(A)-binding protein (EPAB) is required for oocyte maturation and female fertility in mice.
    Guzeloglu-Kayisli O, Lalioti MD, Aydiner F, Sasson I, Ilbay O, Sakkas D, Lowther KM, Mehlmann LM, Seli E., Free PMC Article

    11/3/2012
    PABPC2 was present in pachytene spermatocytes and round spermatids, whereas elongating spermatids still included PABPC1.

    Characterization of two cytoplasmic poly(A)-binding proteins, PABPC1 and PABPC2, in mouse spermatogenic cells.
    Kimura M, Ishida K, Kashiwabara S, Baba T.

    01/21/2010
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