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    The RNA-binding protein FUS/TLS undergoes calcium-mediated nuclear egress during excitotoxic stress and is required for GRIA2 mRNA processing

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    J._Biol._Chem._2019_Tischbein_ ...
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    Authors
    Tischbein, Maeve
    Baron, Desiree M.
    Lin, Yen-Chen
    Gall, Katherine V.
    Landers, John E.
    Fallini, Claudia
    Bosco, Daryl A.
    UMass Chan Affiliations
    Graduate School of Biomedical Sciences
    Department of Neurology
    Document Type
    Journal Article
    Publication Date
    2019-05-15
    Keywords
    RNA transport
    amyotrophic lateral sclerosis (ALS) (Lou Gehrig disease)
    excitatory neurotransmission
    excitotoxicity
    fused in sarcoma/translocated in liposarcoma (FUS/TLS)
    glutamate
    glutamate ionotropic receptor AMPA type subunit 2 (Gria2)
    glutamate receptor 2 (GluA2)
    neurodegeneration
    nucleocytoplasmic transport
    Amino Acids, Peptides, and Proteins
    Biochemistry
    Molecular Biology
    Nervous System Diseases
    Neuroscience and Neurobiology
    Nucleic Acids, Nucleotides, and Nucleosides
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    Abstract
    Excitotoxic levels of glutamate represent a physiological stress that is strongly linked to amyotrophic lateral sclerosis (ALS) and other neurological disorders. Emerging evidence indicates a role for neurodegenerative disease-linked RNA-binding proteins (RBPs) in the cellular stress response. However, the relationships between excitotoxicity, RBP function, and disease have not been explored. Here, using primary cortical and motor neurons, we found that excitotoxicity induced the translocation of select ALS-linked RBPs from the nucleus to the cytoplasm within neurons. RBPs affected by excitotoxicity included TAR DNA-binding protein 43 (TDP-43) and, most robustly, fused in sarcoma/translocated in liposarcoma (FUS/TLS). We noted that FUS is translocated through a calcium-dependent mechanism and that its translocation coincides with striking alterations in nucleocytoplasmic transport. Further, glutamate-induced up-regulation of glutamate ionotropic receptor AMPA type subunit 2 (GRIA2) in neurons depended on FUS expression, consistent with a functional role for FUS in excitotoxic stress. These findings reveal molecular links among prominent factors in neurodegenerative diseases, namely excitotoxicity, disease-associated RBPs, and nucleocytoplasmic transport.
    Source

    J Biol Chem. 2019 May 15. pii: jbc.RA118.005933. doi: 10.1074/jbc.RA118.005933. [Epub ahead of print] Link to article on publisher's site

    DOI
    10.1074/jbc.RA118.005933
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/41060
    PubMed ID
    31092554
    Related Resources

    Link to Article in PubMed

    Rights
    © 2019 by The American Society for Biochemistry and Molecular Biology, Inc. Publisher PDF posted after 12 months as allowed by the publisher's author rights policy at http://www.jbc.org/site/misc/edpolicy.xhtml#copyright.
    ae974a485f413a2113503eed53cd6c53
    10.1074/jbc.RA118.005933
    Scopus Count
    Collections
    Morningside Graduate School of Biomedical Sciences Scholarly Publications
    UMass Chan Faculty and Researcher Publications

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