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    The Ca2+-binding protein sorcin stimulates transcriptional activity of the unfolded protein response mediator ATF6

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    Author
    Parks, Steven Z
    Gao, Tian
    Jimenez Awuapura, Natalia
    Ayathamattam, Joseph
    Chabosseau, Pauline L
    Kalvakolanu, Dhananjaya V
    Valdivia, Héctor H
    Rutter, Guy A
    Leclerc, Isabelle
    Date
    2021-05-07
    Journal
    FEBS Letters
    Publisher
    Wiley-Blackwell
    Type
    Article
    
    Metadata
    Show full item record
    See at
    https://doi.org/10.1002/1873-3468.14101
    Abstract
    Sorcin is a calcium-binding protein involved in maintaining endoplasmic reticulum (ER) Ca2+ stores. We have previously shown that overexpressing sorcin under the rat insulin promoter was protective against high-fat diet-induced pancreatic beta-cell dysfunction in vivo. Activating transcription factor 6 (ATF6) is a key mediator of the unfolded protein response (UPR) that provides cellular protection during the progression of ER stress. Here, using nonexcitable HEK293 cells, we show that sorcin overexpression increased ATF6 signalling, whereas sorcin knock out caused a reduction in ATF6 transcriptional activity and increased ER stress. Altogether, our data suggest that sorcin downregulation during lipotoxic stress may prevent full ATF6 activation and a normal UPR during the progression of obesity and insulin resistance.
    Rights/Terms
    © 2021 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.
    Keyword
    ATF6
    ER stress
    lipotoxicity
    sorcin
    Identifier to cite or link to this item
    http://hdl.handle.net/10713/15887
    ae974a485f413a2113503eed53cd6c53
    10.1002/1873-3468.14101
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