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    Exostosin-1 Glycosyltransferase Regulates Endoplasmic Reticulum Architecture and Dynamics

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    Name:
    2020.09.02.275925v1.full.pdf
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    PDF
    Description:
    pre-print
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    Type
    Preprint
    Authors
    Kerselidou, Despoina
    Dohai, Bushra Saeed
    Nelson, David R
    Daakour, Sarah
    De Cock, Nicolas
    Kim, Dae-Kyum
    Olivet, Julien
    El Assal, Diana C
    Jaiswal, Ashish
    Saha, Deeya
    Pain, Charlotte
    Matthijssens, Filip
    Lemaitre, Pierre
    Herfs, Michael
    Chapuis, Julien
    Ghesquiere, Bart
    Vertommen, Didier
    Kriechbaumer, Verena
    Knoops, Kevin
    Lopez-Iglesias, Carmen
    van Zandvoort, Marc
    Lambert, Jean-Charles
    Hanson, Julien
    Desmet, Christophe
    Thiry, Marc
    Lauersen, Kyle J. cc
    Vidal, Marc
    Van Vlierberghe, Pieter
    Dequiedt, Franck
    Salehi-Ashtiani, Kourosh
    Twizere, Jean-Claude
    KAUST Department
    Biological and Environmental Sciences and Engineering (BESE) Division
    Date
    2020-09-03
    Permanent link to this record
    http://hdl.handle.net/10754/665119
    
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    Abstract
    The endoplasmic reticulum (ER) is a central eukaryotic organelle with a tubular network made of hairpin proteins linked by hydrolysis of GTP nucleotides. Among post-translational modifications initiated at the ER level, glycosylation is the most common reaction. However, our understanding of the impact of glycosylation on ER structure remains unclear. Here, we show that Exostosin-1 (EXT1) glycosyltransferase, an enzyme involved in N-glycosylation, is a key regulator of ER morphology and dynamics. We have integrated multi-omics data and super-resolution imaging to characterize the broad effect of EXT1 inactivation, including ER shape-dynamics-function relationships in mammalian cells. We have observed that, inactivating EXT1 induces cell enlargement and enhances metabolic switches such as protein secretion. In particular, suppressing EXT1 in mouse thymocytes causes developmental dysfunctions associated to ER network extension. Our findings suggest that EXT1 drives glycosylation reactions involving ER structural proteins and high-energy nucleotide sugars, which might also apply to other organelles.
    Citation
    Kerselidou, D., Dohai, B. S., Nelson, D. R., Daakour, S., De Cock, N., Kim, D.-K., … Twizere, J.-C. (2020). Exostosin-1 Glycosyltransferase Regulates Endoplasmic Reticulum Architecture and Dynamics. doi:10.1101/2020.09.02.275925
    Publisher
    Cold Spring Harbor Laboratory
    DOI
    10.1101/2020.09.02.275925
    Additional Links
    http://biorxiv.org/lookup/doi/10.1101/2020.09.02.275925
    ae974a485f413a2113503eed53cd6c53
    10.1101/2020.09.02.275925
    Scopus Count
    Collections
    Biological and Environmental Science and Engineering (BESE) Division; Preprints

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