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    Combinatorial multivalent interactions drive cooperative assembly of the COPII coat

    Stancheva, V.G. and Li, X.-H. and Hutchings, Joshua and Gomez-Navarro, N. and Santhanam, B. and Babu, M. and Zanetti, Giulia and Miller, E.A. (2020) Combinatorial multivalent interactions drive cooperative assembly of the COPII coat. Journal of Cell Biology 219 (11), e202007135. ISSN 0021-9525.

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    Protein secretion is initiated at the endoplasmic reticulum by the COPII coat, which self-assembles to form vesicles. Here, we examine the mechanisms by which a cargo-bound inner coat layer recruits and is organized by an outer scaffolding layer to drive local assembly of a stable structure rigid enough to enforce membrane curvature. An intrinsically disordered region in the outer coat protein, Sec31, drives binding with an inner coat layer via multiple distinct interfaces, including a newly defined charge-based interaction. These interfaces combinatorially reinforce each other, suggesting coat oligomerization is driven by the cumulative effects of multivalent interactions. The Sec31 disordered region could be replaced by evolutionarily distant sequences, suggesting plasticity in the binding interfaces. Such a multimodal assembly platform provides an explanation for how cells build a powerful yet transient scaffold to direct vesicle traffic.


    Item Type: Article
    School: Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences
    Research Centres and Institutes: Structural Molecular Biology, Institute of (ISMB)
    Depositing User: Giulia Zanetti
    Date Deposited: 08 Oct 2020 12:19
    Last Modified: 02 Aug 2023 18:04


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