Combinatorial multivalent interactions drive cooperative assembly of the COPII coat.
J Cell Biol
; 219(11)2020 11 02.
Article
em En
| MEDLINE
| ID: mdl-32997735
ABSTRACT
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.
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Base de dados:
MEDLINE
Assunto principal:
Saccharomyces cerevisiae
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Vesículas Revestidas pelo Complexo de Proteína do Envoltório
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Proteínas de Saccharomyces cerevisiae
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Proteínas de Transporte Vesicular
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Retículo Endoplasmático
Idioma:
En
Ano de publicação:
2020
Tipo de documento:
Article