Structure of the Sec13/31 COPII coat cage View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2006-01

AUTHORS

Scott M. Stagg, Cemal Gürkan, Douglas M. Fowler, Paul LaPointe, Ted R. Foss, Clinton S. Potter, Bridget Carragher, William E. Balch

ABSTRACT

Endomembranes of eukaryotic cells are dynamic structures that are in continuous communication through the activity of specialized cellular machineries1, such as the coat protein complex II (COPII), which mediates cargo export from the endoplasmic reticulum (ER)2,3. COPII consists of the Sar1 GTPase, Sec23 and Sec24 (Sec23/24), where Sec23 is a Sar1-specific GTPase-activating protein and Sec24 functions in cargo selection, and Sec13 and Sec31 (Sec13/31), which has a structural role3. Whereas recent results have shown that Sec23/24 and Sec13/31 can self-assemble to form COPII cage-like particles4, we now show that Sec13/31 can self-assemble to form minimal cages in the absence of Sec23/24. We present a three-dimensional reconstruction of these Sec13/31 cages at 30 Å resolution using cryo-electron microscopy and single particle analysis. These results reveal a novel cuboctahedron geometry with the potential to form a flexible lattice and to generate a diverse range of containers. Our data are consistent with a model for COPII coat complex assembly in which Sec23/24 has a non-structural role as a multivalent ligand localizing the self-assembly of Sec13/31 to form a cage lattice driving ER cargo export. More... »

PAGES

234-238

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nature04339

DOI

http://dx.doi.org/10.1038/nature04339

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1007438875

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/16407955


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