| Structural highlightsFunctionSEC23_YEAST Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. SEC23 interacts with BET3 in order to target TRAPPI complex to COPII involved in internalisation of plasma membrane proteins like the maltose transporter.[1] [2] [3] [4] [5] [6] [7] [8] [9] [10] [11] [12] [13] [14] [15] [16] [17] [18] [19] [20] [21] [22]
Publication Abstract from PubMed
Coat protein complex II (COPII) mediates formation of the membrane vesicles that export newly synthesised proteins from the endoplasmic reticulum. The inner COPII proteins bind to cargo and membrane, linking them to the outer COPII components that form a cage around the vesicle. Regulated flexibility in coat architecture is essential for transport of a variety of differently sized cargoes, but structural data on the assembled coat has not been available. We have used cryo-electron tomography and subtomogram averaging to determine the structure of the complete, membrane-assembled COPII coat. We describe a novel arrangement of the outer coat and find that the inner coat can assemble into regular lattices. The data reveal how coat subunits interact with one another and with the membrane, suggesting how coordinated assembly of inner and outer coats can mediate and regulate packaging of vesicles ranging from small spheres to large tubular carriers. DOI:http://dx.doi.org/10.7554/eLife.00951.001.
The structure of the COPII transport-vesicle coat assembled on membranes.,Zanetti G, Prinz S, Daum S, Meister A, Schekman R, Bacia K, Briggs JA Elife. 2013 Sep 17;2:e00951. doi: 10.7554/eLife.00951. PMID:24062940[23]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
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- ↑ Zanetti G, Prinz S, Daum S, Meister A, Schekman R, Bacia K, Briggs JA. The structure of the COPII transport-vesicle coat assembled on membranes. Elife. 2013 Sep 17;2:e00951. doi: 10.7554/eLife.00951. PMID:24062940 doi:http://dx.doi.org/10.7554/eLife.00951
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