Self-assembly of minimal COPII cages |
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Authors: | Antonny Bruno Gounon Pierre Schekman Randy Orci Lelio |
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Affiliation: | Institut de Pharmacologie Moléculaire et Cellulaire, CNRS, Valbonne, France. antonny@ipmc.cnrs.fr |
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Abstract: | The small G-protein Sar1 and the cytosolic complexes Sec23/24 and Sec13/31 associate sequentially on endoplasmic reticulum membranes to form a protein coat named COPII, which drives the formation of transport vesicles. Using dynamic light scattering, we show that Sec23/24 and Sec13/31 can self-assemble in a stoichiometric manner in solution to form particles with hydrodynamic radii in the range of 40–60 nm. Self-assembly is favoured by lowering the pH, the ionic strength and/or the temperature. Electron microscopy reveals the formation of spherical particles 60–120 nm in diameter with a tight, rough mesh on their surfaces. We suggest that these stuctures, which represent a minimal COPII cage, mimic the molecular organization of the membrane-associated COPII coat. |
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