COPI budding within the Golgi stack
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Updated: May 30, 2026

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
Published on: August 10, 2017
Vincent Popoff1, Frank Adolf, Britta Brügger
1Heidelberg University Biochemistry Center, 69120 Heidelberg, Germany.
Abstract:
The Golgi serves as a hub for intracellular membrane traffic in the eukaryotic cell. Transport within the early secretory pathway, that is within the Golgi and from the Golgi to the endoplasmic reticulum, is mediated by COPI-coated vesicles. The COPI coat shares structural features with the clathrin coat, but differs in the mechanisms of cargo sorting and vesicle formation. The small GTPase Arf1 initiates coating on activation and recruits en bloc the stable heptameric protein complex coatomer that resembles the inner and the outer shells of clathrin-coated vesicles. Different binding sites exist in coatomer for membrane machinery and for the sorting of various classes of cargo proteins. During the budding of a COPI vesicle, lipids are sorted to give a liquid-disordered phase composition. For the release of a COPI-coated vesicle, coatomer and Arf cooperate to mediate membrane separation.
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