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Vesicle and tubule transport containers move proteins and lipids from one membrane system to another. Newly forming transport containers frequently have electron-dense coats. Coats coordinate the accumulation of cargo and sculpt the membrane. Recent advances have shown that components of both COP1 and clathrin-adaptor coats share the same structure and the same motif-based cargo recognition and accessory factor recruitment mechanisms, which leads to insights on conserved aspects of coat recruitment, polymerisation and membrane deformation. These themes point to the way in which evolutionarily conserved features underpin these diverse pathways.

Original publication

DOI

10.1016/j.ceb.2004.06.009

Type

Journal article

Journal

Curr Opin Cell Biol

Publication Date

08/2004

Volume

16

Pages

379 - 391

Keywords

ADP-Ribosylation Factor 1, Adaptor Proteins, Vesicular Transport, Animals, Biological Transport, COP-Coated Vesicles, Clathrin, Clathrin-Coated Vesicles, Coat Protein Complex I, Coated Pits, Cell-Membrane, Endoplasmic Reticulum, Humans, Models, Biological, Protein Structure, Tertiary