Yeast cytosolic coat proteins (COPII) direct the formation of vesicles from the endoplasmic
reticulum. The vesicles selectively capture both cargo molecules and the secretory …

Forward and retrograde trafficking of secretory proteins between the endoplasmic reticulum
and the Golgi apparatus is driven by two biochemically distinct vesicle coats, COPI and …

Secretory proteins are transported to the Golgi complex in vesicles that bud from the
endoplasmic reticulum. The cytoplasmic coat protein complex II (COPII) is responsible for …

Secretory proteins are transported from the endoplasmic reticulum (ER) to the Golgi complex
in vesicles coated with coat protein complex II (COPII). The incorporation of certain transport …

Protein trafficking is achieved by a bidirectional vesicle flow between the various
compartments of the eukaryotic cell. COPII coated vesicles mediate anterograde protein …

The major cytosolic and membrane proteins that represent machinery of coat protein (COP)-
coated transport vesicles within the secretory pathway are characterized to date. This has …

Export of many secretory proteins from the endoplasmic reticulum (ER) relies on signal-
mediated sorting into ER-derived transport vesicles. Recent work on the coat protein …

The coat complex COPII forms vesicles at the endoplasmic reticulum to transport a variety of
cargo proteins to the Golgi structure. Recent biochemical and structural studies reveal the …

Communication between compartments of the exocytic and endocytic pathways in
eukaryotic cells involves transport carriers—vesicles and tubules—that mediate the vectorial …

First discovered by genetic analysis of yeast secretion mutants, the evolutionarily conserved
vesicular coat protein II (COPII) complex is responsible for membrane transport from the …