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 …

A full mechanistic understanding of how secretory cargo proteins are exported from the
endoplasmic reticulum for passage through the early secretory pathway is essential for us to …

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 …

The first step in protein secretion from eukaryotic cells is mediated by COPII vesicles, known
for the cytoplasmic coat proteins that are the minimal machinery required to generate these …

Vesicle trafficking from the endoplasmic reticulum (ER) is a vital cellular process in all
eukaryotes responsible for moving secretory cargoes from the ER to the Golgi apparatus. To …

The COPII coat complex found on endoplasmic reticulum (ER)-derived vesicles plays a
critical role in cargo selection. We now address the potential role of biosynthetic cargo in …

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 protein complex II (COPII) forms transport vesicles from the endoplasmic reticulum
and segregates biosynthetic cargo from ER-resident proteins. Recent high-resolution …

Intracellular transport and homeostasis of the endomembrane system in eukaryotic cells
depend on the formation and fusion of vesicular carriers. Coat protein complex (COP) II …

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