Membrane proteins exit the endoplasmic reticulum (ER) in COPII-transport vesicles. ER
export is a selective process in which transport signals present in the cytoplasmic tail (CT) of …

Cargo is selectively exported from the ER in COPII vesicles. To analyze the role of COPII in
selective transport from the ER, we have purified components of the mammalian COPII …

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 …

We previously identified Sys1p as a high copy number suppressor of Ypt6 GTPase-deficient
yeast mutants that are defective in endosome-to-Golgi transport. Here, we show that Sys1p …

The selective export of proteins and lipids from the endoplasmic reticulum (ER) is mediated
by the coat protein complex II (COPII) that assembles onto the ER membrane. In higher …

Selective export of transmembrane proteins from the endoplasmic reticulum (ER) relies on
recognition of cytosolic-domain-localized transport signals by the Sec24 subunit of the COPII …

The Sar1 GTPase is an essential component of COPII vesicle coats involved in export of
cargo from the ER. We report the 1.7-Å structure of Sar1 and find that consistent with the …

Cargo selection and export from the endoplasmic reticulum is mediated by the COPII coat
machinery that includes the small GTPase Sar1 and the Sec23/24 and Sec13/31 complexes …

Forward transport of proteins from the endoplasmic reticulum (ER) to the Golgi complex
depends on COPII, a membrane coat that forms ER-derived vesicles. Based on …

Coat protein complex II (COPII) plays an integral role in the packaging of secretory cargoes
within membrane-enclosed transport carriers that leave the endoplasmic reticulum (ER) from …