On vesicle formation and tethering in the ER–Golgi shuttle
A Spang - Current opinion in cell biology, 2009 - Elsevier
Transport in the ER–Golgi shuttle is performed by COPII in the anterograde and by COPI in
the retrograde direction. How these transport steps are regulated and which mechanisms act …
the retrograde direction. How these transport steps are regulated and which mechanisms act …
Differential ER exit in yeast and mammalian cells
R Watanabe, H Riezman - Current opinion in cell biology, 2004 - Elsevier
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 …
cargo proteins to the Golgi structure. Recent biochemical and structural studies reveal the …
[HTML][HTML] Mechanisms for exporting large-sized cargoes from the endoplasmic reticulum
K Saito, T Katada - Cellular and Molecular Life Sciences, 2015 - Springer
Cargo proteins exported from the endoplasmic reticulum to the Golgi apparatus are typically
transported in coat protein complex II (COPII)-coated vesicles of 60–90 nm diameter …
transported in coat protein complex II (COPII)-coated vesicles of 60–90 nm diameter …
Selective packaging of cargo molecules into endoplasmic reticulum-derived COPII vesicles
JL Campbell, R Schekman - Proceedings of the National …, 1997 - National Acad Sciences
Coated vesicles transport proteins from the endoplasmic reticulum (ER) to the Golgi
apparatus. The formation of transport vesicles in vitro requires the incubation of an ER …
apparatus. The formation of transport vesicles in vitro requires the incubation of an ER …
Nucleation of COPII vesicular coat complex by endoplasmic reticulum to Golgi vesicle SNAREs
S Springer, R Schekman - Science, 1998 - science.org
Protein trafficking from the endoplasmic reticulum (ER) to the Golgi apparatus involves
specific uptake into coat protein complex II (COPII)–coated vesicles of secretory and of …
specific uptake into coat protein complex II (COPII)–coated vesicles of secretory and of …
COPII and the regulation of protein sorting in mammals
G Zanetti, KB Pahuja, S Studer, S Shim… - Nature cell …, 2012 - nature.com
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 …
endoplasmic reticulum. The cytoplasmic coat protein complex II (COPII) is responsible for …
TFG facilitates outer coat disassembly on COPII transport carriers to promote tethering and fusion with ER–Golgi intermediate compartments
MG Hanna IV, S Block, EB Frankel… - Proceedings of the …, 2017 - National Acad Sciences
The conserved coat protein complex II (COPII) mediates the initial steps of secretory protein
trafficking by assembling onto subdomains of the endoplasmic reticulum (ER) in two layers …
trafficking by assembling onto subdomains of the endoplasmic reticulum (ER) in two layers …
[HTML][HTML] ER-to-Golgi protein delivery through an interwoven, tubular network extending from ER
Cellular versatility depends on accurate trafficking of diverse proteins to their organellar
destinations. For the secretory pathway (followed by approximately 30% of all proteins), the …
destinations. For the secretory pathway (followed by approximately 30% of all proteins), the …
[HTML][HTML] Cargo can modulate COPII vesicle formation from the endoplasmic reticulum
M Aridor, SI Bannykh, T Rowe, WE Balch - Journal of Biological Chemistry, 1999 - ASBMB
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 …
critical role in cargo selection. We now address the potential role of biosynthetic cargo in …
COPII-dependent transport from the endoplasmic reticulum
C Barlowe - Current opinion in cell biology, 2002 - Elsevier
The coat protein complex II (COPII) forms transport vesicles from the endoplasmic reticulum
and segregates biosynthetic cargo from ER-resident proteins. Recent high-resolution …
and segregates biosynthetic cargo from ER-resident proteins. Recent high-resolution …