Coat proteins play multiple roles in the life cycle of a membrane-bound transport intermediate, functioning in lipid bilayer remodeling, cargo selection and targeting to an acceptor compartment. The Coat Protein complex II (COPII) coat is known to act in each of these capacities, but recent work highlights the necessity for numerous accessory factors at all stages of transport carrier existence. Here, we review recent findings that highlight the roles of COPII and its regulators in the biogenesis of tubular COPII-coated carriers in mammalian cells that enable cargo transport between the endoplasmic reticulum and ER-Golgi intermediate compartments, the first step in a series of trafficking events that ultimately allows for the distribution of biosynthetic secretory cargoes throughout the entire endomembrane system.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6640837 | PMC |
| http://dx.doi.org/10.1111/tra.12654 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Multifunctional Roles of Sec13 Paralogues in the Euglenozoan .
bioRxiv
December 2024
Department of Microbiology and Immunology, Jacobs School of Medicine and Biomedical Sciences, University at Buffalo, 955 Main Street, Buffalo NY 14203.
Secretory cargos are exported from the ER via COPII coated vesicles that have an inner matrix of Sec23/Sec24 heterotetramers and an outer cage of Sec13/Sec31 heterotetramers. In addition to COPII, Sec13 is part of the nuclear pore complex (NPC) and the regulatory SEA/GATOR complex in eukaryotes, which typically have one Sec13 orthologue. The kinetoplastid parasite has two paralogues: TbSec13.
View Article and Find Full Text PDFCompromised COPII vesicle trafficking leads to glycogenic hepatopathy.
Dis Model Mech
September 2024
Research Center for Life Sciences Computing, Zhejiang Laboratory, Hangzhou 311100, China.
Being a vital cellular process, coat protein complex II (COPII) vesicle trafficking has been found to play a crucial role in liver metabolism. However, its functions and the underlying mechanisms in systemic metabolic homeostasis have not been fully understood. Here, with a newly identified gene trap zebrafish line (sec31anju221), we show that compromised COPII vesicle trafficking leads to biphasic abnormal hepatic metabolism.
View Article and Find Full Text PDFDelineating the shape of COat Protein complex-II coated membrane bud.
PNAS Nexus
August 2024
Department of Chemistry, Boston University, Boston, MA 02215, USA.
Curvature-generating proteins that direct membrane trafficking assemble on the surface of lipid bilayers to bud transport intermediates, which move protein and lipid cargoes from one cellular compartment to another. However, it remains unclear what controls the overall shape of the membrane bud once curvature induction has begun. In vitro experiments showed that excessive concentrations of the COPII protein Sar1 promoted the formation of membrane tubules from synthetic vesicles, while COPII-coated transport intermediates in cells are generally more spherical or lobed in shape.
View Article and Find Full Text PDFIdentification and characterization of the COPII vesicle-forming GTPase Sar1 in .
Plant Direct
June 2024
Max-Planck-Institut für Molekulare Pflanzenphysiologie Potsdam Germany.
Eukaryotic cells are highly compartmentalized, requiring elaborate transport mechanisms to facilitate the movement of proteins between membrane-bound compartments. Most proteins synthesized in the endoplasmic reticulum (ER) are transported to the Golgi apparatus through COPII-mediated vesicular trafficking. Sar1, a small GTPase that facilitates the formation of COPII vesicles, plays a critical role in the early steps of this protein secretory pathway.
View Article and Find Full Text PDFStage-Specific COPII-Mediated Cargo Selectivity in African Trypanosomes.
mSphere
August 2022
Department of Microbiology and Immunology, Jacobs School of Medicine and Biomedical Sciences, University at Buffalo, Buffalo, New York, USA.
Article Synopsis
- Eukaryotic cells have a secretory pathway that facilitates the transport of proteins between cellular compartments, particularly from the endoplasmic reticulum to the Golgi apparatus via COPII vesicles.
- In African trypanosomes, two forms of the proteins Sec23 and Sec24 form necessary complexes for transporting specific proteins, like GPI-anchored proteins (GPI-APs), which differ in function between their bloodstream form (BSF) and procyclic form (PCF).
- Research indicates that these proteins are essential for maintaining protein trafficking processes across different life stages of the trypanosomes, revealing adaptations that optimize their secretory pathways for varying environments.
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!