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Organization of the ER–Golgi interface for membrane traffic control

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TLDR
Comparison of the ER–Golgi interface across different systems, particularly mammalian and plant cells, reveals fundamental elements and distinct organization of this interface that should provide key insights into the mechanisms that control efficient trafficking of proteins and lipids through the secretory pathway.
Abstract
Coat protein complex I (COPI) and COPII are required for bidirectional membrane trafficking between the endoplasmic reticulum (ER) and the Golgi. While these core coat machineries and other transport factors are highly conserved across species, high-resolution imaging studies indicate that the organization of the ER-Golgi interface is varied in eukaryotic cells. Regulation of COPII assembly, in some cases to manage distinct cellular cargo, is emerging as one important component in determining this structure. Comparison of the ER-Golgi interface across different systems, particularly mammalian and plant cells, reveals fundamental elements and distinct organization of this interface. A better understanding of how these interfaces are regulated to meet varying cellular secretory demands should provide key insights into the mechanisms that control efficient trafficking of proteins and lipids through the secretory pathway.

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References
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Journal ArticleDOI

The Unfolded Protein Response: From Stress Pathway to Homeostatic Regulation

TL;DR: The vast majority of proteins that a cell secretes or displays on its surface first enter the endoplasmic reticulum, where they fold and assemble, and only properly assembled proteins advance from the ER to the cell surface.
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Structural models of primary cell walls in flowering plants: consistency of molecular structure with the physical properties of the walls during growth

TL;DR: This review integrates information on the chemical structure of individual polymers with data obtained from new techniques used to probe the arrangement of the polymers within the walls of individual cells consistent with the physical properties of the wall and its components.
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SNAREpins: Minimal Machinery for Membrane Fusion

TL;DR: Recombinant v- and t- SNARE proteins reconstituted into separate lipid bilayer vesicles assemble into SNAREpins-SNARE complexes linking two membranes, leading to spontaneous fusion of the docked membranes at physiological temperature.
Journal ArticleDOI

The Mechanisms of Vesicle Budding and Fusion

TL;DR: Genetic and biochemical analyses of the secretory pathway have produced a detailed picture of the molecular mechanisms involved in selective cargo transport between organelles, including Vesicle budding and cargo selection, which depend on a machinery that includes the SNARE proteins.
Journal ArticleDOI

Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: evidence for membrane cycling from Golgi to ER.

TL;DR: It is suggested that BFA disrupts a dynamic membrane-recycling pathway between the ER and cis/medial Golgi, effectively blocking membrane transport out of but not back to the ER.
Related Papers (5)
Trending Questions (1)
Is the ER MEMBRANE PROTEIN COMPLEX involved in membrane traffic?

Yes, the ER membrane protein complex, specifically COPI and COPII, is crucial for bidirectional membrane trafficking between the endoplasmic reticulum (ER) and the Golgi, as highlighted in the research paper.