COPI and COPII-coated vesicles bud directly from the endoplasmic reticulum in yeast

Article Abstract:

The yeast coatomer proteins I and II (COPI and COPII) induce the formation of separate secretory vesicles from the endoplasmic reticulum (ER). The two types of vesicles contain targeting proteins essential for docking at the Golgi complex. Neither the COPI nor COPII vesicles possess ER resident proteins, but they contain a GTP-binding protein and a membrane nucleotide exchange factor. The formation of COPI vesicles is inhibited by brefeldin A, while the COPII vesicle formation remains unaffected.

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Does COPI go both ways?

Article Abstract:

The role of vesicles in protein transport within the eukaryotic cell is to ferry cargo proteins along well-defined routes of membrane traffic. A complex, known as coatomer, has been characterized as the one responsible for COPI-coated vesicle formation. Several experiments have been suggested to demonstrate that transport through the Golgi stack relies on both anterograde vesicular traffic and cisternal progression.

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Protein sorting upon exit from the endoplasmic reticulum

Article Abstract:

Research has been conducted on the GPI-anchored proteins transporting from the endoplasmic reticulum to the Golgi apparatus in yeast. Results indicate that the GPI-anchored proteins exit the endoplasmic reticulum in distinct vesicles and need to be sorted from the other plasma membrane proteins at the early stage of the secretory pathway.

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