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Home / The cell / Vesicular trafficking / From the reticulum to the Golgi (summary)

The cell. 5. Vesicular trafficking

From the RETICULUM to the GOLGI

Summary Content

The endoplasmic reticulum mostly communicates with the Golgi apparatus by vesicular trafficking. Most proteins and lipids leaving the endoplasmic reticulum are enclosed in vesicles or are components of the vesicular membrane. The vesicles are formed in specialized regions known as exit zones (Figure 1).

From the ER to the Golgi apparatus
Figure 1. COPII (coat protein II) vesicles are released from the exit zones of the endoplasmic reticulum, are moved away, and fuse between each other, forming the ERGIC (endoplasmic reticulum-Golgi intermediate compartment), which is moved toward the cis domain of the Golgi apparatus. In the cis domain of the Golgi apparatus, all the ERGIC bodies and some vesicles from the endoplasmic reticulum coming from different parts of the cell form the cis cisterns of the Golgi apparatus. At the same time, from the ERGIC and cis cisterns, COPI coated vesicles are released and travel back toward the endoplasmic reticulum in a recycling process.
Vesicles
Vesicles

COPII proteins are involved in the formation of vesicles in the endoplasmic reticulum. They are assembled in the exit zones and perform two functions: vesicle formation and cargo selection. These cargoes are proteins to be included and transported in the vesicle.

COPII vesicles lose part of their protein coat and fuse to one another to form the ERGIC (endoplasmic reticulum-Golgi intermediate compartment). It is a tubule-vesicular compartment that is moved toward the cis domain of the Golgi apparatus by motor proteins and microtubules (cytoskeleton components). Then, the ERGIC becomes cis domain cisterns (Figure 1).

During this process, in the ERGIC and Golgi apparatus, other vesicles are formed. These are the COPI coated vesicles, which select cargoes to be transported back to the endoplasmic reticulum. It is a recycling pathway that brings back proteins that escaped from the endoplasmic reticulum into COPII vesicles. These proteins actually perform their function in the endoplasmic reticulum and are known as resident proteins.

KDEL receptors are involved in the recognition and selection of resident proteins to be included in COPI vesicles. KDEL receptors travel back to the endoplasmic reticulum and release the cargoes. Then, KDEL receptors are included in COPII vesicles and transported to the ERGIC-Golgi apparatus. Thus, KDEL receptors alternate between the endoplasmic reticulum and the ERGIC-Golgi apparatus, bringing back resident proteins. The mechanism for binding a cargo in one organelle and releasing it in the other is based on the pH differences between both compartments. The pH is more basic in the endoplasmic reticulum than in the ERGIC-Golgi apparatus. The affinity of KDEL for its cargoes is higher in basic environments (binds the cargo) and lower in acid ones (releases the cargo).

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