Proteins synthesized in the endoplasmic reticulum (ER) are transported to the Golgi apparatus and then sorted to their destinations. For their passage through the Golgi apparatus, one widely accepted mechanism is cisternal maturation. Cisternal maturation is fulfilled by the retrograde transport of Golgi resident proteins from later to earlier cisternae, and candidate carriers for this retrograde transport are COPI-coated vesicles. We examined the COPI function in cisternal maturation directly by 4D observation of the transmembrane Golgi resident proteins in living yeast cells. COPI temperature-sensitive mutants and induced degradation of COPI proteins were used to knock down COPI function. By either way, inactivation of COPI subunits Ret1 and Sec21 markedly impaired the transition from cis to medial and to trans cisternae. Furthermore, the movement of cisternae within the cytoplasm was severely restricted when COPI subunits were depleted. Our results demonstrate the essential roles of COPI proteins in retrograde trafficking of the Golgi resident proteins and dynamics of the Golgi cisternae.
- Received June 2, 2016.
- Accepted July 15, 2016.
- © 2016. Published by The Company of Biologists Ltd