Cisternal Maturation and COPI

One of the fundamental processes that explains how protein is transported from the endoplasmic reticulum to the golgi bodies and then transferred to other locations is sternal maturation. The concept behind the transport is that golgi cisternae gradually convert into anterograde carriers for secretory transfer of protein. It proceeds through the golgi stack when a new cistern forms, changing as it matures due to the buildup of medial and trans enzymes via vesicles that travel from one cisternae to the next. The aim of the article was to examine the function of coat protein complex 1 (COPI)-coated vesicles in cisternal maturation. COPI-coated vesicles play a role in backward transportation carriers of golgi-resident proteins. Although COPI has a fundamental function in golgi-ER retrograde transport, the role of COPI-coated vesicles in backward cargo transportation is contentious. Midori et al (2016) observed the cisternal maturation using 4D observation of the transmembrane golgi-resident protein in a living yeast cell. Golgi-resident makers were used to observe the cisternal maturation of the golgi. In order to observe COPI function, the researchers used COPI temperature-sensitive mutants and induced degradation of COPI proteins to reduce the expression of COPI function. Cells without COPI have insufficient COPI proteins to recycle golgi-resident proteins, which led to the fixation of intermediate cisternae in the maturation process. Ishii, Suda, Kurokawa, and Nakano (2016) concluded that the core function of COPI proteins in retrograde transportation of the Golgi-resident proteins and dynamics of the golgi cisternae.





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References

Ishii M., Suda Y., Kurokawa K & Nakano A (2016). COPI Is Essential for Golgi Cisternal Maturation and Dynamics. Journal of Cell Science (2016) 129, 325-61.