Journal
MOLECULAR PLANT
Volume 4, Issue 2, Pages 220-228Publisher
CELL PRESS
DOI: 10.1093/mp/ssq082
Keywords
Endomembrane system; Golgi apparatus; glycosylation; glycosyltransferase
Categories
Funding
- Austrian Science Fund [P19494, 20817, J2981-B20]
- Austrian Science Fund (FWF) [P19494] Funding Source: Austrian Science Fund (FWF)
- Austrian Science Fund (FWF) [P 20817] Funding Source: researchfish
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In all eukaryotes, the Golgi apparatus is the main site of protein glycosylation. It is widely accepted that the glycosidases and glycosyltransferases involved in N-glycan processing are found concentrated within the Golgi stack where they provide their function. This means that enzymes catalyzing early steps in the processing pathway are located mainly at the cis-side, whereas late-acting enzymes mostly locate to the trans-side of the stacks, creating a non-uniform distribution along the cis-trans axis of the Golgi. There is compelling evidence that the information for their sorting to specific Golgi cisternae depends on signals encoded in the proteins themselves as well as on the trafficking machinery that recognizes these signals and it is believed that cisternal sub-compartmentalization is achieved and maintained by a combination of retention and retrieval mechanisms. Yet, the signals, mechanism(s), and molecular factors involved are still unknown. Here, we address recent findings and summarize the current understanding of this fundamental process in plant cell biology.
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