Journal
CELLS
Volume 9, Issue 12, Pages -Publisher
MDPI
DOI: 10.3390/cells9122652
Keywords
glycosylation; Golgi; GOLPH3; GORAB; oligomeric golgi complex
Categories
Funding
- Fondazione AIRC per la Ricerca sul Cancro (IG2017) [20779]
- Fondazione Italiana per la Ricerca sul Cancro-Fondazione AIRC per la Ricerca sul Cancro [19686]
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Glycosylation is the most common post-translational modification of proteins; it mediates their correct folding and stability, as well as their transport through the secretory transport. Changes in N- and O-linked glycans have been associated with multiple pathological conditions including congenital disorders of glycosylation, inflammatory diseases and cancer. Glycoprotein glycosylation at the Golgi involves the coordinated action of hundreds of glycosyltransferases and glycosidases, which are maintained at the correct location through retrograde vesicle trafficking between Golgi cisternae. In this review, we describe the molecular machinery involved in vesicle trafficking and tethering at the Golgi apparatus and the effects of mutations in the context of glycan biosynthesis and human diseases.
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