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Gewählte Publikation:

Strasser, R.
(2009): Localization of plant N-glycan processing enzymes along the secretory pathway
PLANT BIOSYST. 2009; 143(3): 636-642. FullText FullText_BOKU

Abstract:
N-glycosylation is an abundant covalent protein modification in all eukaryotic cells. The biosynthesis and processing of protein N-linked glycans results from a series of highly co-ordinated step-by-step enzymatic conversions occurring mainly in the endoplasmic reticulum (ER) and Golgi apparatus. N-glycan processing enzymes are thought to act on cargo glycoproteins in a highly ordered fashion in an assembly line. Thus, the subcellular localization of these enzymes together with their in vivo substrate specificity determines the carbohydrate structures of glycoproteins transported through the secretory pathway. While the substrate specificities of many plant N-glycan processing enzymes are fairly well characterized, the molecular mechanisms underlying enzyme localization to the ER and Golgi have remained largely elusive so far. This review discusses current data on ER and Golgi localization of plant N-glycan processing enzymes.
Autor*innen der BOKU Wien:
Strasser Richard

Find related publications in this database (Keywords)
ER exit
glycosidase
glycosyltransferase
Golgi targeting
N-glycosylation


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