Glycosylation and protein transport

Transport along the secretory pathway is largely signal-mediated. Proteins in the secretory pathway can be covalently modified with various carbohydrate structures, most commonly O-glycans, N-glycans and/or proteoglycans. Carbohydrate modifications can change the physical properties of proteins or c...

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Bibliographic Details
Published inEssays in biochemistry Vol. 36; p. 27
Main Authors Scheiffele, P, Füllekrug, J
Format Journal Article
LanguageEnglish
Published England 01.01.2000
Subjects
Animals
Cell Polarity - physiology
Glycoproteins - metabolism
Glycosylation
Golgi Apparatus - metabolism
Humans
Protein Transport - physiology
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Summary:Transport along the secretory pathway is largely signal-mediated. Proteins in the secretory pathway can be covalently modified with various carbohydrate structures, most commonly O-glycans, N-glycans and/or proteoglycans. Carbohydrate modifications can change the physical properties of proteins or can function as specific recognition epitopes. Glycosylation can act as an apical sorting signal in polarized epithelial cells and provide a signal for surface transport in non-polarized fibroblasts. Homologues of leguminous plant lectins have been identified in yeast, fruitflies, worms and humans. Intracellular lectins are candidate receptors in the secretory pathway to mediate concentration of cargo in carrier vesicles.
ISSN:0071-1365
DOI:10.1042/bse0360027