Glycosylation and protein transport

Scheiffele, P. and Fullekrug, J.. (2000) Glycosylation and protein transport. Essays in Biochemistry, Vol. 36. pp. 27-35.

Full text not available from this repository.

Official URL: http://edoc.unibas.ch/dok/A5259863

Downloads: Statistics Overview


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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Neurobiology > Cell Biology (Scheiffele)
UniBasel Contributors:Scheiffele, Peter
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Portland Press
Note:Publication type according to Uni Basel Research Database: Journal article
Related URLs:
Identification Number:
Last Modified:08 Jun 2012 06:44
Deposited On:22 Mar 2012 13:29

Repository Staff Only: item control page