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Glycosylation and protein transport
1Department of Biochemistry and Biophysics, Howard Hughes Medical Institute, University of California, San Francisco, CA 94143-0452, USA. Scheiffe@uclink4.berkeley.edu
Essays in Biochemistry
|December 11, 2002
Summary
Protein glycosylation, including O-glycans and N-glycans, influences transport in the secretory pathway. Intracellular lectins may act as receptors, concentrating cargo for vesicle transport.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Protein transport in the secretory pathway is primarily signal-mediated.
- Proteins undergo modifications like glycosylation (O-glycans, N-glycans, proteoglycans).
- Carbohydrate modifications affect protein properties and serve as recognition signals.
Purpose of the Study:
- To investigate the role of glycosylation in protein transport.
- To explore the function of intracellular lectins in the secretory pathway.
- To understand how carbohydrate modifications signal protein sorting and transport.
Main Methods:
- Analysis of protein glycosylation patterns.
- Investigating lectin homologues across species (yeast, fruit flies, worms, humans).
- Studying protein sorting and surface transport in polarized and non-polarized cells.
Main Results:
- Glycosylation acts as an apical sorting signal in epithelial cells.
- Glycosylation signals surface transport in fibroblasts.
- Intracellular lectins are identified as potential cargo receptors.
Conclusions:
- Carbohydrate modifications are crucial for protein trafficking.
- Intracellular lectins are implicated in concentrating cargo for vesicle formation.
- Signal-mediated transport relies on specific protein modifications and receptors.