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Lectins and traffic in the secretory pathway
H Hauri1, C Appenzeller, F Kuhn
1Department of Pharmacology, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056, Basel, Switzerland. hans-peter.hauri@unibas.cy
FEBS Letters
|July 6, 2000
Summary
Intracellular animal lectins, including calnexin and ERGIC-53, are crucial for glycoprotein quality control and transport within the secretory pathway. These lectins ensure proper protein folding and sorting from the endoplasmic reticulum to the Golgi apparatus and beyond.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Intracellular animal lectins are increasingly recognized for their critical roles in cellular quality control mechanisms.
- Glycoproteins require precise folding and sorting for proper function within the secretory pathway.
Purpose of the Study:
- To review the functions of key intracellular lectins involved in glycoprotein traffic.
- To highlight the roles of calnexin, calreticulin, ERGIC-53, and VIP36 in protein quality control and sorting.
Main Methods:
- Literature review and synthesis of existing research on intracellular lectins and glycoprotein trafficking.
- Discussion of experimental evidence implicating specific lectins in endoplasmic reticulum and Golgi functions.
Main Results:
- Calnexin and calreticulin facilitate glycoprotein folding and oligomerization in the endoplasmic reticulum.
- ERGIC-53 acts as a mannose lectin cargo receptor for glycoprotein transport from the ER to the Golgi.
- VIP36 may be involved in glycosylation quality control within the Golgi apparatus.
Conclusions:
- Intracellular lectins are essential regulators of glycoprotein processing and transport.
- These lectins mediate critical steps in the secretory pathway, ensuring the fidelity of glycoprotein maturation and delivery.