Organization of Golgi Glycosyltransferases in Membranes: Complexity via Complexes

Organization of Golgi Glycosyltransferases in Membranes: Complexity via Complexes J. Membrane Biol. 198, 1–13 (2004) DOI: 10.1007/s00232-004-0656-5 Topical Review W.W. Young, Jr Department of Molecular, Cellular, and Craniofacial Biology, School of Dentistry and Departments of Biochemistry and Molecular Biology and Pharmacology and Toxicology, School of Medicine, University of Louisville, Louisville, KY40292, USA Received: 1 October 2003/Revised: 19 December 2003 Introduction glycosyltransferases destined to become Golgi resi- dents, are recruited as cargo into coat protein COPII- Much of the glycosylation of proteins, lipids, and coated vesicles. As the nascent VTC moves forward, proteoglycans of mammalian cells is catalyzed by it matures to form sequentially the cis, medial, and glycosyltransferases located in the Golgi apparatus. trans Golgi cisternae and finally the trans Golgi This review will summarize recent data that deline- network (TGN). This maturation is accomplished by ates how those glycosyltransferases are organized in the retrograde trafficking of COPI-coated vesicles. membranes during what can be called their ‘‘life cy- These vesicles are enriched at least three-fold in Golgi cle’’; namely, the focus will be on the mechanisms resident glycosylation enzymes as compared to ante- responsible for and the molecules associated with rograde cargo molecules by a process mediated by the the synthesis in the endoplasmic reticulum (ER), the small http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Membrane Biology Springer Journals

Organization of Golgi Glycosyltransferases in Membranes: Complexity via Complexes

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Publisher
Springer-Verlag
Copyright
Copyright © 2004 by Springer-Verlag
Subject
Life Sciences; Human Physiology; Biochemistry, general
ISSN
0022-2631
eISSN
1432-1424
D.O.I.
10.1007/s00232-004-0656-5
Publisher site
See Article on Publisher Site

Abstract

J. Membrane Biol. 198, 1–13 (2004) DOI: 10.1007/s00232-004-0656-5 Topical Review W.W. Young, Jr Department of Molecular, Cellular, and Craniofacial Biology, School of Dentistry and Departments of Biochemistry and Molecular Biology and Pharmacology and Toxicology, School of Medicine, University of Louisville, Louisville, KY40292, USA Received: 1 October 2003/Revised: 19 December 2003 Introduction glycosyltransferases destined to become Golgi resi- dents, are recruited as cargo into coat protein COPII- Much of the glycosylation of proteins, lipids, and coated vesicles. As the nascent VTC moves forward, proteoglycans of mammalian cells is catalyzed by it matures to form sequentially the cis, medial, and glycosyltransferases located in the Golgi apparatus. trans Golgi cisternae and finally the trans Golgi This review will summarize recent data that deline- network (TGN). This maturation is accomplished by ates how those glycosyltransferases are organized in the retrograde trafficking of COPI-coated vesicles. membranes during what can be called their ‘‘life cy- These vesicles are enriched at least three-fold in Golgi cle’’; namely, the focus will be on the mechanisms resident glycosylation enzymes as compared to ante- responsible for and the molecules associated with rograde cargo molecules by a process mediated by the the synthesis in the endoplasmic reticulum (ER), the small

Journal

The Journal of Membrane BiologySpringer Journals

Published: Jan 1, 2004

References

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