Nucleocytoplasmic Glycosylation

Christopher M. West; Chad Slawson; Natasha E. Zachara; Gerald W. Hart

doi:10.1101/glycobiology.4e.18

Nucleocytoplasmic Glycosylation

Review

In: Essentials of Glycobiology [Internet]. 4th edition. Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 2022. Chapter 18.

Authors

Christopher M. West, Chad Slawson, Natasha E. Zachara, Gerald W. Hart

Book Editors

Book Affiliations

¹ Distinguished Professor of Medicine and of Cellular & Molecular Medicine, Co-Director, Glycobiology Research and Training Center, University of California, San Diego, La Jolla, California, USA
² Professor of Surgery, Beth Israel Deaconess Medical Center, Director, National Center for Functional Glycomics, Harvard Medical School, Boston, Massachusetts, USA
³ Distinguished Professor of Cellular & Molecular Medicine, Co-Director, Glycobiology Research and Training Center, University of California, San Diego, La Jolla, California, USA
⁴ Horace W. Goldsmith Foundation Chair, Professor of Cell Biology, Albert Einstein College of Medicine, Bronx, New York, USA
⁵ Sr. Eminent Scholar in Drug Discovery, Georgia Research Alliance William Henry Terry Professor of Biochemistry & Molecular Biology, Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia, USA
⁶ Professor of Mycology, ETH Zürich, Institute of Microbiology, Department of Biology, Zürich, Switzerland
⁷ Distinguished Research Professor, Georgia Athletics Association Professor in Complex Carbohydrate Research, Professor of Biochemistry and Molecular Biology, Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia, USA
⁸ Endowed Chair and Professor, Yabumoto Department of Intractable Disease Research, Research Institute for Microbial Diseases, Immunology Frontier Research Center, Osaka University, Osaka, Japan
⁹ Distinguished Professor of Molecular Sciences, Macquarie University, Sydney, Australia and Principal Research Leader, Institute for Glycomics, Griffith University, Gold Coast, Australia
¹⁰ Professor and Eminent Scholar Emeritus, Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia, USA
¹¹ Professor, Departments of Pharmacology and Neuroscience, Johns Hopkins University, Baltimore, Maryland, USA
¹² Director of Max-Planck-Institute of Colloids and Interfaces, Potsdam, Germany, Professor, Freie Universität, Berlin, Germany

PMID: 35536974
Bookshelf ID: NBK579979
DOI: 10.1101/glycobiology.4e.18

Excerpt

The glycosylation of macromolecules is a highly compartmentalized process. Most of the enzyme donor precursors are synthesized in the cytoplasm or nucleoplasm and transferred into the secretory pathway. There they are incorporated into the glycoproteins, glycolipids, or polysaccharides that are fated for delivery to the extracellular environment or organelles such as the lysosome. In some cases, the donor sugars are transferred to intermediate lipids presented at the cytoplasmic surface of secretory pathway membranes, and subsequently flipped into the secretory pathway for final incorporation into glycoconjugates. In other cases, polysaccharides are synthesized at the cytoplasmic surface of the plasma membrane and simultaneously translocated to the cell surface. Thus the cytoplasm has a key role in the assembly of glycans that are, however, destined to function outside of the cytoplasm. In addition, entirely different glycosyltransferases exist in the cytoplasm or nucleus to glycosylate proteins and lipids that remain to function in the cytoplasm or nucleoplasm. There is also evidence for cytoplasmic and nuclear glycoconjugates that have acquired secretory pathway–type glycans by unexplained mechanisms. The origin and role of these nucleocytoplasmic glycoconjugates, mainly glycoproteins, are the focus of this chapter. We begin with examples of monoglycosylation, including both endogenous processes and those associated with parasitism, and note that one form, O-linked β-N-acetylglucosamine (O-β-GlcNAc), is so prevalent that an entire chapter is devoted to it (Chapter 19). We then continue to complex glycans and glycosylation associated with mitochondria and chloroplasts and conclude with an assessment of nucleocytoplasmic carbohydrate binding proteins that may serve as glycan readers.

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