Synthesis, Processing, and Function of N-Glycans in N-Glycoproteins

Erhard Bieberich

doi:10.1007/978-3-031-12390-0_3

Synthesis, Processing, and Function of N-Glycans in N-Glycoproteins

Erhard Bieberich

Research output: Chapter in Book/Report/Conference proceeding › Chapter › peer-review

15 Citations (SciVal)

Abstract

Many membrane-resident and secreted proteins, including growth factors and their receptors are N-glycosylated. The initial N-glycan structure is synthesized in the endoplasmic reticulum (ER) as a branched structure on a lipid anchor (dolicholpyrophosphate) and then co-translationally, “en bloc” transferred and linked via N-acetylglucosamine to asparagine within a specific N-glycosylation acceptor sequence of the nascent recipient protein. In the ER and then the Golgi apparatus, the N-linked glycan structure is modified by hydrolytic removal of sugar residues (“trimming”) followed by re-glycosylation with additional sugar residues (“processing”) such as galactose, fucose or sialic acid to form complex N-glycoproteins. While the sequence of the reactions leading to biosynthesis, “en bloc” transfer and processing of N-glycans is well investigated, it is still not completely understood how N-glycans affect the biological fate and function of N-glycoproteins. This review will discuss the biology of N-glycoprotein synthesis, processing and function with specific reference to the physiology and pathophysiology of the immune and nervous system, as well as infectious diseases such as Covid-19.

Original language	English
Title of host publication	Advances in Neurobiology
Pages	65-93
Number of pages	29
DOIs	https://doi.org/10.1007/978-3-031-12390-0_3
State	Published - 2023

Publication series

Name	Advances in Neurobiology
Volume	29
ISSN (Print)	2190-5215
ISSN (Electronic)	2190-5223

Bibliographical note

Publisher Copyright:
© 2023, The Author(s), under exclusive license to Springer Nature Switzerland AG.

Funding

Acknowledgements This work was supported in part by NIH grants R01NS095215, R01AG034389, and R01AG064234, and the VA grant I01BX003643. I also thank the Department of Physiology (Chair Dr. Alan Daugherty), University of Kentucky Medical School for institutional support. This work was supported in part by NIH grants R01NS095215, R01AG034389, and R01AG064234, and the VA grant I01BX003643. I also thank the Department of Physiology (Chair Dr. Alan Daugherty), University of Kentucky Medical School for institutional support.

Funders	Funder number
University of Kentucky Medical School
National Institutes of Health (NIH)	R01NS095215, R01AG034389, R01AG064234
U.S. Department of Veterans Affairs	I01BX003643

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Keywords

Chaperones
Congenital disorders of glycosylation
ERAD
Gangliosides
Glycolipids
Glycosyltransferases
N-glycans
N-glycoproteins
Processing
Trimming

ASJC Scopus subject areas

Biochemistry
Neurology
Developmental Neuroscience
Cellular and Molecular Neuroscience

Access to Document

10.1007/978-3-031-12390-0_3

Cite this

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abstract = "Many membrane-resident and secreted proteins, including growth factors and their receptors are N-glycosylated. The initial N-glycan structure is synthesized in the endoplasmic reticulum (ER) as a branched structure on a lipid anchor (dolicholpyrophosphate) and then co-translationally, “en bloc” transferred and linked via N-acetylglucosamine to asparagine within a specific N-glycosylation acceptor sequence of the nascent recipient protein. In the ER and then the Golgi apparatus, the N-linked glycan structure is modified by hydrolytic removal of sugar residues (“trimming”) followed by re-glycosylation with additional sugar residues (“processing”) such as galactose, fucose or sialic acid to form complex N-glycoproteins. While the sequence of the reactions leading to biosynthesis, “en bloc” transfer and processing of N-glycans is well investigated, it is still not completely understood how N-glycans affect the biological fate and function of N-glycoproteins. This review will discuss the biology of N-glycoprotein synthesis, processing and function with specific reference to the physiology and pathophysiology of the immune and nervous system, as well as infectious diseases such as Covid-19.",

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doi = "10.1007/978-3-031-12390-0\_3",

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KW - Processing

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ER -

Synthesis, Processing, and Function of N-Glycans in N-Glycoproteins

Abstract

Publication series

Bibliographical note

Funding

UN SDGs

Keywords

ASJC Scopus subject areas

Access to Document

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Cite this