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

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

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 languageEnglish
Title of host publicationAdvances in Neurobiology
Pages65-93
Number of pages29
DOIs
StatePublished - 2023

Publication series

NameAdvances in Neurobiology
Volume29
ISSN (Print)2190-5215
ISSN (Electronic)2190-5223

Bibliographical note

Funding Information:
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.

Funding Information:
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.

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

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

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