How glycosylation affects glycosylation: the role of N-glycans in glycosyltransferase activity
- PMID: 32363402
- DOI: 10.1093/glycob/cwaa041
How glycosylation affects glycosylation: the role of N-glycans in glycosyltransferase activity
Abstract
N-glycosylation is one of the most important posttranslational modifications of proteins. It plays important roles in the biogenesis and functions of proteins by influencing their folding, intracellular localization, stability and solubility. N-glycans are synthesized by glycosyltransferases, a complex group of ubiquitous enzymes that occur in most kingdoms of life. A growing body of evidence shows that N-glycans may influence processing and functions of glycosyltransferases, including their secretion, stability and substrate/acceptor affinity. Changes in these properties may have a profound impact on glycosyltransferase activity. Indeed, some glycosyltransferases have to be glycosylated themselves for full activity. N-glycans and glycosyltransferases play roles in the pathogenesis of many diseases (including cancers), so studies on glycosyltransferases may contribute to the development of new therapy methods and novel glycoengineered enzymes with improved properties. In this review, we focus on the role of N-glycosylation in the activity of glycosyltransferases and attempt to summarize all available data about this phenomenon.
Keywords: N-glycosylation; enzyme activity; glycan; glycosyltransferase.
© The Author(s) 2020. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com.
Similar articles
-
3D Structure and Function of Glycosyltransferases Involved in N-glycan Maturation.Int J Mol Sci. 2020 Jan 9;21(2):437. doi: 10.3390/ijms21020437. Int J Mol Sci. 2020. PMID: 31936666 Free PMC article. Review.
-
Bump-and-Hole Engineering Identifies Specific Substrates of Glycosyltransferases in Living Cells.Mol Cell. 2020 Jun 4;78(5):824-834.e15. doi: 10.1016/j.molcel.2020.03.030. Epub 2020 Apr 22. Mol Cell. 2020. PMID: 32325029 Free PMC article.
-
Importance of N-glycosylation on alpha5beta1 integrin for its biological functions.Biol Pharm Bull. 2009 May;32(5):780-5. doi: 10.1248/bpb.32.780. Biol Pharm Bull. 2009. PMID: 19420742 Review.
-
Promiscuity and specificity of eukaryotic glycosyltransferases.Biochem Soc Trans. 2020 Jun 30;48(3):891-900. doi: 10.1042/BST20190651. Biochem Soc Trans. 2020. PMID: 32539082 Free PMC article. Review.
-
Comparative proteomic analyses reveal that Gnt2-mediated N-glycosylation affects cell wall glycans and protein content in Fusarium oxysporum.J Proteomics. 2015 Oct 14;128:189-202. doi: 10.1016/j.jprot.2015.07.035. Epub 2015 Aug 4. J Proteomics. 2015. PMID: 26254006
Cited by
-
Proteomics-based mass spectrometry profiling of SARS-CoV-2 infection from human nasopharyngeal samples.Mass Spectrom Rev. 2024 Jan-Feb;43(1):193-229. doi: 10.1002/mas.21813. Epub 2022 Sep 29. Mass Spectrom Rev. 2024. PMID: 36177493 Free PMC article. Review.
-
N-Glycan on the Non-Consensus N-X-C Glycosylation Site Impacts Activity, Stability, and Localization of the Sda Synthase B4GALNT2.Int J Mol Sci. 2023 Feb 18;24(4):4139. doi: 10.3390/ijms24044139. Int J Mol Sci. 2023. PMID: 36835549 Free PMC article.
-
The role of N-glycosylation in B-cell biology and IgG activity. The aspects of autoimmunity and anti-inflammatory therapy.Front Immunol. 2023 Jul 27;14:1188838. doi: 10.3389/fimmu.2023.1188838. eCollection 2023. Front Immunol. 2023. PMID: 37575234 Free PMC article. Review.
-
Loss of N-acetylglucosaminyl transferase V is involved in the impaired osteogenic differentiation of bone marrow mesenchymal stem cells.Exp Anim. 2023 Aug 7;72(3):413-424. doi: 10.1538/expanim.22-0129. Epub 2023 Apr 5. Exp Anim. 2023. PMID: 37019682 Free PMC article.
-
A universal glycoenzyme biosynthesis pipeline that enables efficient cell-free remodeling of glycans.Nat Commun. 2022 Oct 24;13(1):6325. doi: 10.1038/s41467-022-34029-7. Nat Commun. 2022. PMID: 36280670 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
