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Ubiquitous Importance of Protein Glycosylation

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High-Throughput Glycomics and Glycoproteomics

Part of the book series: Methods in Molecular Biology ((MIMB,volume 1503))

Abstract

More than half of all proteins are glycosylated. The attached glycans provide proteins with important structural and functional properties and glycan parts of glycoproteins have essential roles in many key biological processes. This chapter describes the effect of glycosylation on the structure and function of proteins, with emphasis on regulation of protein half-life and modulation of protein function by alternative glycosylation. In addition, this chapter highlights the importance of glycan–lectin interactions, the ability of glycans to block phosphorylation of proteins, and the importance of glycans in disease.

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Authors and Affiliations

  1. Genos Glycoscience Research Laboratory, Hondlova 2/11, Zagreb, Croatia

    Jasminka Krištić & Gordan Lauc

  2. Faculty of Pharmacy and Biochemistry, University of Zagreb, A. Kovačića 1, 10000, Zagreb, Croatia

    Gordan Lauc

Authors
  1. Jasminka Krištić
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  2. Gordan Lauc
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Correspondence to Gordan Lauc .

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Editors and Affiliations

  1. Faculty of Pharmacy and Biochemistry, University of Zagreb, Zagreb, Croatia

    Gordan Lauc

  2. Center for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, The Netherlands

    Manfred Wuhrer

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Krištić, J., Lauc, G. (2017). Ubiquitous Importance of Protein Glycosylation. In: Lauc, G., Wuhrer, M. (eds) High-Throughput Glycomics and Glycoproteomics. Methods in Molecular Biology, vol 1503. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-6493-2_1

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