title: Diversity and functions of protein glycosylation in insects.
abstract: The majority of proteins is modified with carbohydrate structures. This modification, called glycosylation, was shown to be crucial for protein folding, stability and subcellular location, as well as protein-protein interactions, recognition and signaling. Protein glycosylation is involved in multiple physiological processes, including embryonic development, growth, circadian rhythms, cell attachment as well as maintenance of organ structure, immunity and fertility. Although the general principles of glycosylation are similar among eukaryotic organisms, insects synthesize a distinct repertoire of glycan structures compared to plants and vertebrates. Consequently, a number of unique insect glycans mediate functions specific to this class of invertebrates. For instance, the core α1,3-fucosylation of N-glycans is absent in vertebrates, while in insects this modification is crucial for the development of wings and the nervous system. At present, most of the data on insect glycobiology comes from research in Drosophila. Yet, progressively more information on the glycan structures and the importance of glycosylation in other insects like beetles, caterpillars, aphids and bees is becoming available. This review gives a summary of the current knowledge and recent progress related to glycan diversity and function(s) of protein glycosylation in insects. We focus on N- and O-glycosylation, their synthesis, physiological role(s), as well as the molecular and biochemical basis of these processes.
authors.affiliation: Department of Crop Protection, Ghent University, Coupure Links 653, 9000 Ghent, Belgium; Department of Molecular Biotechnology, Ghent University, Coupure Links 653, 9000 Ghent, Belgium. Electronic address: Tomasz.Walski@UGent.be.
authors.forename: Tomasz
authors.initials: T
authors.lastname: Walski
authors.affiliation: Department of Crop Protection, Ghent University, Coupure Links 653, 9000 Ghent, Belgium; Department of Molecular Biotechnology, Ghent University, Coupure Links 653, 9000 Ghent, Belgium. Electronic address: Kristof.DeSchutter@UGent.be.
authors.forename: Kristof
authors.initials: K
authors.lastname: De Schutter
authors.affiliation: Department of Molecular Biotechnology, Ghent University, Coupure Links 653, 9000 Ghent, Belgium. Electronic address: ElsJM.VanDamme@UGent.be.
authors.forename: Els J M
authors.initials: EJM
authors.lastname: Van Damme
authors.affiliation: Department of Crop Protection, Ghent University, Coupure Links 653, 9000 Ghent, Belgium. Electronic address: Guy.Smagghe@UGent.be.
authors.forename: Guy
authors.initials: G
authors.lastname: Smagghe
mesh_terms: D000818:Animals; D050260:Carbohydrate Metabolism; D006031:Glycosylation; D019476:Insect Proteins / Q000378:metabolism*; D007313:Insecta / Q000378:metabolism*
chemical_list: D019476:Insect Proteins
keywords: CNS; Development; Fucose; Insect glycans; Pauci-mannose; Post-translational modifications; Protein glycosylation