title: The Early Metazoan Trichoplax adhaerens Possesses a Functional O-GlcNAc System.
abstract: Protein O-GlcNAcylation is a reversible post-translational signaling modification of nucleocytoplasmic proteins that is essential for embryonic development in bilateria. In a search for a reductionist model to study O-GlcNAc signaling, we discovered the presence of functional O-GlcNAc transferase (OGT), O-GlcNAcase (OGA), and nucleocytoplasmic protein O-GlcNAcylation in the most basal extant animal, the placozoan Trichoplax adhaerens. We show via enzymatic characterization of Trichoplax OGT/OGA and genetic rescue experiments in Drosophila melanogaster that these proteins possess activities/functions similar to their bilaterian counterparts. The acquisition of O-GlcNAc signaling by metazoa may have facilitated the rapid and complex signaling mechanisms required for the evolution of multicellular organisms.
authors.affiliation: From the Division of Molecular Microbiology and.
authors.forename: Nithya
authors.initials: N
authors.lastname: Selvan
authors.affiliation: MRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dow Street, Dundee, DD1 5EH, United Kingdom and.
authors.forename: Daniel
authors.initials: D
authors.lastname: Mariappa
authors.affiliation: the Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands.
authors.forename: Henk W P
authors.initials: HW
authors.lastname: van den Toorn
authors.affiliation: the Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands.
authors.forename: Albert J R
authors.initials: AJ
authors.lastname: Heck
authors.affiliation: From the Division of Molecular Microbiology and.
authors.forename: Andrew T
authors.initials: AT
authors.lastname: Ferenbach
authors.affiliation: From the Division of Molecular Microbiology and MRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dow Street, Dundee, DD1 5EH, United Kingdom and dmfvanaalten@dundee.ac.uk.
authors.forename: Daan M F
authors.initials: DM
authors.lastname: van Aalten
mesh_terms: D000117:Acetylglucosamine / Q000737:chemistry; D000818:Animals; D030801:Animals, Genetically Modified; D002467:Cell Nucleus / Q000201:enzymology; D003433:Crosses, Genetic; D003593:Cytoplasm / Q000201:enzymology; D004331:Drosophila melanogaster; D057809:HEK293 Cells; D006801:Humans; D020128:Inhibitory Concentration 50; D008969:Molecular Sequence Data; D017351:N-Acetylglucosaminyltransferases / Q000378:metabolism*; D054909:Placozoa / Q000201:enzymology*; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary; D034622:RNA Interference; D015398:Signal Transduction
chemical_list: D017351:N-Acetylglucosaminyltransferases; C449880:O-GlcNAc transferase; D000117:Acetylglucosamine
keywords: Animal Model; Drosophila Genetics; Evolution; O-GlcNAcylation; Post-translational Modification (PTM); Trichoplax adhaerens