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A mutant O-GlcNAcase as a probe to reveal global dynamics of protein O-GlcNAcylation during Drosophila embryonic development

DOI: 10.1042/BJ20150610 DOI Help

Authors: D. Mariappa (University of Dundee) , Nithya Selvan (University of Dundee) , V. S. Borodkin (University of Dundee) , J. Alonso (University of Dundee) , A. T. Ferenbach (University of Dundee) , C. Shepherd (University of Dundee) , I. H. Navratilova (University of Dundee) , Daniel Van Aalten (University of Dundee)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Biochemical Journal , VOL 470 , PAGES 255 - 262

State: Published (Approved)
Published: August 2015

Abstract: O-GlcNAcylation is a reversible type of Ser/Thr glycosylation on nucleocytoplasmic proteins in metazoa. Various genetic approaches in several animal models have revealed that O-GlcNAcylation is essential for embryogenesis. However, the dynamic changes in global O-GlcNAcylationand the underlying mechanistic biology linking them to embryonic development is not understood. One of the limiting factors towards characterizing changes in O-GlcNAcylation has been the limited specificity of currently available tools to detect this modification. In this study, harnessing the unusual properties of an O-GlcNAcase mutant that binds O-GlcNAc sites with nanomolar affinity, we uncoverchanges in protein O-GlcNAcylation as a function of Drosophila development.

Journal Keywords: O-Glcnacase (Oga); Fluorescence Polarization; Drosophila; Embryonic Development; O-Glcnac Probe

Subject Areas: Biology and Bio-materials


Instruments: I03-Macromolecular Crystallography

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