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Literature DB >> 26348912

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

Daniel Mariappa¹, Nithya Selvan², Vladimir Borodkin¹, Jana Alonso¹, Andrew T Ferenbach¹, Claire Shepherd³, Iva Hopkins Navratilova³, Daan M F vanAalten^1,2.

Abstract

O-GlcNAcylation is a reversible type of serine/threonine 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-GlcNAcylation and 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 the present study, harnessing the unusual properties of an O-GlcNAcase (OGA) mutant that binds O-GlcNAc (O-N-acetylglucosamine) sites with nanomolar affinity, we uncover changes in protein O-GlcNAcylation as a function of Drosophila development.

Entities: CellLine Chemical Disease Gene Mutation Species

Keywords: Drosophila; Fluorescence polarization; O-GlcNAc probe; O-GlcNAcase (OGA); embryonic development

Mesh：

Substances：

Year: 2015 PMID： 26348912 PMCID： PMC4941924 DOI： 10.1042/BJ20150610

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

39 in total

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Authors: Jana Alonso; Juan F Santarén
Journal: Proteomics Date: 2005-02 Impact factor: 3.984

2. The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny.

Authors: R Shafi; S P Iyer; L G Ellies; N O'Donnell; K W Marek; D Chui; G W Hart; J D Marth
Journal: Proc Natl Acad Sci U S A Date: 2000-05-23 Impact factor: 11.205

3. Structure-based design of beta 1,4-galactosyltransferase I (beta 4Gal-T1) with equally efficient N-acetylgalactosaminyltransferase activity: point mutation broadens beta 4Gal-T1 donor specificity.

Authors: Boopathy Ramakrishnan; Pradman K Qasba
Journal: J Biol Chem Date: 2002-03-26 Impact factor: 5.157

Review 4. The emerging link between O-GlcNAc and Alzheimer disease.

Authors: Yanping Zhu; Xiaoyang Shan; Scott A Yuzwa; David J Vocadlo
Journal: J Biol Chem Date: 2014-10-21 Impact factor: 5.157

Review 5. Cancer metabolism and elevated O-GlcNAc in oncogenic signaling.

Authors: Zhiyuan Ma; Keith Vosseller
Journal: J Biol Chem Date: 2014-10-21 Impact factor: 5.157

6. Probing the dynamics of O-GlcNAc glycosylation in the brain using quantitative proteomics.

Authors: Nelly Khidekel; Scott B Ficarro; Peter M Clark; Marian C Bryan; Danielle L Swaney; Jessica E Rexach; Yi E Sun; Joshua J Coon; Eric C Peters; Linda C Hsieh-Wilson
Journal: Nat Chem Biol Date: 2007-05-13 Impact factor: 15.040

7. Characterization of the specificity of O-GlcNAc reactive antibodies under conditions of starvation and stress.

Authors: Russell A Reeves; Albert Lee; Roger Henry; Natasha E Zachara
Journal: Anal Biochem Date: 2014-04-18 Impact factor: 3.365

Review 8. Three Decades of Research on O-GlcNAcylation - A Major Nutrient Sensor That Regulates Signaling, Transcription and Cellular Metabolism.

Authors: Gerald W Hart
Journal: Front Endocrinol (Lausanne) Date: 2014-10-27 Impact factor: 5.555

9. GlcNAcstatins are nanomolar inhibitors of human O-GlcNAcase inducing cellular hyper-O-GlcNAcylation.

Authors: Helge C Dorfmueller; Vladimir S Borodkin; Marianne Schimpl; Daan M F van Aalten
Journal: Biochem J Date: 2009-05-13 Impact factor: 3.857

10. O-GlcNAc modifications regulate cell survival and epiboly during zebrafish development.

Authors: Danielle M Webster; Chin Fen Teo; Yuhua Sun; Dorota Wloga; Steven Gay; Kimberly D Klonowski; Lance Wells; Scott T Dougan
Journal: BMC Dev Biol Date: 2009-04-21 Impact factor: 1.978

18 in total

Review 1. Chemical and Biochemical Strategies To Explore the Substrate Recognition of O-GlcNAc-Cycling Enzymes.

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Journal: Chembiochem Date: 2018-11-12 Impact factor: 3.164

Review 2. Critical observations that shaped our understanding of the function(s) of intracellular glycosylation (O-GlcNAc).

Authors: Natasha E Zachara
Journal: FEBS Lett Date: 2018-11-24 Impact factor: 4.124

Review 3. Deciphering the Functions of Protein O-GlcNAcylation with Chemistry.

Authors: Matthew Worth; Hao Li; Jiaoyang Jiang
Journal: ACS Chem Biol Date: 2017-01-19 Impact factor: 5.100

Review 4. Molecular Interrogation to Crack the Case of O-GlcNAc.

Authors: Arielis Estevez; Dongsheng Zhu; Connor Blankenship; Jiaoyang Jiang
Journal: Chemistry Date: 2020-07-20 Impact factor: 5.236

5. Native detection of protein O-GlcNAcylation by gel electrophoresis.

Authors: Chuan Fu; Daan M F van Aalten
Journal: Analyst Date: 2020-10-26 Impact factor: 4.616

6. A mutant O-GlcNAcase enriches Drosophila developmental regulators.

Authors: Nithya Selvan; Ritchie Williamson; Daniel Mariappa; David G Campbell; Robert Gourlay; Andrew T Ferenbach; Tonia Aristotelous; Iva Hopkins-Navratilova; Matthias Trost; Daan M F van Aalten
Journal: Nat Chem Biol Date: 2017-06-12 Impact factor: 15.040

7. Mutations in N-acetylglucosamine (O-GlcNAc) transferase in patients with X-linked intellectual disability.

Authors: Anke P Willems; Mehmet Gundogdu; Marlies J E Kempers; Jacques C Giltay; Rolph Pfundt; Martin Elferink; Bettina F Loza; Joris Fuijkschot; Andrew T Ferenbach; Koen L I van Gassen; Daan M F van Aalten; Dirk J Lefeber
Journal: J Biol Chem Date: 2017-06-05 Impact factor: 5.157