Identifying potentially O-GlcNAcylated proteins using metabolic labeling, bioorthogonal enrichment, and Western blotting

Banerjee, 2013, Chemical approaches to study O-GlcNAcylation, Chemical Society Reviews, 42, 4345, 10.1039/C2CS35412H Bond, 2015, A little sugar goes a long way: The cell biology of O-GlcNAc, The Journal of Cell Biology, 208, 869, 10.1083/jcb.201501101 Boyce, 2011, Metabolic cross-talk allows labeling of O-linked beta-N-acetylglucosamine-modified proteins via the N-acetylgalactosamine salvage pathway, Proceedings of the National Academy of Sciences of the United States of America, 108, 3141, 10.1073/pnas.1010045108 Chuh, 2016, Chemical methods for encoding and decoding of posttranslational modifications, Cell Chemical Biology, 23, 86, 10.1016/j.chembiol.2015.11.006 Chuh, 2017, The new chemical reporter 6-alkynyl-6-deoxy-GlcNAc reveals O-GlcNAc modification of the apoptotic caspases that can block the cleavage/activation of Caspase-8, Journal of the American Chemical Society, 139, 7872, 10.1021/jacs.7b02213 Chuh, 2015, Chemistry-enabled methods for the visualization of cell-surface glycoproteins in metazoans, Glycoconjugate Journal, 32, 443, 10.1007/s10719-015-9589-3 Chuh, 2014, Changes in metabolic chemical reporter structure yield a selective probe of O-GlcNAc modification, Journal of the American Chemical Society, 136, 12283, 10.1021/ja504063c Clark, 2008, Direct in-gel fluorescence detection and cellular imaging of O-GlcNAc-modified proteins, Journal of the American Chemical Society, 130, 11576, 10.1021/ja8030467 Comer, 2001, Characterization of a mouse monoclonal antibody specific for O-linked N-acetylglucosamine, Analytical Biochemistry, 293, 169, 10.1006/abio.2001.5132 Grammel, 2013, Chemical reporters for biological discovery, Nature Chemical Biology, 9, 475, 10.1038/nchembio.1296 Hart, 2011, Cross talk between O-GlcNAcylation and phosphorylation: Roles in signaling, transcription, and chronic disease, Annual Review of Biochemistry, 80, 825, 10.1146/annurev-biochem-060608-102511 Hu, 2010, Site-specific interplay between O-GlcNAcylation and phosphorylation in cellular regulation, FEBS Letters, 584, 2526, 10.1016/j.febslet.2010.04.044 Li, 2016, An OGA-resistant probe allows specific visualization and accurate identification of O-GlcNAc-modified proteins in cells, ACS Chemical Biology, 11, 3002, 10.1021/acschembio.6b00678 O'Donnell, 2004, Ogt-dependent X-chromosome-linked protein glycosylation is a requisite modification in somatic cell function and embryo viability, Molecular and Cellular Biology, 24, 1680, 10.1128/MCB.24.4.1680-1690.2004 Ramakrishnan, 2002, 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, The Journal of Biological Chemistry, 277, 20833, 10.1074/jbc.M111183200 Shafi, 2000, The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny, Proceedings of the National Academy of Sciences of the United States of America, 97, 5735, 10.1073/pnas.100471497 Shen, 2017, Catalytic promiscuity of O-GlcNAc transferase enables unexpected metabolic engineering of cytoplasmic proteins with 2-azido-2-deoxy-glucose, ACS Chemical Biology, 12, 206, 10.1021/acschembio.6b00876 Sinclair, 2009, Drosophila O-GlcNAc transferase (OGT) is encoded by the polycomb group (PcG) gene, super sex combs (sxc), Proceedings of the National Academy of Sciences of the United States of America, 106, 13427, 10.1073/pnas.0904638106 Snow, 1987, Monoclonal antibodies identify a group of nuclear pore complex glycoproteins, The Journal of Cell Biology, 104, 1143, 10.1083/jcb.104.5.1143 Speers, 2004, Profiling enzyme activities in vivo using click chemistry methods, Chemistry & Biology, 11, 535, 10.1016/j.chembiol.2004.03.012 Teo, 2010, Glycopeptide-specific monoclonal antibodies suggest new roles for O-GlcNAc, Nature Chemical Biology, 6, 338, 10.1038/nchembio.338 Thompson, 2018, Methods for the detection, study, and dynamic profiling of O-GlcNAc glycosylation, Methods in Enzymology, 598, 101, 10.1016/bs.mie.2017.06.009 Vocadlo, 2012, O-GlcNAc processing enzymes: Catalytic mechanisms, substrate specificity, and enzyme regulation, Current Opinion in Chemical Biology, 16, 488, 10.1016/j.cbpa.2012.10.021 Vocadlo, 2003, A chemical approach for identifying O-GlcNAc-modified proteins in cells, Proceedings of the National Academy of Sciences of the United States of America, 100, 9116, 10.1073/pnas.1632821100 Wang, 2016, Loss of O-GlcNAc glycosylation in forebrain excitatory neurons induces neurodegeneration, Proceedings of the National Academy of Sciences of the United States of America, 113, 15120, 10.1073/pnas.1606899113 Yang, 2017, Protein O-GlcNAcylation: Emerging mechanisms and functions, Nature Reviews. Molecular Cell Biology, 18, 452, 10.1038/nrm.2017.22 Zachara, 2011, Detection and analysis of proteins modified by O-linked N-acetylglucosamine, Current Protocols in Molecular Biology, 10.1002/0471142727.mb1706s95 Zaro, 2017, The small molecule 2-azido-2-deoxy-glucose is a metabolic chemical reporter of O-GlcNAc modifications in mammalian cells, revealing an unexpected promiscuity of O-GlcNAc transferase, ACS Chemical Biology, 12, 787, 10.1021/acschembio.6b00877 Zaro, 2011, Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1, Proceedings of the National Academy of Sciences of the United States of America, 108, 8146, 10.1073/pnas.1102458108