Proteomic approaches to analyze the dynamic relationships between nucleocytoplasmic protein glycosylation and phosphorylation - PubMed (original) (raw)
Review
Proteomic approaches to analyze the dynamic relationships between nucleocytoplasmic protein glycosylation and phosphorylation
Stephen A Whelan et al. Circ Res. 2003.
Abstract
O-linked beta-N-acetylglucosamine (O-GlcNAc) is both an abundant and dynamic posttranslational modification similar to phosphorylation that occurs on serine and threonine residues of cytosolic and nuclear proteins in all metazoans and cell types examined, including cardiovascular tissue. Since the discovery of O-GlcNAc more than 20 years ago, the elucidation of O-GlcNAc as a posttranslational modification has been slow, albeit similar to the rate of acceptance of phosphorylation, because of the lack of tools available for its study. Identifying O-GlcNAc posttranslational modifications on proteins is a major challenge to proteomics. The recent development of mild beta-elimination followed by Michael addition with dithiothreitol has significantly improved the site mapping of both O-GlcNAc and O-phosphate in functional proteomics. beta-Elimination followed by Michael addition with dithiothreitol facilitates the study of the labile O-GlcNAc modification in the etiology of disease states. We discuss how recent technological innovations will expand our present understanding of O-GlcNAc and what the implications are for diabetes and cardiovascular complications.
Similar articles
- Nucleocytoplasmic glycosylation, O-GlcNAc: identification and site mapping.
Zachara NE, Cheung WD, Hart GW. Zachara NE, et al. Methods Mol Biol. 2004;284:175-94. doi: 10.1385/1-59259-816-1:175. Methods Mol Biol. 2004. PMID: 15173616 - Identification of O-GlcNAc sites on proteins.
Whelan SA, Hart GW. Whelan SA, et al. Methods Enzymol. 2006;415:113-33. doi: 10.1016/S0076-6879(06)15008-9. Methods Enzymol. 2006. PMID: 17116471 - Global identification of O-GlcNAc-modified proteins.
Nandi A, Sprung R, Barma DK, Zhao Y, Kim SC, Falck JR, Zhao Y. Nandi A, et al. Anal Chem. 2006 Jan 15;78(2):452-8. doi: 10.1021/ac051207j. Anal Chem. 2006. PMID: 16408927 - Dynamic nuclear and cytoplasmic glycosylation: enzymes of O-GlcNAc cycling.
Iyer SP, Hart GW. Iyer SP, et al. Biochemistry. 2003 Mar 11;42(9):2493-9. doi: 10.1021/bi020685a. Biochemistry. 2003. PMID: 12614143 Review. No abstract available. - O-GlcNAc a sensor of cellular state: the role of nucleocytoplasmic glycosylation in modulating cellular function in response to nutrition and stress.
Zachara NE, Hart GW. Zachara NE, et al. Biochim Biophys Acta. 2004 Jul 6;1673(1-2):13-28. doi: 10.1016/j.bbagen.2004.03.016. Biochim Biophys Acta. 2004. PMID: 15238246 Review.
Cited by
- The role of protein O-linked beta-N-acetylglucosamine in mediating cardiac stress responses.
Chatham JC, Marchase RB. Chatham JC, et al. Biochim Biophys Acta. 2010 Feb;1800(2):57-66. doi: 10.1016/j.bbagen.2009.07.004. Epub 2009 Jul 14. Biochim Biophys Acta. 2010. PMID: 19607882 Free PMC article. Review. - O-GlcNAcylation: a novel post-translational mechanism to alter vascular cellular signaling in health and disease: focus on hypertension.
Lima VV, Rigsby CS, Hardy DM, Webb RC, Tostes RC. Lima VV, et al. J Am Soc Hypertens. 2009 Nov-Dec;3(6):374-87. doi: 10.1016/j.jash.2009.09.004. J Am Soc Hypertens. 2009. PMID: 20409980 Free PMC article. - O-GlcNAc modification of proteins affects volume regulation in Jurkat cells.
Nagy T, Balasa A, Frank D, Rab A, Rideg O, Kotek G, Magyarlaki T, Bogner P, Kovács GL, Miseta A. Nagy T, et al. Eur Biophys J. 2010 Jul;39(8):1207-17. doi: 10.1007/s00249-009-0573-3. Epub 2009 Dec 31. Eur Biophys J. 2010. PMID: 20043149 - Deciphering the Functions of O-GlcNAc Glycosylation in the Brain: The Role of Site-Specific Quantitative O-GlcNAcomics.
Thompson JW, Sorum AW, Hsieh-Wilson LC. Thompson JW, et al. Biochemistry. 2018 Jul 10;57(27):4010-4018. doi: 10.1021/acs.biochem.8b00516. Epub 2018 Jul 2. Biochemistry. 2018. PMID: 29936833 Free PMC article. - Nutrient-driven O-GlcNAc in proteostasis and neurodegeneration.
Akan I, Olivier-Van Stichelen S, Bond MR, Hanover JA. Akan I, et al. J Neurochem. 2018 Jan;144(1):7-34. doi: 10.1111/jnc.14242. Epub 2017 Nov 20. J Neurochem. 2018. PMID: 29049853 Free PMC article. Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources