O-GlcNAc: a regulatory post-translational modification - PubMed (original) (raw)
Review
O-GlcNAc: a regulatory post-translational modification
Lance Wells et al. Biochem Biophys Res Commun. 2003.
Abstract
Beta-N-acetylglucosamine (O-GlcNAc) is a regulatory post-translational modification of nuclear and cytosolic proteins. The enzymes for its addition and removal have recently been cloned and partially characterized. While only about 80 mammalian proteins have been identified to date that carry this modification, it is clear that this represents just a small percentage of the modified proteins. O-GlcNAc has all the properties of a regulatory modification including being dynamic and inducible. The modification appears to modulate transcriptional and signal transduction events. There are also accruing data that O-GlcNAc plays a role in apoptosis and neurodegeneration. A working model is emerging that O-GlcNAc serves as a metabolic sensor that attenuates a cell's response to extracellular stimuli based on the energy state of the cell. In this review, we will focus on the enzymes that add/remove O-GlcNAc, the functional impact of O-GlcNAc modification, and the current working model for O-GlcNAc as a nutrient sensor.
Similar articles
- O-GlcNAc turns twenty: functional implications for post-translational modification of nuclear and cytosolic proteins with a sugar.
Wells L, Hart GW. Wells L, et al. FEBS Lett. 2003 Jul 3;546(1):154-8. doi: 10.1016/s0014-5793(03)00641-0. FEBS Lett. 2003. PMID: 12829252 Review. - Nucleocytoplasmic O-glycosylation: O-GlcNAc and functional proteomics.
Vosseller K, Wells L, Hart GW. Vosseller K, et al. Biochimie. 2001 Jul;83(7):575-81. doi: 10.1016/s0300-9084(01)01295-0. Biochimie. 2001. PMID: 11522385 Review. - Dynamic interplay between O-GlcNAc and O-phosphate: the sweet side of protein regulation.
Slawson C, Hart GW. Slawson C, et al. Curr Opin Struct Biol. 2003 Oct;13(5):631-6. doi: 10.1016/j.sbi.2003.08.003. Curr Opin Struct Biol. 2003. PMID: 14568619 Review. - Modulation of transcription factor function by O-GlcNAc modification.
Ozcan S, Andrali SS, Cantrell JE. Ozcan S, et al. Biochim Biophys Acta. 2010 May-Jun;1799(5-6):353-64. doi: 10.1016/j.bbagrm.2010.02.005. Epub 2010 Mar 2. Biochim Biophys Acta. 2010. PMID: 20202486 Free PMC article. Review. - O-GlcNAc cycling: how a single sugar post-translational modification is changing the way we think about signaling networks.
Slawson C, Housley MP, Hart GW. Slawson C, et al. J Cell Biochem. 2006 Jan 1;97(1):71-83. doi: 10.1002/jcb.20676. J Cell Biochem. 2006. PMID: 16237703 Review.
Cited by
- 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. - Glucosamine cardioprotection in perfused rat hearts associated with increased O-linked N-acetylglucosamine protein modification and altered p38 activation.
Fülöp N, Zhang Z, Marchase RB, Chatham JC. Fülöp N, et al. Am J Physiol Heart Circ Physiol. 2007 May;292(5):H2227-36. doi: 10.1152/ajpheart.01091.2006. Epub 2007 Jan 5. Am J Physiol Heart Circ Physiol. 2007. PMID: 17208994 Free PMC article. - Emerging roles of the αC-β4 loop in protein kinase structure, function, evolution, and disease.
Yeung W, Ruan Z, Kannan N. Yeung W, et al. IUBMB Life. 2020 Jun;72(6):1189-1202. doi: 10.1002/iub.2253. Epub 2020 Feb 26. IUBMB Life. 2020. PMID: 32101380 Free PMC article. Review. - O-GlcNAc stabilizes SMAD4 by inhibiting GSK-3β-mediated proteasomal degradation.
Kim YJ, Kang MJ, Kim E, Kweon TH, Park YS, Ji S, Yang WH, Yi EC, Cho JW. Kim YJ, et al. Sci Rep. 2020 Nov 16;10(1):19908. doi: 10.1038/s41598-020-76862-0. Sci Rep. 2020. PMID: 33199824 Free PMC article. - UDP-glucose pyrophosphorylase. An old protein with new tricks.
Kleczkowski LA, Geisler M, Ciereszko I, Johansson H. Kleczkowski LA, et al. Plant Physiol. 2004 Mar;134(3):912-8. doi: 10.1104/pp.103.036053. Plant Physiol. 2004. PMID: 15020755 Free PMC article. Review. No abstract available.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources