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Science 23 March 2001:
Vol. 291. no. 5512, pp. 2376 - 2378
DOI: 10.1126/science.1058714

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Glycosylation of Nucleocytoplasmic Proteins: Signal Transduction and O-GlcNAc

Lance Wells,* Keith Vosseller,* Gerald W. Hartdagger

The dynamic glycosylation of serine or threonine residues on nuclear and cytosolic proteins by O-linked beta -N-acetylglucosamine (O-GlcNAc) is abundant in all multicellular eukaryotes. On several proteins, O-GlcNAc and O-phosphate alternatively occupy the same or adjacent sites, leading to the hypothesis that one function of this saccharide is to transiently block phosphorylation. The diversity of proteins modified by O-GlcNAc implies its importance in many basic cellular and disease processes. Here we systematically examine the current data implicating O-GlcNAc as a regulatory modification important to signal transduction cascades.

Department of Biological Chemistry, Johns Hopkins School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205 USA.
*   These authors contributed equally to this work.

dagger    To whom correspondence should be addressed. E-mail: gwhart{at}jhmi.edu


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Neurology 61, 322-326
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A chemical approach for identifying O-GlcNAc-modified proteins in cells.
D. J. Vocadlo, H. C. Hang, E.-J. Kim, J. A. Hanover, and C. R. Bertozzi (2003)
PNAS 100, 9116-9121
   Abstract »    Full Text »    PDF »
Sugar-dependent nuclear import of glycosylated proteins in living cells.
C. Rondanino, M.-T. Bousser, M. Monsigny, and A.-C. Roche (2003)
Glycobiology 13, 509-519
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Roles of the Tetratricopeptide Repeat Domain in O-GlcNAc Transferase Targeting and Protein Substrate Specificity.
S. P. N. Iyer and G. W. Hart (2003)
J. Biol. Chem. 278, 24608-24616
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Mechanisms of the free fatty acid-induced increase in hepatic glucose production.
T. K. T. Lam, A. Carpentier, G. F. Lewis, G. van de Werve, I. G. Fantus, and A. Giacca (2003)
Am J Physiol Endocrinol Metab 284, E863-E873
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Getting Better Without AGE: New Insights Into the Diabetic Heart.
D. A. Kass (2003)
Circ. Res. 92, 704-706
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Melanoma Cell CD44 Interaction with the alpha 1(IV)1263-1277 Region from Basement Membrane Collagen Is Modulated by Ligand Glycosylation.
J. L. Lauer-Fields, N. B. Malkar, G. Richet, K. Drauz, and G. B. Fields (2003)
J. Biol. Chem. 278, 14321-14330
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Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1.
J. Wysocka, M. P. Myers, C. D. Laherty, R. N. Eisenman, and W. Herr (2003)
Genes & Dev. 17, 896-911
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Insulin Resistance of Glycogen Synthase Mediated by O-Linked N-Acetylglucosamine.
G. J. Parker, K. C. Lund, R. P. Taylor, and D. A. McClain (2003)
J. Biol. Chem. 278, 10022-10027
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Pharmacological Agents That Directly Modulate Insulin Secretion.
M. E. Doyle and J. M. Egan (2003)
Pharmacol. Rev. 55, 105-131
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The Arabidopsis lue1 mutant defines a katanin p60 ortholog involved in hormonal control of microtubule orientation during cell growth.
T. Bouquin, O. Mattsson, H. Naested, R. Foster, and J. Mundy (2003)
J. Cell Sci. 116, 791-801
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GlcNAc 2-Epimerase Can Serve a Catabolic Role in Sialic Acid Metabolism.
S. J. Luchansky, K. J. Yarema, S. Takahashi, and C. R. Bertozzi (2003)
J. Biol. Chem. 278, 8035-8042
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Mitochondrial and nucleocytoplasmic targeting of O-linked GlcNAc transferase.
D. C. Love, J. Kochran, R. L. Cathey, S.-H. Shin, and J. A. Hanover (2003)
J. Cell Sci. 116, 647-654
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Identification and Cloning of a Novel Family of Coiled-coil Domain Proteins That Interact with O-GlcNAc Transferase.
S. P. N. Iyer, Y. Akimoto, and G. W. Hart (2003)
J. Biol. Chem. 278, 5399-5409
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Imaging with 99mTc ECDG Targeted at the Multifunctional Glucose Transport System: Feasibility Study with Rodents.
D. J. Yang, C.-G. Kim, N. R. Schechter, A. Azhdarinia, D.-F. Yu, C.-S. Oh, J. L. Bryant, J.-J. Won, E. E. Kim, and D. A. Podoloff (2003)
Radiology 226, 465-473
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