The dynamic carbohydrate post-translational modification (PTM) O-linked β-N-acetyl glucosamine (O-GlcNAc) is found on thousands of proteins throughout the nucleus and cytoplasm, and rivals phosphorylation in terms of the number of substrates and pathways influenced. O-GlcNAc is highly conserved and essential in most organisms, with disruption of O-GlcNAc cycling linked to diseases ranging from cancer to neurodegeneration. Nuclear pore proteins were the first identified O-GlcNAc-modified substrates, generating intense and ongoing interest in understanding the role of O-GlcNAc cycling in nuclear pore complex structure and function. Recent advances in detecting and altering O-GlcNAcylation levels have provided insights into many mechanisms by which O-GlcNAcylation influences the nucleocytoplasmic localization and stability of protein targets. The emerging view is that the multifunctional enzymes of O-GlcNAc cycling are critical nutrient-sensing components of a complex network of signaling cascades involving multiple PTMs. Furthermore, O-GlcNAc plays a role in maintaining the structural integrity of the nuclear pore and regulating its function as the gatekeeper of nucleocytoplasmic trafficking.
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April 2017
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This artistic rendition shows an Atomic Force Microscopy tip probing the mechanics of an individual virus particle. The colour scale of the particle indicates the deformation and stress of the viral shell obtained with Finite Element Analysis. The applied force is monitored by focusing a laser beam at the end of the microcantilever. For more information please see study by Moreno-Madrid et al. in this issue, pages 499–511. Image provided by Pedro De Pablo.
Review Article|
April 13 2017
O-GlcNAc cycling and the regulation of nucleocytoplasmic dynamics
Moriah Eustice;
Moriah Eustice
1Laboratory of Cell Biochemistry and Biology, NIDDK, National Institutes of Health, Bethesda, MD, U.S.A.
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Michelle R. Bond;
Michelle R. Bond
1Laboratory of Cell Biochemistry and Biology, NIDDK, National Institutes of Health, Bethesda, MD, U.S.A.
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John A. Hanover
1Laboratory of Cell Biochemistry and Biology, NIDDK, National Institutes of Health, Bethesda, MD, U.S.A.
Correspondence: John A. Hanover (jah@helix.nih.gov)
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Publisher: Portland Press Ltd
Received:
November 09 2016
Revision Received:
February 05 2017
Accepted:
February 09 2017
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2017 The Author(s); published by Portland Press Limited on behalf of the Biochemical Society
2017
Biochem Soc Trans (2017) 45 (2): 427–436.
Article history
Received:
November 09 2016
Revision Received:
February 05 2017
Accepted:
February 09 2017
Citation
Moriah Eustice, Michelle R. Bond, John A. Hanover; O-GlcNAc cycling and the regulation of nucleocytoplasmic dynamics. Biochem Soc Trans 15 April 2017; 45 (2): 427–436. doi: https://doi.org/10.1042/BST20160171
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