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Sci. Signal., 12 January 2010
Vol. 3, Issue 104, p. ra2
[DOI: 10.1126/scisignal.2000526]

RESEARCH ARTICLES

Editor's Summary

A Mitotic Balance of O-GlcNAcylation and Phosphorylation
The posttranslational modification of proteins by the attachment of O-linked β-N-acetylglucosamine (O-GlcNAc) adds an additional layer of regulation to various cellular processes, including cell division. Noting that overexpression of the single enzyme that performs this modification, O-GlcNAc transferase (OGT), causes polyploidy and aberrant spindle formation in cultured cells, Wang et al. performed a global analysis of O-GlcNAcylation and phosphorylation in mitotic cells. They found that in cells forced to overexpress OGT, activation of the cyclin-dependent kinase 1, a master mitotic regulator, was suppressed and the abundance of components of the chromosomal passenger complex was reduced. They identified hundreds of O-GlcNAcylation sites, many of which were located either at the same residue as a potential phosphorylation site or within phosphorylation consensus motifs. Thus, both phosphorylation and O-GlcNAcylation appear to serve as interconnected regulatory events in mitosis.

Citation: Z. Wang, N. D. Udeshi, C. Slawson, P. D. Compton, K. Sakabe, W. D. Cheung, J. Shabanowitz, D. F. Hunt, G. W. Hart, Extensive Crosstalk Between O-GlcNAcylation and Phosphorylation Regulates Cytokinesis. Sci. Signal. 3, ra2 (2010).

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