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O‐GlcNAc Transferase is a Critical Regulator of Cytokinesis
Author(s) -
Slawson Chad,
Hart Gerald W.
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.4.a37-a
Subject(s) - cytokinesis , midbody , transferase , aurora b kinase , mitosis , aurora inhibitor , kinase , microbiology and biotechnology , chemistry , biochemistry , biology , enzyme , cell cycle , cell , cell division
O‐GlcNAc is a ubiquitous and dynamic post‐translational protein modification consisting of a single N‐acetylglucosamine moiety linked to serine or threonine residues on nuclear and cytoplasmic proteins. Previous work in our laboratory has shown that elevated O‐GlcNAc levels either though pharmacological or genetic manipulation leads to delays in cell cycle progression. These delays were most severe at M phase and suggest the O‐GlcNAc modification is essential for proper M phase progression. O‐GlcNAc transferase, the enzyme responsible for the addition of the sugar moiety, is localized at the mitotic spindle in early M phase and then concentrates at the midbody during cytokinesis. Here we show that O‐GlcNAc transferase co‐localizes with Aurora Kinase B at the midbody. Over‐expressed O‐GlcNAc transferase causes a decline in the expression of Aurora Kinase B and impaired cytokinesis. O‐GlcNAc transferase and Aurora kinase B both also interact with Protein Phosphatase 1 (PP1c). When PP1c is affinity purified from mitotic cells, Aurora kinase B, O‐GlcNAc transferase, and O‐GlcNAcase, the enzyme responsible with the removal of the moiety, all co‐purify with PP1. These data suggest that the O‐GlcNAc cycling enzymes are in a functional complex with Aurora Kinase B and PP1c and act together to regulate cytokinesis. This work is supported by NIH grants CA42486 and HD13563. G.W. H. receives a portion of royalties for the sale of the CTD110.6 under licensing agreement between Covance Research Products and The Johns Hopkins University School of Medicine. The terms of this arrangement are in accordance with the conflict of interest policy at The Johns Hopkins University.