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Vimentin is a Target of an O‐GlcNAc/O‐Phosphate Signaling Complex at M‐Phase
Author(s) -
Slawson Chad,
Hart Gerald W.
Publication year - 2007
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.21.5.a615
Subject(s) - midbody , vimentin , cytokinesis , phosphorylation , microbiology and biotechnology , mitosis , chemistry , intermediate filament , cytoplasm , signal transduction , biochemistry , biology , cytoskeleton , cell division , cell , immunology , immunohistochemistry
O‐GlcNAc is a ubiquitous and dynamic post‐translational modification consisting of a single N‐acetylglucosamine moiety linked to serine or threonine residues on nuclear and cytoplasmic proteins. Previously, we demonstrated that O‐GlcNAc transferase (OGT), the enzyme responsible for the addition of the sugar moiety, is localized to the mitotic spindle in early M phase and then concentrates at the midbody during cytokinesis. O‐GlcNAc transferase associates with aurora kinase B, protein phosphatase 1, and O‐GlcNAcase, the enzyme responsible with the removal of the moiety, at the midbody. These data suggest that an O‐GlcNAc/O‐Phosphate signaling complex exists to regulate the post‐translational status of M‐phase proteins. One potential target of this signaling complex is the intermediate filament protein vimentin, a filament protein key to cytokinesis. Not only is mitotic phosphorylation increased on vimentin, but O‐GlcNAcylation is also increased. Over‐expression of OGT or O‐GlcNAcase increases phosphorylation at Ser‐71 of vimentin. These data suggest that the O‐GlcNAc/O‐Phosphate signaling complex targets vimentin and acts to potentially regulate its function. This work is supported by NIH grants CA42486 and HD13563. Dr. Hart receives a share of royalty received by the university on sales of the 110.6 antibody. Terms of this arrangement are managed by JHU.