Extensive Crosstalk Between O-GlcNAcylation and Phosphorylation Regulates Cytokinesis

Zihao Wang, Namrata D. Udeshi, Chad Slawson, Philip D. Compton, Kaoru Sakabe, Win D. Cheung, Jeffrey Shabanowitz, Donald F. Hunt, Gerald W. Hart*

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

This PDF file includes:

• Fig. S1. Schematic of O-GlcNAc peptide enrichment and analysis.
• Fig. S2. Preparation of noninfected control samples.
• Fig. S3. Schematic of sample preparations for MS analyses.
• Fig. S4. CAD MS/MS spectrum of an identified peptide originating from Aurora kinase B.
• Fig. S5. INCENP localization is unchanged in cells overexpressing OGT.
• Fig. S6. Classes of proteins that show a twofold increase or decrease in phosphorylation in spindle and midbodies from cells overexpressing OGT.
• Fig. S7. Phosphorylation sequence motifs for proteins that show greater than a twofold change.
• Fig. S8. Analysis of the O-GlcNAcylation site sequences and changes in their O-GlcNAcylation in spindle and midbodies from cells overexpressing OGT.
• Fig. S9. Schematic of CDK1 activation.
• Fig. S10. CAD MS/MS of a peptide from PLK1.
• Fig. S11. PLK1 localization is unaffected by OGT overexpression.
• Fig. S12. OGT overexpression does not change the localization of pT210-PLK1 and MYT1.
• Fig. S13. Quantitative PCR of genes whose mRNA levels are unaffected by OGT overexpression.
• Table S8. Description of supplementary table headers (tables S1 to S7).

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• Tables S1 to S7 (Data files in Excel format).

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© 2010 American Association for the Advancement of Science