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Sci. Signal., 3 December 2013
[DOI: 10.1126/scisignal.2004289]

Supplementary Materials for:

Lysine Methylation Promotes VEGFR-2 Activation and Angiogenesis

Edward J. Hartsough, Rosana D. Meyer, Vipul Chitalia, Yan Jiang, Victor E. Marquez, Irina V. Zhdanova, Janice Weinberg, Catherine E. Costello, Nader Rahimi*

*Corresponding author. E-mail: nrahimi{at}bu.edu

This PDF file includes:

  • Fig. S1. Validation of the anti–methyl-Lys and anti–methyl-Arg antibodies.
  • Fig. S2. Mass spectra of methylated VEGFR-2 peptides and their locations.
  • Fig. S3. Ratios of methylation of Lys1041 and tyrosine phosphorylation of VEGFR-2.
  • Fig. S4. Phosphorylation of Lys and Arg mutant CKRs in response to ligand stimulation.
  • Fig. S5. Mutation of Lys1041 to Phe inhibits, whereas mutation to Gln partially preserves, phosphorylation of VEGFR-2.
  • Fig. S6. The K1041R mutation does not inhibit ligand binding or dimerization of VEGFR-2.
  • Fig. S7. Adox treatment inhibits the methylation of VEGFR-2.
  • Fig. S8. Remethylation of the K1041R VEGFR-2 mutant does not increase its tyrosine phosphorylation.

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Technical Details

Format: Adobe Acrobat PDF

Size: 5.22 MB


Citation: E. J. Hartsough, R. D. Meyer, V. Chitalia, Y. Jiang, V. E. Marquez, I. V. Zhdanova, J. Weinberg, C. E. Costello, N. Rahimi, Lysine Methylation Promotes VEGFR-2 Activation and Angiogenesis. Sci. Signal. 6, ra104 (2013).

© 2013 American Association for the Advancement of Science


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