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Sci. Signal., 17 November 2009
[DOI: 10.1126/scisignal.2000431]

Supplementary Materials for:

Tyrosine Phosphorylation Inhibits PKM2 to Promote the Warburg Effect and Tumor Growth

Taro Hitosugi, Sumin Kang, Matthew G. Vander Heiden, Tae-Wook Chung, Shannon Elf, Katherine Lythgoe, Shaozhong Dong, Sagar Lonial, Xu Wang, Georgia Z. Chen, Jianxin Xie, Ting-Lei Gu, Roberto D. Polakiewicz, Johannes L. Roesel, Titus J. Boggon, Fadlo R. Khuri, D. Gary Gilliland, Lewis C. Cantley, Jonathan Kaufman, Jing Chen*

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

This PDF file includes:

  • Fig. S1. Six tyrosine residues of PKM2 are phosphorylated in cells harboring active FGFR1 mutants.
  • Fig. S2. FGFR1 directly phosphorylates PKM2.
  • Fig. S3. ABL, JAK2, and FLT3 effectively and directly phosphorylate PKM2 at Y105 in vitro, whereas epidermal growth factor receptor (EGFR) is less effective.
  • Fig. S4. Presence of the PKM2 Y105F mutant in lung cancer H1299 cells leads to decreased proliferation under hypoxic conditions.
  • Fig. S5. Y105 phosphorylation may affect FBP-binding to PKM2 in an "intra-molecular manner" in cellular contexts with high tyrosine phosphorylation stoichiometry of PKM2.
  • Fig. S6. FGFR1 binds PKM2 in a tyrosine phosphorylation–dependent manner but this binding is dispensable for FGFR1-dependent inhibition of PKM2.

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Citation: T. Hitosugi, S. Kang, M. G. Vander Heiden, T.-W. Chung, S. Elf, K. Lythgoe, S. Dong, S. Lonial, X. Wang, G. Z. Chen, J. Xie, T.-L. Gu, R. D. Polakiewicz, J. L. Roesel, T. J. Boggon, F. R. Khuri, D. G. Gilliland, L. C. Cantley, J. Kaufman, J. Chen, Tyrosine phosphorylation inhibits PKM2 to promote the Warburg effect and tumor growth. Sci. Signal. 2, ra73 (2009).

© 2009 American Association for the Advancement of Science


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