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
