ERK-Mediated Phosphorylation of Fibroblast Growth Factor Receptor 1 on Ser⁷⁷⁷ Inhibits Signaling

Malgorzata Zakrzewska, Ellen Margrethe Haugsten, Beata Nadratowska-Wesolowska, Angela Oppelt, Barbara Hausott, Yixin Jin, Jacek Otlewski, Jørgen Wesche, Antoni Wiedlocha*

*To whom correspondence should be addressed. E-mail: Antoni.Wiedlocha{at}rr-research.no

This PDF file includes:

• Fig. S1. In vitro phosphorylation assay with the recombinant C-terminal tail of FGFR1 and Akt or MEK1.
• Fig. S2. Effect of U0126 on ERK1/2 activity.
• Fig. S3. Effect of MEK inhibitors on FGFR1 activity in the presence or absence of brefeldin A or cycloheximide.
• Fig. S4. The effect of siRNA-mediated knockdown of ERK1/2 and GRB2 on FGFR1 activity.
• Fig. S5. Effect of the phosphorylation status of FGFR1 Ser⁷⁷⁷ on cell proliferation and migration in additional clones of stably transfected U2OS cells.
• Fig. S6. Correlation between organism complexity and tyrosine, serine, and threonine contents in the cytoplasmic region of FGFR1 proteins.

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© 2013 American Association for the Advancement of Science