The Tyrosine Kinase Fer Is a Downstream Target of the PLD-PA Pathway that Regulates Cell Migration

Toshiki Itoh,* Junya Hasegawa, Kazuya Tsujita, Yasunori Kanaho, Tadaomi Takenawa*

*To whom correspondence should be addressed. E-mail: takenawa{at}med.kobe-u.ac.jp (T.T.) and titoh{at}med.kobe-u.ac.jp (T.I.)

This PDF file includes:

• Fig. S1. The F-BAR–FX unit and other known units for membrane curvature and specific lipid interactions.
• Fig. S2. The lipid specificity of Fer.
• Fig. S3. Cortactin tyrosine phosphorylation by Fer.
• Fig. S4. Fer tyrosine kinase activity is required for lamellipodia formation.
• Fig. S5. Fer-induced lamellipodia formation is dependent on Rac.
• Fig. S6. The F-BAR domain is essential for Fer-induced lamellipodia formation.
• Fig. S7. Fer is translocated to the plasma membrane through the F-BAR–FX unit upon EGF stimulation.
• Fig. S8. PLD activity is necessary for Fer activation.
• Fig. S9. Fer knockdown.
• Fig. S10. PLD and Fer are present in the same signaling pathway that results in cell migration.

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Citation: T. Itoh, J. Hasegawa, K. Tsujita, Y. Kanaho, T. Takenawa, The tyrosine kinase Fer is a downstream target of the PLD-PA pathway that regulates cell migration. Sci. Signal. 2, ra52 (2009).

© 2009 American Association for the Advancement of Science