Supplementary Materials

Supplementary Materials for:

TGF-β promotes PI3K-AKT signaling and prostate cancer cell migration through the TRAF6-mediated ubiquitylation of p85α

Anahita Hamidi, Jie Song, Noopur Thakur, Susumu Itoh, Anders Marcusson, Anders Bergh, Carl-Henrik Heldin,* Maréne Landström*

*Corresponding author. Email: marene.landstrom{at}medbio.umu.se (M.L.); c-h.heldin{at}licr.uu.se (C.-H.H.)

This PDF file includes:

  • Fig. S1. AKT interacts with TRAF6 in a TGF-β–dependent manner.
  • Fig. S2. TGF-β induces Lys63-linked polyubiquitylation and activation of AKT.
  • Fig. S3. TGF-β–induced polyubiquitylation and activation of AKT require the E3 ligase activity of TRAF6.
  • Fig. S4. TGF-β–induced activation of AKT depends on the PI3K pathway and is not dependent on the kinase activities of TβRI or TβRII.
  • Fig. S5. TGF-β–induced activation of AKT is not dependent on the kinase activity of TAK1 or the PDGFR.
  • Fig. S6. SMAD7 is required for Lys63-linked polyubiquitylation of p85α and AKT.
  • Fig. S7. TRAF6, pAKT Ser473, TβRI, and p85α colocalize at the cell membrane.
  • Fig. S8. Mutation of Lys513 and Lys519 to arginine does not affect binding of p85α to p110α.
  • Fig. S9. PI3K activity is increased by TGF-β stimulation and requires the E3 ligase activity of TRAF6 but not the kinase activity of TβRI.
  • Fig. S10. TGF-β–induced polyubiquitylation of p85α on Lys513 and Lys519 is important for AKT activation and migration of p85−/− MEFs.
  • Fig. S11. Negative control for immunohistochemistry and in situ PLA.
  • Fig. S12. Mass spectrometry analysis.

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Citation: A. Hamidi, J. Song, N. Thakur, S. Itoh, A. Marcusson, A. Bergh, C.-H. Heldin, M. Landström, TGF-β promotes PI3K-AKT signaling and prostate cancer cell migration through the TRAF6-mediated ubiquitylation of p85α. Sci. Signal.10, eaal4186 (2017).

© 2017 American Association for the Advancement of Science