Supplementary Materials

Supplementary Materials for:

The C-Terminal SH3 Domain Contributes to the Intramolecular Inhibition of Vav Family Proteins

María Barreira, Salvatore Fabbiano, José R. Couceiro, Eva Torreira, Jorge L. Martínez-Torrecuadrada, Guillermo Montoya, Oscar Llorca, Xosé R. Bustelo*

*Corresponding author. E-mail: xbustelo@usal.es

This PDF file includes:

  • Fig. S1. The known activation steps of Vav family proteins.
  • Fig. S2. Truncation of the CSH3 domain promotes the activation of Vav1 in cells.
  • Fig. S3. The Vav1 CSH3 domain does not interact with the Vav1 PRR-NSH3 region.
  • Fig. S4. The CSH3 domain inhibits Vav1 in cis.
  • Fig. S5. EM structure of unphosphorylated 6×His–Vav1Δ1–144.
  • Fig. S6. Characterization of residues of the DH domain α6 helix that contribute to the stability of the inhibitory CSH3-Vav1 interaction.
  • Fig. S7. The CSH3 domain of Vav1 uses two different topological regions to interact with the DH and PH domains.
  • Fig. S8. Effect of mutation of the CSH3 DFC-R and YVEED regions on the biological activity of Vav1.
  • Fig. S9. Characterization of phospho-specific antibodies specific for Vav1.
  • Fig. S10. Proposed model for the regulation of Vav family proteins.
  • Table S1. Detection of phospho-sites in Vav1 by mass spectrometry.
  • Table S2. List of additional plasmids.
  • Table S3. List of primers.

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Citation: M. Barreira, S. Fabbiano, J. R. Couceiro, E. Torreira, J. L. Martínez-Torrecuadrada, G. Montoya, O. Llorca, X. R. Bustelo, The C-Terminal SH3 Domain Contributes to the Intramolecular Inhibition of Vav Family Proteins. Sci. Signal. 7, ra35 (2014).

© 2014 American Association for the Advancement of Science