Supplementary Materials

Supplementary Materials for:

Dimerization of the adaptor Gads facilitates antigen receptor signaling by promoting the cooperative binding of Gads to the adaptor LAT

Sigalit Sukenik, Maria P. Frushicheva, Cecilia Waknin-Lellouche, Enas Hallumi, Talia Ifrach, Rose Shalah, Dvora Beach, Reuven Avidan, Ilana Oz, Evgeny Libman, Ami Aronheim, Oded Lewinson, Deborah Yablonski*

*Corresponding author. Email: debya{at}tx.technion.ac.il

This PDF file includes:

  • Mathematical modeling
  • Fig. S1. Molecular weights of the monomeric and dimeric forms of Gads.
  • Fig. S2. Thermal stabilities of the monomeric and dimeric forms of MBP-Gads SH2.
  • Fig. S3. Model of the SH2 domain dimerization interface.
  • Fig. S4. The R109D, R109A, and F92A single mutations are not sufficient to disrupt Gads SH2 dimerization.
  • Fig. S5. Thermal stabilities of nondimerizing Gads mutants.
  • Fig. S6. Multiple sequence alignment of the C-terminal regions of LAT molecules from 15 mammalian species.
  • Fig. S7. Cell surface FcεRI abundance is independent of Gads.
  • Fig. S8. FcεRI-induced cell surface expression of the degranulation marker CD107a depends on the Gads dimerization interface.
  • Table S1. Summary of the abbreviations used in the mathematical model.
  • Table S2. Calculated kinetic constants.
  • Reference (60)

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Citation: S. Sukenik, M. P. Frushicheva, C. Waknin-Lellouche, E. Hallumi, T. Ifrach, R. Shalah, D. Beach, R. Avidan, I. Oz, E. Libman, A. Aronheim, O. Lewinson, D. Yablonski, Dimerization of the adaptor Gads facilitates antigen receptor signaling by promoting the cooperative binding of Gads to the adaptor LAT. Sci. Signal. 10, eaal1482 (2017).

© 2017 American Association for the Advancement of Science