Supplementary Materials

Supplementary Materials for:

The Ability of Sos1 to Oligomerize the Adaptor Protein LAT Is Separable from Its Guanine Nucleotide Exchange Activity in Vivo

Robert L. Kortum, Lakshmi Balagopalan, Clayton P. Alexander, Julie Garcia, John M. Pinski, Robert K. Merrill, Phan H. Nguyen, Wenmei Li, Isha Agarwal, Itoro O. Akpan, Connie L. Sommers, Lawrence E. Samelson*

*Corresponding author. E-mail: samelsonl@helix.nih.gov

This PDF file includes:

  • Fig. S1. RasGRP1 is not required for the TCR-dependent phosphorylation of LAT.
  • Fig. S2. Deletion of Sos1 does not alter anti-CD3ε–stimulated clustering of pTyr proteins.
  • Fig. S3. Characterization of Sos1-transgenic founder lines.
  • Fig. S4. TCR-dependent phosphorylation of ERK1/2 requires the RasGEF activity of Sos1.
  • Fig. S5. The RasGEF activity of Sos1 is required for the negative selection of thymocytes in Rasgrp1–/– mice.
  • Fig. S6. Multiple Sos1 functions are required for optimal pre-TCR–dependent development.
  • Fig. S7. Multiple Sos1 functions are required for anti-CD3ε–stimulated proliferation of Rag2–/– thymocytes.
  • Fig. S8. Optimal LAT clustering requires an intact Sos1 PRR.
  • Fig. S9. Combined expression of the mutant Sos1 proteins F929A and Sos-SH2 restores normal thymocyte development to Sos1(T)–/– mice.

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Citation: R. L. Kortum, L. Balagopalan, C. P. Alexander, J. Garcia, J. M. Pinski, R. K. Merrill, P. H. Nguyen, W. Li, I. Agarwal, I. O. Akpan, C. L. Sommers, L. E. Samelson, The Ability of Sos1 to Oligomerize the Adaptor Protein LAT Is Separable from Its Guanine Nucleotide Exchange Activity in Vivo. Sci. Signal. 6, ra99 (2013).

© 2013 American Association for the Advancement of Science