Supplementary Materials

Supplementary Materials for:

Binding of the cytoplasmic domain of CD28 to the plasma membrane inhibits Lck recruitment and signaling

Jessica Dobbins, Etienne Gagnon, Jernej Godec, Jason Pyrdol, Dario A. A. Vignali, Arlene H. Sharpe, Kai W. Wucherpfennig*

*Corresponding author. Email: kai_wucherpfennig{at}dfci.harvard.edu

This PDF file includes:

  • Fig. S1. Characterization of TFP-expressing cell lines and donor dequenching FRET measurements.
  • Fig. S2. SPR analysis of CD28-Lck binding.
  • Fig. S3. Analysis of the cell surface abundance of CD28 in OT-I+ hybridomas.
  • Fig. S4. SPR analysis of the interaction between the CD28 15-mer peptide and Lck SH2 or Lck U-SH3-SH2.
  • Fig. S5. Equilibrium binding measurements of the interaction between the Lck SH2 domain and the CD28 PYAP motif.
  • Fig. S6. Flow cytometric analysis of splenic T cells from transduced bone marrow chimeric mice.
  • Table S1. Identification of the tyrosine residues of CD28CD that are phosphorylated by Lck.

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Citation: J. Dobbins, E. Gagnon, J. Godec, J. Pyrdol, D. A. A. Vignali, A. H. Sharpe, K. W. Wucherpfennig, Binding of the cytoplasmic domain of CD28 to the plasma membrane inhibits Lck recruitment and signaling. Sci. Signal. 9, ra75 (2016).

© 2016 American Association for the Advancement of Science