Supplementary Materials

Supplementary Materials for:

Dephosphorylation of the adaptor LAT and phospholipase C–γ by SHP-1 inhibits natural killer cell cytotoxicity

Omri Matalon, Sophia Fried, Aviad Ben-Shmuel, Maor H. Pauker, Noah Joseph, Danielle Keizer, Marina Piterburg, Mira Barda-Saad*

*Corresponding author. Email: mira.barda-saad{at}biu.ac.il

This PDF file includes:

  • Fig. S1. Analysis of PLC-γ1 phosphorylation in NK cells under inhibitory and activating conditions.
  • Fig. S2. Analysis of protein abundance and the interaction between LAT and PLC-γ.
  • Fig. S3. Analysis of the abundances of CFP-tagged wild-type and Y132F mutant LAT proteins.
  • Fig. S4. Binding of SHP-1 to LAT is mediated by the interaction of the SHP-1 catalytic domain with LAT Tyr132.
  • Fig. S5. SHP-1:PLC-γ complex is more abundant during the inhibition of NK cells than during their activation, which results in PLC-γ1/2 dephosphorylation.
  • Fig. S6. Analysis of LAT ubiquitylation and abundance after inhibition of NK cells.
  • Fig. S7. Analysis of the knockdown of Cbl-b and c-Cbl proteins and the abundance of LAT mutant protein.
  • Fig. S8. Proposed molecular mechanisms for tuning the threshold for NK cell activation.

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Citation: O. Matalon, S. Fried, A. Ben-Shmuel, M. H. Pauker, N. Joseph, D. Keizer, M. Piterburg, M. Barda-Saad, Dephosphorylation of the adaptor LAT and phospholipase C–γ by SHP-1 inhibits natural killer cell cytotoxicity. Sci. Signal. 9, ra54 (2016).

© 2016 American Association for the Advancement of Science