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Sci. Signal., 10 July 2012
[DOI: 10.1126/scisignal.2002754]

Supplementary Materials for:

Complementary Phosphorylation Sites in the Adaptor Protein SLP-76 Promote Synergistic Activation of Natural Killer Cells

Hun Sik Kim* and Eric O. Long*

*To whom correspondence should be addressed. E-mail: eLong{at}nih.gov (E.O.L.); hunkim{at}amc.seoul.kr (H.S.K.)

This PDF file includes:

  • Fig. S1. SLP-76 is required for synergy between 2B4 and DNAM-1.
  • Fig. S2. NKG2D and 2B4 independently induce the phosphorylation of Vav1 at Tyr160 and Tyr174.
  • Fig. S3. Synergistic Ca2+ mobilization requires both SLP-76 and Vav1.
  • Fig. S4. SLP-76 phosphorylation through combined stimulation of NKG2D and 2B4 is Syk-independent.
  • Fig. S5. SLP-76 phosphorylation by combined stimulation of NKG2D and 2B4 is not sensitive to treatment with piceatannol.
  • Fig. S6. Fyn is required for the phosphorylation of SLP-76 at Tyr113 stimulated by 2B4 but not for the phosphorylation of Tyr128 stimulated by NKG2D.
  • Fig. S7. SLP-76 overexpression does not enhance Ca2+ mobilization in response to the combined stimulation of NKG2D and 2B4.
  • Fig. S8. Treatment of cells with ionomycin results in similar Ca2+ mobilization in transfected NKL cells irrespective of the SLP-76 mutant expressed.
  • Fig. S9. Different tyrosines in SLP-76 are required for the Ca2+ mobilization stimulated by engagement of either NKG2D or 2B4 alone.

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Citation: H. S. Kim, E. O. Long, Complementary Phosphorylation Sites in the Adaptor Protein SLP-76 Promote Synergistic Activation of Natural Killer Cells. Sci. Signal. 5, ra49 (2012).

© 2012 American Association for the Advancement of Science


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