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.)

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• 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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