STING Specifies IRF3 Phosphorylation by TBK1 in the Cytosolic DNA Signaling Pathway

Yasuo Tanaka and Zhijian J. Chen*

*To whom correspondence should be addressed. E-mail: zhijian.chen{at}utsouthwestern.edu

This PDF file includes:

• Fig. S1. STING-dependent activation of IRF3 in L929 cells and in a cell-free assay.
• Fig. S2. Characterization of the cell-free assay of IRF3 activation by recombinant STING proteins.
• Fig. S3. NEMO is dispensable for the activation of IRF3 by STING.
• Fig. S4. Confocal fluorescence microscopy of STING, IRF3, and TBK1 in L929 cells.
• Fig. S5. Ser³⁶⁶ and Leu³⁷⁴ of STING are required for the phosphorylation of IRF3, but not TBK1, in cell-free assays.
• Fig. S6. The S366A and L374A STING mutant proteins still form aggregates.
• Fig. S7. STING is phosphorylated by TBK1 upon stimulation of cells with ISD.
  

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© 2012 American Association for the Advancement of Science