Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


Sci. Signal., 6 March 2012
[DOI: 10.1126/scisignal.2002521]

Supplementary Materials for:

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.

[Download PDF]

Technical Details

Format: Adobe Acrobat PDF

Size: 2.86 MB


Citation: Y. Tanaka, Z. J. Chen, STING Specifies IRF3 Phosphorylation by TBK1 in the Cytosolic DNA Signaling Pathway. Sci. Signal. 5, ra20 (2012).

© 2012 American Association for the Advancement of Science


To Advertise     Find Products


Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882