Science Immunology

Supplementary Materials

Supplementary Material for:

Ubiquitination of STING at lysine 224 controls IRF3 activation

Guoxin Ni, Hiroyasu Konno, Glen N. Barber*

*Corresponding author. Email: gbarber{at}med.miami.edu

Published 5 May 2017, Sci. Immunol. 2, eaah7119 (2017)
DOI: 10.1126/sciimmunol.aah7119

This PDF file includes:

  • Materials and Methods
  • Fig. S1. STING is ubiquitinated on lysine 224 with K63-linked polyubiquitin chains.
  • Fig. S2. Ubiquitination on lysine 224 is essential for STING activity.
  • Fig. S3. Ubiquitination on lysine 224 is required for STING translocation.
  • Fig. S4. K224R mutation does not affect STING dimer formation or its interaction with CDNs.
  • Fig. S5. Hyperactivity of STING K289R is caused by increased ubiquitination on K224.
  • Fig. S6. Ubiquitination on K224 is essential for STING activity in human cells.
  • Fig. S7. MUL1 ubiquitinates STING in vitro.
  • Fig. S8. MUL1 regulates dsDNA-induced STING-dependent innate response.
  • Fig. S9. MUL1 partially regulates STING activity in human cells.
  • Fig. S10. Entire Western blots.

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Other Supplementary Material for this manuscript includes the following:

  • Table S1 (Microsoft Excel format). Raw data.
  • Table S2 (Microsoft Excel format). siRNA screening data.

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