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.