Supplementary Materials

Supplementary Materials for:

The Ubiquitin-Specific Protease USP15 Promotes RIG-I–Mediated Antiviral Signaling by Deubiquitylating TRIM25

Eva-Katharina Pauli, Ying Kai Chan, Meredith E. Davis, Sebastian Gableske, May K. Wang, Katharina F. Feister, Michaela U. Gack*

*Corresponding author. E-mail: michaela_gack@hms.harvard.edu

This PDF file includes:

  • Fig. S1. Viral infection increases the binding of USP15 to TRIM25.
  • Fig. S2. USP15 protein abundance is not increased in response to type I IFN or viral infection.
  • Fig. S3. Depletion of USP15 enhances the ubiquitylation of endogenous TRIM25 in infected primary human lung fibroblasts.
  • Fig. S4. Quantification of HOIP- and HOIL-1L–mediated monoubiquitylation of TRIM25 in the presence of wild-type USP15 or a catalytically inactive mutant USP15.
  • Fig. S5. Quantification of TRIM25 protein abundance in the absence or presence of ectopically expressed USP15.
  • Fig. S6. Quantification of VSV-eGFP replication in cells overexpressing USP15 and of SeV replication in NHLFs in which USP15 is knocked down.
  • Table S1. Peptides identified in affinity-purified TRIM25-RING-BB complexes analyzed by mass spectrometry.

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Citation: E.-K. Pauli, Y. K. Chan, M. E. Davis, S. Gableske, M. K. Wang, K. F. Feister, M. U. Gack, The Ubiquitin-Specific Protease USP15 Promotes RIG-I–Mediated Antiviral Signaling by Deubiquitylating TRIM25. Sci. Signal. 7, ra3 (2014).

© 2014 American Association for the Advancement of Science