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Sci. Signal., 1 November 2011
[DOI: 10.1126/scisignal.2001653]

Supplementary Materials for:

Persistent Stimulation with Interleukin-17 Desensitizes Cells Through SCFβ-TrCP-Mediated Degradation of Act1

Peiqing Shi, Shu Zhu, Yingying Lin, Yongfeng Liu, Yan Liu, Zhijian Chen, Yufang Shi, Youcun Qian*

*To whom correspondence should be addressed. E-mail: ycqian{at}sibs.ac.cn

This PDF file includes:

  • Fig. S1. Persistent degradation of Act1 is mediated by continuous stimulation with IL-17.
  • Fig. S2. IL-17 stimulates Act1 degradation through a ubiquitin-dependent proteasomal pathway.
  • Fig. S3. Stimulation with IL-17 may lead to Act1 degradation in vivo.
  • Fig. S4. The kinase responsible for Act1 phosphorylation remains unknown.
  • Fig. S5. Stimulation with either BAFF or CD40L does not lead to the phosphorylation and degradation of Act1.
  • Fig. S6. Overexpression of the ΔF-box mutant TrCP1 enables TNF-α–stimulated accumulation of pIκBα.
  • Fig. S7. The abundance of Act1 protein correlates with the strength of the IL-17– dependent response.
  • Fig. S8. Proposed model for the intrinsic mechanisms that control the IL-17 signaling pathway.

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Citation: P. Shi, S. Zhu, Y. Lin, Y. Liu, Y. Liu, Z. Chen, Y. Shi, Y. Qian, Persistent Stimulation with Interleukin-17 Desensitizes Cells Through SCFβ-TrCP-Mediated Degradation of Act1. Sci. Signal. 4, ra73 (2011).

© 2011 American Association for the Advancement of Science


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