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Sci. Signal., 20 November 2012
[DOI: 10.1126/scisignal.2003149]

Supplementary Materials for:

GPRC5B Activates Obesity-Associated Inflammatory Signaling in Adipocytes

Yeon-Jeong Kim, Takamitsu Sano, Takuji Nabetani, Yoshimi Asano, Yoshio Hirabayashi*

*To whom correspondence should be addressed. E-mail: hirabaya{at}riken.jp

This PDF file includes:

  • Fig. S1. Cellular localization of GPRC5B.
  • Fig. S2. GPRC5B contains multiple phosphorylated sites.
  • Fig. S3. Specificity of phosphorylation site–specific polyclonal antibodies for pGPRC5B.
  • Fig. S4. Tyrosine phosphorylation of GPRC5B in H2O2-stimulated cells.
  • Fig. S5. Interactions between the Fyn-SH2 domain and C-terminal phosphopeptides of GPRC5B.
  • Fig. S6. Increased GPRC5B abundance enhances the kinase activity of Fyn in HEK 293 cells.
  • Fig. S7. Tissue weights of mice fed an HFD.
  • Fig. S8. Representative images of liver sections from mice fed an HFD.
  • Fig. S9. Relative GPRC5B mRNA and protein abundance in mouse tissues.
  • Fig. S10. Enhanced UCP1 abundance in brown adipose tissue of GPRC5B–/– mice.
  • Fig. S11. Molecular interaction of GPRC5B and Fyn functionally leads to positive feedback regulation of the IKKε–NF-κB signaling axis.
  • Fig. S12. Functional role of GPRC5B in adipose inflammation.
  • Fig. S13. Sequence comparison of human GPRC5B and Drosophila BOSS.
  • Table S1. Serum parameters of mice in this study.

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Citation: Y.-J. Kim, T. Sano, T. Nabetani, Y. Asano, Y. Hirabayashi, GPRC5B Activates Obesity-Associated Inflammatory Signaling in Adipocytes. Sci. Signal. 5, ra85 (2012).

© 2012 American Association for the Advancement of Science


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