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Sci. Signal., 11 May 2010
[DOI: 10.1126/scisignal.2000647]

Supplementary Materials for:

γ Activates GSK3 to Promote LRP6-Mediated β-Catenin Transcriptional Activity

Kristin K. Jernigan, Christopher S. Cselenyi, Curtis A. Thorne, Alison J. Hanson, Emilios Tahinci, Nicole Hajicek, William M. Oldham, Laura A. Lee, Heidi E. Hamm, John R. Hepler, Tohru Kozasa, Maurine E. Linder, Ethan Lee*

*To whom correspondence should be addressed. E-mail: ethan.lee{at}

This PDF file includes:

  • Fig. S1. A schematic showing the preparation of Xenopus egg extract used for β-catenin degradation and phosphorylation assays.
  • Fig. S2. Screen for heterotrimeric G protein subunits that inhibit β-catenin degradation and phosphorylation in Xenopus egg extract.
  • Fig. S3. Gβ1γ2 inhibits [35S]β-catenin degradation in a dose-dependent manner.
  • Fig. S4. Free Gβγ sequesters GSK3 to the membrane fraction in Xenopus egg extract.
  • Fig. S5. Myc-GSK3 interacts with Gβ1γ2, but not Gαo.
  • Fig. S6. Myc-cβARK interacts with HA-Gβ1γ2, but not CFP-axin, dishevelled, or GSK3.
  • Fig. S7. Gβ1γ2 does not enhance activation by Wnt3a or LiCl treatment, and activation by Wnt3a or LiCl is not blocked by c-βARK.
  • Fig. S8. Free Gβγ is required for enhanced GSK3 activity toward Tau and LRP6ICD.

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Citation: K. K. Jernigan, C. S. Cselenyi, C. A. Thorne, A. J. Hanson, E. Tahinci, N. Hajicek, W. M. Oldham, L. A. Lee, H. E. Hamm, J. R. Hepler, T. Kozasa, M. E. Linder, E. Lee, γ Activates GSK3 to Promote LRP6-Mediated β-Catenin Transcriptional Activity. Sci. Signal. 3, ra37 (2010).

© 2010 American Association for the Advancement of Science

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