Supplementary Materials

Supplementary Materials for:

Phosphorylation of FADD by the kinase CK1α promotes KRASG12D-induced lung cancer

Brittany M. Bowman, Katrina A. Sebolt, Benjamin A. Hoff, Jennifer L. Boes, Danette L. Daniels, Kevin A. Heist, Craig J. Galbán, Rajiv M. Patel, Jianke Zhang, David G. Beer, Brian D. Ross, Alnawaz Rehemtulla* Stefanie Galbán

*Corresponding author. E-mail: alnawaz{at}umich.edu

This PDF file includes:

  • Fig. S1. Fadd-null lesions have lower abundance of phosphorylated ERK1/2 but no detectable difference for an apoptotic marker.
  • Fig. S2. Fadd-null lesions still express Fadd transgene.
  • Fig. S3. Increased FADD mRNA correlates with KRAS mutation status in lung cancer patients.
  • Fig. S4. FADD interacts with proteins involved in the cell cycle.
  • Fig. S5. Immunohistochemistry of Csnk1a1-null lesions reveals residual CK1α protein.
    Legend for Data file S1

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Technical Details

Format: Adobe Acrobat PDF

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Other Supplementary Material for this manuscript includes the following:

  • Data file S1. Mass spectrometry data.

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Citation: B. M. Bowman, K. A. Sebolt, B. A. Hoff, J. L. Boes, D. L. Daniels, K. A. Heist, C. J. Galbán, R. M. Patel, J. Zhang, D. G. Beer, B. D. Ross, A. Rehemtulla, S. Galbán, Phosphorylation of FADD by the kinase CK1α promotes KRASG12D-induced lung cancer. Sci. Signal. 8, ra9 (2015).

© 2014 American Association for the Advancement of Science