Supplementary Materials

Supplementary Materials for:

The DUF1669 domain of FAM83 family proteins anchor casein kinase 1 isoforms

Luke J. Fulcher, Polyxeni Bozatzi, Theresa Tachie-Menson, Kevin Z. L. Wu, Timothy D. Cummins, Joshua C. Bufton, Daniel M. Pinkas, Karen Dunbar, Sabin Shrestha, Nicola T. Wood, Simone Weidlich, Thomas J. Macartney, Joby Varghese, Robert Gourlay, David G. Campbell, Kevin S. Dingwell, James C. Smith, Alex N. Bullock, Gopal P. Sapkota*

*Corresponding author. Email: g.sapkota{at}dundee.ac.uk

This PDF file includes:

  • Fig. S1. Sequence alignment of the DUF1669 domain of the FAM83 proteins.
  • Fig. S2. Coomassie images of GFP-Trap immunoprecipitations of FAM83A–H proteins used to identify interacting partners by MS.
  • Fig. S3. Immunoblots of controls for Fig. 2.
  • Fig. S4. FAM83G interacts with CK1α but not with CK1γ or TTBK1.
  • Fig. S5. CK1-specificity switch with DUF1669 chimera.
  • Fig. S6. Fluorescence images of GFP and mCherry-CK1α controls.
  • Fig. S7. FAM83H colocalizes with and contributes to the subcellular localization of endogenous CK1ε.
  • Fig. S8. Validation of CK1α and CK1ε antibodies for immunofluorescence applications.

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Other Supplementary Material for this manuscript includes the following:

  • File S1 (.txt format). Supplemental ImageJ Macro for quantification of colocalization in cells.

© 2018 American Association for the Advancement of Science