|
Liu et al. 10.1073/pnas.0409472102. |
Supporting Information
Files in this Data Supplement:
Supporting Table 1
Supporting Figure 6
Supporting Figure 7
Supporting Figure 6
Fig. 6. LRRFIP2 primary sequences. Alignment of Xenopus and human LRRFIP2 amino acid sequences was carried out with CLUSTALW (1). Identical residues are highlighted in blue; homologous residues are highlighted in gray.
1. Thompson, J. D., Higgins, D. G. & Gibson, T. J. (1994) Nucleic Acids Res. 22, 4673-4680.
Supporting Figure 7
Fig. 7. The central region of Dvl3 containing the PDZ and DEP domains is responsible for interaction with LRRFIP2. (A) Schematic representation of the mutant constructs of Dvl3. (B) Immunoprecipitation analysis to examine the interaction between LRRFIP2 and truncated mutants of Dvl3. HEK293T cells were transfected with the indicated plasmids. The cell lysates were immunoprecipitated by using an anti-Flag antibody, and associated Myc-tagged truncated Dvl3 proteins were detected by immunoblotting using an anti-Myc antibody (Top). Myc-tagged proteins in cell lysates were detected with Western blots and are indicated by asterisks (Middle). Immunoprecipited Flag-LRRFIP2 is shown in Bottom with anti-Flag antibody.
