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. 2014 Nov 1;25(21):3424–3436. doi: 10.1091/mbc.E14-04-0885

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© 2014 Kunttas-Tatli et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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FIGURE 2: — Removal of ASAD disrupts APC self-association. (A) Schematic representation of Drosophila APC2 and APC1 constructs used in the study. (B) mCherry (mCh)-tagged full-length APC2 protein (red arrow) coimmunoprecipitates untagged full-length protein (black arrow). mCh-APC2 ASAD mutants (both deletion and point mutant) and mCh-APC2-C (red arrows) fail to coimmunoprecipitate untagged APC2-FL (black arrows in 2–4). (C) Yeast two-hybrid experiments demonstrated that APC2-N can interact directly with APC2-N. Deletion of the ASAD (APC2-N-ΔASAD) or disruption of the potential coiled coil (APC2-N-ASADPro) abolishes this interaction. (D) mCh-APC1-N coimmunoprecipitates untagged APC2-FL protein but fails to coimmunoprecipitate the APC2-ΔASAD mutant (black arrow). APC2-N175K contains a mutation in the Arm repeats and retains the mCh-APC1-N interaction. (E) mCh-KAP3 coimmunoprecipitates both full-length APC2 and the APC2-ΔASAD mutant (black arrows). CL, cell lysate; DL, depleted lysate; P, pull down.