Product Description

In vertebrate cells, APC2 antibody for research polyposis coli protein 2 (APC2) is a component of the destruction complex that regulates the phosphorylation status of b-catenin and thus Wnt signaling. APC2 is enriched at the cortex of the cell in both mammalian and Drosophila embryos, and mutations that disrupt cortical enrichment also interfere with destruction complex function. However, a precise mechanism for APC2 cortex localization has yet to be elucidated.

To identify potential factors that influence the cortical enrichment of APC2, we analyzed the cortical distribution of tagged variants of Drosophila APC2. We found that mCh-APC2-N, which lacks the Arm repeats and EB1-binding domain, is not enriched at the cortex, and mCh-APC2-C, which contains only the SAMP domain, does not significantly redistribute to the cortex together with EGFP-APC2-FL (Fig. 1C-F).

APC2 Antibody for Research: Best Practices and Applications

Interestingly, a-catenin and the Arm domain of APC2 are both involved in the formation of higher-order complexes, and they are known to interact with each other (Joslyn et al., 1993). Thus, we speculate that the Arm-binding 15R and 20R domains might mediate the interaction of APC2 with other proteins that is necessary for its cortical enrichment.

To test this hypothesis, we performed RNA interference (RNAi) in S2 cells. We targeted the a-catenin gene, DRSC11917; the Arm domain of APC2, DRSC18738; and the nuclear b-catenin binding protein, DRSC29423, using primers from the Drosophila RNAi Screening Center (McCartney et al., 1998). Knockdown of these genes resulted in a loss of APC2 cortical enrichment, but not of the destruction complex or of the phosphorylation status of b-catenin, implying that these factors do not contribute to the cortical accumulation of APC2. However, a-catenin and Arm RNAi also disrupted the phosphorylation state of the Cadherin -catenin binder, and therefore could affect Wnt signaling (supplementary material Fig. S1E, F).