FIGURE 4.

The amino acid stretch Ser⁷⁹⁴–Ala⁸¹⁰ within the cytoplasmic tail of ADAM17 binds to PLK2. A, schematic representation of truncated and deletion mutants within the cytoplasmic domain of ADAM17 used to map the interaction interface required for PLK2 binding. A gray box highlights the identified binding epitope for PLK2. B, Western blots of co-immunoprecipitates and lysates of HEK293T cells transiently co-transfected with the ADAM17 mutants represented in A in presence or absence of FLAG-PLK2. Precipitation of PLK2 with the anti-FLAG antibody (M2) led to co-precipitation of ADAM17Δ801, ADAM17Δ811, and ADAM17Δ821. C, Western blots of co-immunoprecipitates and lysates of HEK293T cells transiently co-transfected with the ADAM17 deletion mutant ADAM17ΔSSTA in presence or absence of FLAG-PLK2. D, Western blots of co-immunoprecipitates and lysates of HEK293T cells transiently co-transfected with the ADAM17 deletion mutants represented in A in presence or absence of FLAG-PLK2. Precipitation of PLK2 with the anti-FLAG antibody (M2) led to co-precipitation of ADAM17-D4 and ADAM17-D5. Single transfections of ADAM17 mutants served as specificity controls.