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Abelson (Abl) family tyrosine kinases have been implicated in cell morphogenesis, adhesion, motility, and oncogenesis. Using a candidate approach for genes involved in planar cell polarity (PCP) signaling, we identified  Drosophila  Abl (dAbl) as a modulator of Frizzled(Fz)/PCP signaling. We demonstrate that  dAbl  positively regulates the Fz/Dishevelled (Dsh) PCP pathway without affecting canonical Wnt/Wg–Fz signaling. Genetic dissection suggests that Abl functions via Fz/Dsh signaling in photoreceptor R3 specification, a well-established Fz–PCP signaling readout. Molecular analysis shows that dAbl binds and phosphorylates Dsh on Tyr473 within the DEP domain. This phosphorylation event on Dsh is functionally critical, as the equivalent DshY473F mutant is nonfunctional in PCP signaling and stable membrane association, although it rescues canonical Wnt signaling. Strikingly, mouse embryonic fibroblasts (MEFs) deficient for  Abl1  and  Abl2/Arg  genes also show reduced Dvl2 phosphorylation as compared with control MEFs, and this correlates with a change in subcellular localization of endogenous Dvl2. As in  Drosophila , such Abl-deficient MEFs show no change in canonical Wnt signaling. Taken together, our results argue for a conserved role of Abl family members in the positive regulation of Dsh activity toward Fz–Dsh/PCP signaling by Dsh phosphorylation.

Abelson family kinases regulate Frizzled planar cell polarity signaling via Dsh phosphorylation