The phosphatase Shp1 interacts with and dephosphorylates cortactin to inhibit invadopodia function.
Alessia VaroneChiara AmorusoMarcello MontiManpreet PathejaAdelaide GrecoLuigi AulettaAntonella ZannettiDaniela CordaPublished in: Cell communication and signaling : CCS (2021)
The main finding here reported is that cortactin is a specific substrate of the tyrosine phosphatase Shp1 and that its phosphorylation/dephosphorylation affects invadopodia formation and, as a consequence, the ability of melanoma cells to invade the extracellular matrix. Shp1 can thus be considered as a regulator of melanoma cell invasiveness and a potential target for antimetastatic drugs. Video abstract.