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The phosphatase Shp1 interacts with and dephosphorylates cortactin to inhibit invadopodia function.

Alessia VaroneChiara AmorusoMarcello MontiManpreet PathejaAdelaide GrecoLuigi AulettaAntonella ZannettiDaniela Corda
Published 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.
Keyphrases
  • extracellular matrix
  • protein kinase
  • single cell
  • cell therapy
  • transcription factor
  • binding protein
  • human health
  • climate change
  • risk assessment
  • basal cell carcinoma