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Phosphoinositides, specially PI(3,4,5)P3, and PI(4,5)P2, are recognized by SHIP2 an associate of the inositol polyphosphate 5-phosphatase family. SHIP2 dephosphorylates PI(3,4,5)P3 to create PI(3,4)P2; the latter interacts with specific target proteins (e.g. lamellipodin). In different glioblastoma cell lines and primary cultures, SHIP2 discoloration in the plasma membrane partly contrasts with PI(4,5)P2 immunoreactivity. Through depletion of SHIP2 at a glioblastoma cell line 1321 N1 cells, we show that SHIP2 inhibits cell migration. Thusour results reveal a novel function of SHIP2 at the constraint of PI(4,5)P2, PI4P and cell migration in PTEN-deficient glioblastoma N1 cells. Regulation of PI(4,5)P2 and PI4P articles by SHIP2 controls N1 cell migration through the organization of focal adhesions. In N1 cells, the PI(4,5)P2 binding protein myosin-1c was identified as a new interactor of SHIP2.
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