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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 form PI(3,4)P2; the latter interacts with specific target proteins (e.g. lamellipodin). Although the SHIP2 preferred substrate is PI(3,4,5)P3, PI(4,5)P2 may also be dephosphorylated into PI4P. In numerous glioblastoma cell lines and primary cultures, SHIP2 discoloration in the plasma membrane partly overlaps with PI(4,5)P2 immunoreactivity. Through depletion of SHIP2 at a glioblastoma cell 1321 N1 cells, we now show that SHIP2 inhibits cell regeneration. Thusour results reveal a novel function of SHIP2 at the control 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 company of focal adhesions.
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