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The SHIP2 interactor Myo1c is required for cell migration in 1321 N1 glioblastoma cells.

par Elong Edimo, William's ;Ramos, Ana Raquel ;Ghosh, Somadri ;Vanderwinden, Jean-Marie ;Erneux, Christophe
Référence Biochemical and biophysical research communications, 476, page (508-514)
Publication Publié, 2016-05

Article révisé par les pairs

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Résumé :

The phosphoinositide 5-phosphatases consist of several enzymes that have been shown to modulate cell migration and invasion. SHIP2, one family member, is known to interact with growth factor receptors and cytoskeletal proteins. In a human model of glioblastoma 1321 N1 cells, we recently identified Myo1c as a new interactor of SHIP2. This was shown in a complex of proteins also containing filamin A. We show here that SHIP2 localization at lamellipodia and ruffles is impaired in Myo1c depleted cells. In the absence of Myo1c, N1 cells tend to associate to form clusters. Cell migration is very much reduced in Myo1c depleted cells, concomitantly with a decrease in FAK Tyr397 phosphorylation, focal adhesion length and PI(4,5)P2 immunostaining. In N1 cells, Myo1c is thus important for lamellipodia formation to assemble a protein complex containing SHIP2 to facilitate cell migration.