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Title: SHIP2 controls plasma membrane PI(4,5)P2 thereby participating in the control of cell migration in 1321 N1 glioblastoma cells
Authors: Edimo, William's Elong
Ghosh, Somadri
Derua, Rita
Janssens, Veerle
Waelkens, Etienne
Vanderwinden, Jean-Marie
Robe, Pierre
Erneux, Christophe # ×
Issue Date: Mar-2016
Publisher: Co. of Biologists
Series Title: Journal of Cell Science vol:129 issue:6 pages:1101-1114
Article number: jcs.179663
Abstract: Phosphoinositides, particularly PI(3,4,5)P3, and PI(4,5)P2, are recognized by SHIP2 a member 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 could also be dephosphorylated to PI4P. Through depletion of SHIP2 in a glioblastoma cell line 1321 N1 cells, we show that SHIP2 inhibits cell migration. In different glioblastoma cell lines and primary cultures, SHIP2 staining at the plasma membrane partly overlaps with PI(4,5)P2 immunoreactivity. PI(4,5)P2 was upregulated in SHIP2-deficient N1 cells as compared to control cells; in contrast, PI4P was very much decreased in SHIP2-deficient cells. Therefore, SHIP2 controls both PI(3,4,5)P3 and PI(4,5)P2 levels in intact cells. In N1 cells, the PI(4,5)P2 binding protein myosin-1c was identified as a new interactor of SHIP2. Regulation of PI(4,5)P2 and PI4P content by SHIP2 controls N1 cell migration through the organization of focal adhesions. Thus, our results reveal a novel role of SHIP2 in the control of PI(4,5)P2, PI4P and cell migration in PTEN-deficient glioblastoma N1 cells.
URI: 
ISSN: 0021-9533
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Laboratory of Protein Phosphorylation and Proteomics
× corresponding author
# (joint) last author

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