Article (Scientific journals)
Phosphatidylinositol 3,4,5-trisphosphate modulation in Ship2-deficient mouse embryonic fibroblasts
Blero, D.; Zhang, J.; Pesesse, X. et al.
2005In FEBS Journal, 272, p. 2512-2522
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Keywords :
inositol 5-phosphatase; mouse embryonic fibroblasts; phosphatidylinositol 3,4,5-trisphosphate; SH2 domain; signal transduction
Abstract :
[en] SHIP2, the ubiquitous SH2 domain containing inositol 5-phosphatase, includes a series of protein interacting domains and has the ability to dephosphorylate phosphatidylinositol 3,4,5-trisphosphate [PtdIns(3,4,5)P3] in vitro. The present study, which was undertaken to evaluate the impact of SHIP2 on PtdIns(3,4,5)P3 levels, was performed in a mouse embryonic fibroblast (MEF) model using SHIP2 deficient (– ⁄ –) MEF cells derived from knockout mice. PtdIns(3,4,5)P3 was upregulated in serum stimulated – ⁄ – MEF cells as compared to +⁄+ MEF cells. Although the absence of SHIP2 had no effect on basal PtdIns(3,4,5)P3 levels, we show here that this lipid was significantly upregulated in SHIP2 – ⁄ – cells but only after short-term (i.e. 5–10 min) incubation with serum. The difference in PtdIns(3,4,5)P3 levels in heterozygous fibroblast cells was intermediate between the +⁄+ and the – ⁄ – cells. In our model, insulin-like growth factor-1 stimulation did not show this upregulation. Serum stimulated phosphoinositide 3-kinase (PI 3-kinase) activity appeared to be comparable between +⁄+ and – ⁄ – cells. Moreover, protein kinase B, but not mitogen activated protein kinase activity, was also potentiated in SHIP2 deficient cells stimulated by serum. The upregulation of protein kinase B activity in serum stimulated cells was totally reversed in the presence of the PI 3-kinase inhibitor LY-294002, in both +⁄+ and – ⁄ – cells. Altogether, these data establish a link between SHIP2 and the acute control of PtdIns(3,4,5)P3 levels in intact cells
Disciplines :
Biochemistry, biophysics & molecular biology
Genetics & genetic processes
Author, co-author :
Blero, D.;  Université Libre de Bruxelles - ULB > Interdisciplinary Research Institute
Zhang, J.;  Université Libre de Bruxelles - ULB > Interdisciplinary Research Institute (IRIBHM)
Pesesse, X.;  Université Libre de Bruxelles - ULB > Interdisciplinary Research Institute (IRIBHM)
Payrastre, B.;  INSERM U563 > , Departement d’Oncogenese et Signalization dans les Cellules Hematopoietiques, Hoˆ pital Purpan, Toulouse Cedex, France
Dumont, J. E.;  Université Libre de Bruxelles - ULB > Interdisciplinary Research Institute (IRIBHM)
Schurmans, Stéphane  ;  Université Libre de Bruxelles - ULB > Institut de Recherche Interdisciplinaire en Biologie Humaine et Moleculaire
Erneux, C.;  Université Libre de Bruxelles - ULB > Interdisciplinary Research Institute (IRIBHM)
Language :
English
Title :
Phosphatidylinositol 3,4,5-trisphosphate modulation in Ship2-deficient mouse embryonic fibroblasts
Publication date :
2005
Journal title :
FEBS Journal
ISSN :
1742-464X
eISSN :
1742-4658
Publisher :
Blackwell Publishing, Oxford, United Kingdom
Volume :
272
Pages :
2512-2522
Peer reviewed :
Peer Reviewed verified by ORBi
Commentary :
Abbreviations: CHO-IR, chinese hamster ovary cells overexpressing the insulin receptor; EGF, epidermal growth factor; FBS, foetal bovine serum; FGF, fibroblast growth factor; HGF, hepatocyte growth factor; IGF, insulin-like growth factor; MAP, mitogen activated protein; M-CSF, macrophage colony-stimulating factor; MEF, mouse embryonic fibroblast; PDGF, platelet-derived growth factor; PI 3-kinase, phosphoinositide 3-kinase; PKB, protein kinase B; PtdIns(3,4)P2, phosphatidylinositol 3,4-bisphosphate; PtdIns(3,4,5)P3, phosphatidylinositol 3,4,5-trisphosphate; PtdIns4P, phosphatidylinositol 4-phosphate; PtdIns(4,5)P2, phosphatidylinositol 4,5-bisphosphate; PTEN, phosphate and tension homolog deleted on chromosome 10; SHIP, SH2 domain containing inositol phosphatase
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