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Endogenous SHIP2 does not localize in lipid rafts in 3T3-L1 adipocytes
Christine Jacobs1, Sheela Onnockx, Isabelle Vandenbroere
1Faculté de Médecine, Institut de Recherche Interdisciplinaire en Biologie Humaine et Moléculaire, Université Libre de Bruxelles, BatC.4.126, Route de Lennik 808, B-1070 Bruxelles, Belgium. chjacobs@ulb.ac.be
Abstract:
SH2 domain containing inositol polyphosphate 5-phosphatase (SHIP2) dephosphorylates phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P(3)) into phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P(2)). SHIP2 knock-out mice demonstrated that SHIP2 acts as a negative regulator of insulin cascade in vivo. Our two-hybrid study showed that SHIP2 interacts with c-Cbl associated protein (CAP) and c-Cbl, implicated in the insulin signaling. As some proteins implicated in insulin signaling, like insulin receptor, CAP, c-Cbl or TC10, were reported to localize in lipid rafts, we addressed the same question for SHIP2. SHIP2 was detected in the non-raft fraction in CHO-IR, C2C12 myotubes and 3T3-L1 adipocytes except when it is overexpressed in CHO-IR, where we detected SHIP2 in the raft fraction.
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