The SH2 domain containing inositol 5‐phosphatase SHIP2 displays phosphatidylinositol 3,4,5‐trisphosphate and inositol 1,3,4,5‐tetrakisphosphate 5‐phosphatase activity

FEBS Letters

Parker, Peter¹  Moreau, Colette¹  Drayer, A.Lyndsay¹  Pesesse, Xavier¹  Woscholski, Rüdiger²  Erneux, Christophe¹ 

[1] Interdisciplinary Research Institute (IRIBHN), Université Libre de Bruxelles, Campus Erasme, Bldg. C, 808 Route de Lennik, 1070 Brussels, Belgium;Protein Phosphorylation Laboratory, Imperial Cancer Research Fund, 44 Lincoln's Inn Fields, London WC2A 3PX, UK

关键词: Phosphatidylinositol metabolism;    Signal transduction;    InsP3;    inositol 1;    4;    5-trisphosphate;    InsP4;    inositol 1;    3;    4;    5-tetrakisphosphate;    PtdIns(4;    5)P2;    phosphatidylinositol 4;    5-bisphosphate;    PtdIns(3;    4;    5)P3;    phosphatidylinositol 3;    4;    5-trisphosphate;    PtdIns(3;    4)P2;    phosphatidylinositol 3;    4-bisphosphate;    rSHIP2;    recombinant SHIP2;   

DOI  :  10.1016/S0014-5793(98)01255-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Distinct forms of inositol and phosphatidylinositol polyphosphate 5-phosphatases selectively remove the phosphate from the 5-position of the inositol ring from both soluble and lipid substrates. SHIP1 is the 145-kDa SH2 domain-containing inositol 5-phosphatase expressed in haematopoietic cells. SHIP2 is a related but distinct gene product. We report here that SHIP2 can be expressed in an active form both in Escherichia coli and in COS-7 cells. A truncated 103-kDa recombinant protein could be purified from bacteria that display both inositol 1,3,4,5-tetrakisphosphate (InsP₄) and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P₃) phosphatase activities. COS-7 cell lysates transfected with SHIP2 had increased PtdIns(3,4,5)P₃ phosphatase activity as compared to the vector alone.

【 授权许可】

Unknown