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FEBS Lett. 1998 Oct 23;437(3):301-3.

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

Author information

1
Interdisciplinary Research Institute (IRIBHN), Université Libre de Bruxelles, Brussels, Belgium. xpesesse@ulb.ac.be

Abstract

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.

PMID:
9824312
DOI:
10.1016/s0014-5793(98)01255-1
[Indexed for MEDLINE]
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