[en] SHIP2 is a new member of the inositol polyphosphate 5-phosphatase family showing homology to SHIP1. The structure of both enzymes is characterized by the presence of a 5' SH2 domain, a central catalytic domain, and a 3' proline-rich region. Recent results suggest that SHIP2 and SHIP1 act downstream of various receptors by removing a phosphate from the 5' position of the phosphatidylinositol 3'-kinase phosphatidylinositol 3,4, 5-triphosphate product and of inositol 1,3,4,5-tetrakisphosphate. Human SHIP2 is highly expressed in adult heart, skeletal muscle, and placenta, whereas SHIP1 expression is limited to the hematopoietic system. We report here the molecular analysis of the mouse SHIP2 cDNA and the corresponding protein, the structure of the gene, and the identification of its promoter. SHIP2 mRNA expression was analyzed in embryonic and adult mouse tissues by reverse transcription-polymerase chain reaction and in situ hybridization. In embryonic day 15.5 mice, SHIP2 was strongly expressed in the liver, specific regions of the central nervous system, the thymus, the lung, and the cartilage perichondrium. In adult mice, SHIP2 mRNA was markedly present in the brain and the thymus and at different stages of spermatozoa maturation in the seminiferous tubules. The subtle differences in the protein structure of SHIP2 and SHIP1 as well as their different patterns of expression are discussed
Schurmans, Stéphane ; Université Libre de Bruxelles - ULB > Institut de Recherche Interdisciplinaire en Biologie Humaine et Nucléaire, Institut de Biologie et de Médecine Moléculaire
Carrio, R.; University of Cantabria, 39011 Santander, Spain
Behrens, J.; Université Libre de Bruxelles - ULB
Pouillon, V.; Université Libre de Bruxelles - ULB
Merino, J.; University of Cantabria, 39011 Santander, Spain
Clément, S.; Université Libre de Bruxelles - ULB
Language :
English
Title :
The mouse SHIP2 (Inppl1) gene: complementary DNA, genomic structure, promoter analysis, and gene expression in the embryo and adult mouse
Boshart M., Klüppel M., Schmidt A., Schütz G., Luckow B. Reporter constructs with low background activity utilising the CAT gene. Gene. 110:1992;129-130.
Bucher P. Weight matrix descriptions of four eukaryotic RNA polymerase II promoter elements derived from 502 unrelated promoter sequences. J. Mol. Biol. 212:1990;563-578.
Carrio R., López-Hoyos M., Jimeno J., Benedict M. A., Merino R., Benito A., Fernández-Luna J. L., Núñez G., García-Porrero J. A., Merino J. A1 demonstrates restricted tissue distribution during embryonic development and functions to protect against cell death. Am. J. Pathol. 149:1996;2133-2142.
Drayer A. L., Pesesse X., De Smedt F., Woscholski R., Parker P., Erneux C. Cloning and expression of a human placenta inositol 1,3,4,5-tetrakisphosphate and phosphatidylinositol 3,4,5-triphosphate 5-phosphatase. Biochem. Biophys. Res. Commun. 225:1996;243-249.
Erneux C., Govaerts C., Communi D., Pesesse X. The diversity and possible functions of the inositol polyphosphate 5-phosphatases. Biochim. Biophys. Acta. 1436:1998;185-199.
Habib T., Hejna J. A., Moses R. E., Deckers S. J. Growth factors and insulin stimulate tyrosine phosphorylation of the 51C/SHIP2 protein. J. Biol. Chem. 273:1998;18605-18609.
Hejna J. A., Saito H., Merkens L. S., Tittle T. V., Jakobs P. M., Whitney M. A., Grompe M., Friedberg A. S., Moses R. E. Cloning and characterization of a human cDNA (INPPL1) sharing homology with inositol polyphosphate phosphatases. Genomics. 29:1995;285-287.
Ishihara H., Sasaoka T., Hori H., Wada T., Hirai H., Haruta T., Langlois W. J., Kobayashi M. Molecular cloning of rat SH2-containing inositol phosphatase 2 (SHIP2) and its role in the regulation of insulin signaling. Biochem. Biophys. Res. Commun. 260:1999;265-272.
Liu Q., Shalaby F., Jones J., Bouchard D., Dumont D. J. The SH2-containing inositol polyphosphate 5-phosphatase, SHIP, is expressed during hematopoiesis and spermatogenesis. Blood. 91:1998;2753-2759.
Nichols K. E., Harkin D. P., Levitz S., Krainer M., Kolquist K. A., Genovese C., Bernard A., Ferguson M., Zuo L., Snyder E., Buckler A. J., Wise C., Ashley J., Lovett M., Valentine M. B., Look A. T., Gerald W., Housman D. E., Haber D. A. Inactivating mutations in an SH2 domain-encoding gene in X-linked lymphoproliferative syndrome. Proc. Natl Acad. Sci. USA. 95:1998;13765-13770.
Pesesse X., Deleu S, De Smedt F., Drayer L., Erneux C. Identification of a second SH2-domain-containing protein closely related to the phosphatidylinositol polyphosphate 5-phosphatase SHIP. Biochem. Biophys. Res. Commun. 239:1997;697-700.
Pesesse X., Moreau C., Drayer A. L., Woscholski R., Parker P., Erneux C. The SH2 domain containing inositol 5-phosphatase SHIP2 displays phosphatidylinositol 3,4,5-triphosphate and inositol 1,3,4,5-tetrakisphosphate 5-phosphatase activity. FEBS Lett. 437:1998;301-303.
Ponting C. P. SAM: A novel motif in yeast sterile and Drosophila polyhomeotic proteins. Protein Sci. 4:1995;1928-1930.
Sambrook J., Fritsch E. F., Maniatis T. Molecular Cloning: A Laboratory Manual. 1989;Cold Spring Harbor Laboratory Press, Cold Spring Harbor. p. 7.79-7.83.
Sayos J., Wu C., Morra M., Wang N., Zhang X., Allen D., van Scaik S., Notarangelo L., Geha R., Roncarolo M. G., Oettgen H., De Vries J. E., Aversal G., Terhorst C. The X-linked lymphoproliferative-disease gene product SAP regulates signals induced through the co-receptor SLAM. Nature. 395:1998;462-469.
Schurmans S., Schiffmann S. N., Gurden H., Lemaire M., Lipp H. P., Schwam V., Pochet R., Imperato A., Böhme G. A., Parmentier M. Impaired long-term potentiation induction in dentate gyrus of calretinin-deficient mice. Proc. Natl Acad. Sci. USA. 94:1997;10415-10420.
Stapleton D., Balan I., Pawson T., Sicheri F. The crystal structure of an Eph receptor SAM domain reveals a mechanism for modular dimerization. Nat. Struct. Biol. 6:1999;44-49.
Thanos C. D., Goodwill K. E., Bowie J. U. Oligomeric structure of the human EphB2 receptor SAM domain. Science. 283:1999;833-836.
Wisniewski D., Strife A., Swendeman S., Erdjument-Bromage H., Geromanos S., Kavanaugh W. M., Tempst P., Clarkson B. A novel SH2-containing phosphatidylinositol 3,4,5-triphosphate 5-phosphatase (SHIP2) is constitutively tyrosine phosphorylated and associated with src homologous and collagen gene (SHC) in chronic myelogenous leukemia progenitor cells. Blood. 93:1999;2707-2720.
Woscholski R., Parker P. Inositol lipid 5-phosphatases - Traffic signals and signal traffic. Trends Biochem. Sci. 22:1997;427-431.
Yamabhai M., Kay B. K. Examining the specificity of Src homology 3 domain-ligand interactions with alkaline phosphatase fusion proteins. Anal. Biochem. 247:1997;143-151.
