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SHIP2

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Encyclopedia of Signaling Molecules

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Synonyms

INPPL1; SH2 domain containing inositol phosphate 5-phosphatase type 2

Historical Background

Inositol polyphosphate 5-phosphatase or phosphoinositide 5-phosphatases (or PI 5-phosphatases) are enzymes that can act on inositol phosphates and/or phosphoinositides (PIs) as substrates to dephosphorylate the phosphate at 5 position of the inositol ring (Balla 2013). In human, it consists in a family of ten different isoenzymes (Blero et al. 2007). One of the first isoenzyme to be cloned was OCRL1 which is mutated in the Lowe syndrome and Dent-2 disease (Attree et al. 1992). Our interest in the family of PI 5-phosphatases originated from the cloning of INPP5A (i.e., type 1 inositol 1,4,5-trisphosphate 5-phosphatase), a phosphatase that can act on soluble inositol phosphates, i.e., Ins(1,4,5)P3 and Ins(1,3,4,5)P4 as substrate. At that time, its catalytic domain showed some sequence similarity with OCRL1 and another PI 5-phosphatase INPP5B that was identified by the group of Majerus....

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References

  • Attree O, Olivos IM, Okabe I, Bailey LC, Nelson DL, Lewis RA, McInnes RR, Nussbaum RL. The Lowe’s oculocerebrorenal syndrome gene encodes a protein highly homologous to inositol polyphosphate-5-phosphatase. Nature. 1992;358:239–42.

    Article  CAS  PubMed  Google Scholar 

  • Awad A, Sar S, Barre R, Cariven C, Marin M, Salles JP, Erneux C, Samuel D, Gassama-Diagne A. SHIP2 regulates epithelial cell polarity through its lipid product that binds to Dlg1, a pathway subverted by Hepatitis C virus core protein. Mol Biol Cell. 2013;24:2171–85.

    Google Scholar 

  • Balla T. Phosphoinositides: tiny lipids with giant impact on cell regulation. Physiol Rev. 2013;93:1019–137.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Below JE, Earl DL, Shively KM, McMillin MJ, Smith JD, Turner EH, Stephan MJ, Al-Gazali LI, Hertecant JL, Chitayat D, et al. Whole-genome analysis reveals that mutations in inositol polyphosphate phosphatase-like 1 cause opsismodysplasia. Am J Hum Genet. 2013;92:137–43.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Blero D, Zhang J, Pesesse X, Payrastre B, Dumont JE, Schurmans S, Erneux C. Phosphatidylinositol 3,4,5-trisphosphate modulation in SHIP2-deficient mouse embryonic fibroblasts. FEBS J. 2005;272:2512–22.

    Article  CAS  PubMed  Google Scholar 

  • Blero D, Payrastre B, Schurmans S, Erneux C. Phosphoinositide phosphatases in a network of signalling reactions. Pflugers Arch. 2007;455:31–44.

    Article  CAS  PubMed  Google Scholar 

  • Clement S, Krause U, Desmedt F, Tanti JF, Behrends J, Pesesse X, Sasaki T, Penninger J, Doherty M, Malaisse W, et al. The lipid phosphatase SHIP2 controls insulin sensitivity. Nature. 2001;409:92–7.

    Article  CAS  PubMed  Google Scholar 

  • Clement S, Krause U, Desmedt F, Tanti JF, Behrends J, Pesesse X, Sasaki T, Penninger J, Doherty M, Malaisse W, et al. Corrigendum: the lipid phosphatase SHIP2 controls insulin sensitivity. Nature. 2005;431:878.

    Article  Google Scholar 

  • Damen JE, Liu L, Rosten P, Humphries RK, Jefferson AB, Majerus PW, Krystal G. The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5- triphosphate 5-phosphatase. Proc Natl Acad Sci USA. 1996;93:1689–93.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Drayer AL, 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-trisphosphate 5- phosphatase. Biochem Biophys Res Commun. 1996;225:243–9.

    Article  CAS  PubMed  Google Scholar 

  • Dubois E, Jacoby M, Blockmans M, Pernot E, Schiffmann SN, Foukas LC, Henquin JC, Vanhaesebroeck B, Erneux C, Schurmans S. Developmental defects and rescue from glucose intolerance of a catalytically-inactive novel Ship2 mutant mouse. Cell Signal. 2012;24:1971–80.

    Article  CAS  PubMed  Google Scholar 

  • Dyson JM, O’Malley CJ, Becanovic J, Munday AD, Berndt MC, Coghill ID, Nandurkar HH, Ooms LM, Mitchell CA. The SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2, binds filamin and regulates submembraneous actin. J Cell Biol. 2001;155:1065–79.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Elong Edimo W, Ghosh S, Derua R, Janssens V, Waelkens E, Vanderwinden JM, Robe P, Erneux C. SHIP2 controls plasma membrane PI(4,5)P2 thereby participating in the control of cell migration in 1321 N1 glioblastoma. J Cell Sci. 2016;129:1101–14.

    Article  PubMed  Google Scholar 

  • Erneux C, Edimo WE, Deneubourg L, Pirson I. SHIP2 multiple functions: a balance between a negative control of PtdIns(3,4,5)P3 level, a positive control of PtdIns(3,4)P2 production, and intrinsic docking properties. J Cell Biochem. 2011;112:2203–9.

    Article  CAS  PubMed  Google Scholar 

  • Fradet A, Fitzgerald J. INPPL1 gene mutations in opsismodysplasia. J Hum Genet. 2017;62:135–40.

    Google Scholar 

  • Giuriato S, Payrastre B, Drayer AL, Plantavid M, Woscholski R, Parker P, Erneux C, Chap H. Tyrosine phosphorylation and relocation of SHIP are integrin-mediated in thrombin-stimulated human blood platelets. J Biol Chem. 1997;272:26857–63.

    Article  CAS  PubMed  Google Scholar 

  • Giuriato S, Blero D, Robaye B, Bruyns C, Payrastre B, Erneux C. SHIP2 overexpression strongly reduces the proliferation rate of K562 erythroleukemia cell line. Biochem Biophys Res Commun. 2002;296:106–10.

    Article  CAS  PubMed  Google Scholar 

  • Giuriato S, Pesesse X, Bodin S, Sasaki T, Viala C, Marion E, Penninger J, Schurmans S, Erneux C, Payrastre B. SH2-containing inositol 5-phosphatases 1 and 2 in blood platelets: their interactions and roles in the control of phosphatidylinositol 3,4,5-trisphosphate levels. Biochem J. 2003;376:199–207.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Hejna JA, Saito H, Merkens LS, Tittle TV, Jakobs PM, Whitney MA, Grompe M, Friedberg AS, Moses RE. Cloning and characterization of a human cDNA (INPPL1) sharing homology with inositol polyphosphate phosphatases. Genomics. 1995;29:285–7.

    Article  CAS  PubMed  Google Scholar 

  • Hoekstra E, Das AM, Willemsen M, Swets M, Kuppen PJ, van der Woude CJ, Bruno M J, Shah JP, Ten Hagen TL, Chisholm JD, et al. Lipid phosphatase SHIP2 functions as oncogene in colorectal cancer by regulating PKB activation. Oncotarget. 2016;7:73525–40.

    Google Scholar 

  • Huber C, Faqeih EA, Bartholdi D, Bole-Feysot C, Borochowitz Z, Cavalcanti DP, Frigo A, Nitschke P, Roume J, Santos HG, et al. Exome sequencing identifies INPPL1 mutations as a cause of opsismodysplasia. Am J Hum Genet. 2013;92:144–9.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Jurynec MJ, Grunwald DJ. SHIP2, a factor associated with diet-induced obesity and insulin sensitivity, attenuates FGF signaling in vivo. Dis Model Mech. 2010;3:733–42.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Nakatsu F, Perera RM, Lucast L, Zoncu R, Domin J, Gertler FB, Toomre D, De Camilli P. The inositol 5-phosphatase SHIP2 regulates endocytic clathrin-coated pit dynamics. J Cell Biol. 2010;190(3):307–15.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Oikawa T, Takenawa T. PtdIns(3,4)P2 instigates focal adhesions to generate podosomes. Cell Adhes Migr. 2009;3:195–7.

    Article  Google Scholar 

  • 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. 1997;239:697–700.

    Article  CAS  PubMed  Google Scholar 

  • Pesesse X, Moreau C, Drayer AL, Woscholski R, Parker P, Erneux C. 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 Lett. 1998;437:301–3.

    Article  CAS  PubMed  Google Scholar 

  • Prasad NK, Tandon M, Handa A, Moore GE, Babbs CF, Snyder PW, Bose S. High expression of obesity-linked phosphatase SHIP2 in invasive breast cancer correlates with reduced disease-free survival. Tumour Biol. 2008;29:330–41.

    Article  CAS  PubMed  Google Scholar 

  • Rajadurai CV, Havrylov S, Coelho PP, Ratcliffe CD, Zaoui K, Huang BH, Monast A, Chughtai N, Sangwan V, Gertler FB, et al. 5’-Inositol phosphatase SHIP2 recruits Mena to stabilize invadopodia for cancer cell invasion. J Cell Biol. 2016;214:719–34.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Sasaoka T, Wada T, Tsuneki H. Lipid phosphatases as a possible therapeutic target in cases of type 2 diabetes and obesity. Pharmacol Ther. 2006;112:799–809.

    Article  CAS  PubMed  Google Scholar 

  • Sharma VP, Eddy R, Entenberg D, Kai M, Gertler FB, Condeelis J. Tks5 and SHIP2 regulate invadopodium maturation, but not initiation, in breast carcinoma cells. Curr Biol. 2013;23:2079–89.

    Article  CAS  PubMed  Google Scholar 

  • Sleeman MW, Wortley KE, Lai KMV, Gowen LC, Kintner J, Kline WO, Garcia K, Stitt TN, Yancopoulos GD, Wiegand SJ, et al. Absence of the lipid phosphatase SHIP2 confers resistance to diary obesity. Nat Med. 2005;11:199–205.

    Article  CAS  PubMed  Google Scholar 

  • Taylor V, Wong M, Brandts C, Reilly L, Dean NM, Cowsert LM, Moodie S, Stokoe D. 5’ phospholipid phosphatase SHIP-2 causes protein kinase B inactivation and cell cycle arrest in glioblastoma cells. Mol Cell Biol. 2000;20:6860–71.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  • Wisniewski D, Strife A, Swendeman S, Erdjument-Bromage H, Geromanos S, Kavanaugh WM, Tempst P, Clarkson B. A novel SH2-containing phosphatidylinositol 3,4,5-trisphosphate 5- phosphatase (SHIP2) is constitutively tyrosine phosphorylated and associated with src homologous and collagen gene (SHC) in chronic myelogenous leukemia progenitor cells. Blood. 1999;93:2707–20.

    CAS  PubMed  Google Scholar 

  • Xie J, Vandenbroere I, Pirson I. SHIP2 associates with intersectin and recruits it to the plasma membrane in response to EGF. FEBS Lett. 2008;582:3011–7.

    Article  CAS  PubMed  Google Scholar 

  • Xie J, Erneux C, Pirson I. How does SHIP1/2 balance PtdIns(3,4)P2 and does it signal independently of its phosphatase activity? BioEssays. 2013;35:733–43.

    Article  CAS  PubMed  Google Scholar 

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Authors and Affiliations

  1. Institut de Recherche Interdisciplinaire en Biologie Humaine et Moléculaire (IRIBHM), Université Libre de Bruxelles (ULB), Campus Erasme, 1070, Brussels, Belgium

    Christophe Erneux

  2. Laboratoire de Génétique Fonctionnelle, GIGA-Research Centre, Université de Liège (ULg), 1 rue de l’Hôpital, 4000, Liège, Belgium

    Stéphane Schurmans

Authors
  1. Christophe Erneux
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  2. Stéphane Schurmans
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Correspondence to Christophe Erneux .

Editor information

Editors and Affiliations

  1. Dept. Biological Science, Department of Molecular Science and Tech College of Natural Science, Suwon, Korea (Republic of)

    Sangdun Choi

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Erneux, C., Schurmans, S. (2016). SHIP2. In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-6438-9_101857-1

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  • DOI: https://doi.org/10.1007/978-1-4614-6438-9_101857-1

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  • Print ISBN: 978-1-4614-6438-9

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