Literature DB >> 9367831

Identification of a second SH2-domain-containing protein closely related to the phosphatidylinositol polyphosphate 5-phosphatase SHIP.

X Pesesse1, S Deleu, F De Smedt, L Drayer, C Erneux.   

Abstract

Distinct inositol and phosphatidylinositol polyphosphates 5-phosphatases have recently been cloned. Primers have been designed coding for highly conserved amino acid regions that are shared between sequences of 5-phosphatases. One of the PCR fragment referred to as 51 C, shows 99% identity to a previously reported sequence (INPPL-1) present in the database. We report here the identification of cDNAs for a new SH2-domain-containing protein showing homology to the inositol 5-phosphatase SHIP and therefore referred to as SHIP2. SHIP2 differs at both N- and C-terminal ends with the sequence of INPPL-1. The translated sequence of SHIP2 encodes a 1258 amino acid protein with a predicted molecular mass of 142 kDa. Particularly high levels of SHIP2 were found in human heart, skeletal muscle and placenta as shown by Northern blot analysis. SHIP2 was also expressed in dog thyroid cells in primary culture where the expression was enhanced in TSH and EGF-stimulated cells.

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Year:  1997        PMID: 9367831     DOI: 10.1006/bbrc.1997.7538

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  51 in total

1.  Distribution of the src-homology-2-domain-containing inositol 5-phosphatase SHIP-2 in both non-haemopoietic and haemopoietic cells and possible involvement of SHIP-2 in negative signalling of B-cells.

Authors:  E Muraille; X Pesesse; C Kuntz; C Erneux
Journal:  Biochem J       Date:  1999-09-15       Impact factor: 3.857

2.  SHIP is a negative regulator of growth factor receptor-mediated PKB/Akt activation and myeloid cell survival.

Authors:  Q Liu; T Sasaki; I Kozieradzki; A Wakeham; A Itie; D J Dumont; J M Penninger
Journal:  Genes Dev       Date:  1999-04-01       Impact factor: 11.361

3.  Inhibition of endogenous SHIP2 ameliorates insulin resistance caused by chronic insulin treatment in 3T3-L1 adipocytes.

Authors:  T Sasaoka; K Fukui; T Wada; S Murakami; J Kawahara; H Ishihara; M Funaki; T Asano; M Kobayashi
Journal:  Diabetologia       Date:  2005-01-15       Impact factor: 10.122

4.  Synthesis and biological activity of PTEN-resistant analogues of phosphatidylinositol 3,4,5-trisphosphate.

Authors:  Honglu Zhang; Nicolas Markadieu; Renaud Beauwens; Christophe Erneux; Glenn D Prestwich
Journal:  J Am Chem Soc       Date:  2006-12-27       Impact factor: 15.419

Review 5.  Insulin signaling and the regulation of glucose transport.

Authors:  Louise Chang; Shian-Huey Chiang; Alan R Saltiel
Journal:  Mol Med       Date:  2004 Jul-Dec       Impact factor: 6.354

6.  An SH2 domain-containing 5' inositolphosphatase inhibits insulin-induced GLUT4 translocation and growth factor-induced actin filament rearrangement.

Authors:  P Vollenweider; M Clodi; S S Martin; T Imamura; W M Kavanaugh; J M Olefsky
Journal:  Mol Cell Biol       Date:  1999-02       Impact factor: 4.272

7.  SH2-containing inositol 5'-phosphatase SHIP2 associates with the p130(Cas) adapter protein and regulates cellular adhesion and spreading.

Authors:  N Prasad; R S Topping; S J Decker
Journal:  Mol Cell Biol       Date:  2001-02       Impact factor: 4.272

8.  NMR studies of a heterotypic Sam-Sam domain association: the interaction between the lipid phosphatase Ship2 and the EphA2 receptor.

Authors:  Marilisa Leone; Jason Cellitti; Maurizio Pellecchia
Journal:  Biochemistry       Date:  2008-12-02       Impact factor: 3.162

9.  5-Stabilized phosphatidylinositol 3,4,5-trisphosphate analogues bind Grp1 PH, inhibit phosphoinositide phosphatases, and block neutrophil migration.

Authors:  Honglu Zhang; Ju He; Tatiana G Kutateladze; Takahiro Sakai; Takehiko Sasaki; Nicolas Markadieu; Christophe Erneux; Glenn D Prestwich
Journal:  Chembiochem       Date:  2010-02-15       Impact factor: 3.164

10.  The Sam domain of the lipid phosphatase Ship2 adopts a common model to interact with Arap3-Sam and EphA2-Sam.

Authors:  Marilisa Leone; Jason Cellitti; Maurizio Pellecchia
Journal:  BMC Struct Biol       Date:  2009-09-18
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