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

Pesesse, Xavier; Moreau, Colette; Drayer, Anneke Lyndsay; Woscholski, Rüdiger; Parker, Peter J.; Erneux, Christophé

doi:10.1016/s0014-5793(98)01255-1

Cited by 114 publications

(106 citation statements)

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“…This protein, referred to as SHIP-2, displays enzymic activity comparable to that of SHIP-1. The substrates in itro are Ins(1,3,4,5)P % and PtdIns(3,4,5)P $ [20,21]. Recent work by Habib et al [21] has demonstrated that 51C\SHIP-2 associates with Shc in human non-haemopoietic cell lines stimulated with growth factors and insulin.…”

Section: Figure 1 Alignment Of Ship-1 and Ship-2 Sequencesmentioning

confidence: 99%

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

Muraille

Pesesse

Kuntz

et al. 1999

Biochemical Journal

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The termination of activation signals is a critical step in the control of the immune response; perturbation of inhibitory feedback pathways results in profound immune defects culminating in autoimmunity and overwhelming inflammation. FcγRIIB receptor is a well described inhibitory receptor. The ligation of B-cell receptor (BCR) and FcγRIIB leads to the inhibition of B-cell activation. Numerous studies have demonstrated that the SH2-domain-containing inositol 5-phosphatase SHIP (referred hereto as SHIP-1) is essential in this process. The cDNA encoding a second SH2-domain-containing inositol 5-phosphatase, SHIP-2, has been cloned [Pesesse, Deleu, De Smedt, Drayer and Erneux (1997) Biochem. Biophys. Res. Commun. 239, 697-700]. Here we report the distribution of SHIP-2 in mouse tissues: a Western blot analysis of mouse tissues reveals that SHIP-2 is expressed in both haemopoietic and non-haemopoietic cells. In addition to T-cell and B-cell lines, spleen, thymus and lung are shown to coexpress SHIP-1 and SHIP-2. Moreover, SHIP-2 is detected in fibroblasts, heart and different brain areas. SHIP-2 shows a maximal tyrosine phosphorylation and association to Shc after ligation of BCR to FcγRIIB but not after stimulation of BCR alone. Our results therefore suggest a possible role for SHIP-2 in the negative regulation of immunocompetent cells.

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Section: Figure 1 Alignment Of Ship-1 and Ship-2 Sequencesmentioning

confidence: 99%

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

Muraille

Pesesse

Kuntz

et al. 1999

Biochemical Journal

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“…SHIPs are tyrosine-phosphorylated proteins with several interesting features: an amino-terminal SH2 domain, a central catalytic domain and, at the carboxyl tail, several NPxY motifs [able to interact with phosphotyrosine-binding domain (PTB)] and Src homology 3-interacting prolinerich motifs (Drayer et al, 1996;Pesesse et al, 1997;Erneux et al, 1998;Majerus et al, 1999;Rohrschneider et al, 2000). Because of their ability to interact with SH2/PTB-containing protein, such as Src homology 2 domain-containing transforming protein 1 (Shc) (Pradhan and Coggeshall, 1997), and to dephosphorylate phosphatidylinositol 3,4,5-trisphosphate [PtdIns(3,4,5)P 3 ] (Drayer et al, 1996;Pesesse et al, 1998), the SHIPs have the potential to regulate the Ras/MAP kinase pathway and many, if not all, PI 3K induced events.…”

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The SH2 domain-containing 5-phosphatase SHIP2 is expressed in the germinal layers of embryo and adult mouse brain: increased expression in N-CAM-deficient mice

et al. 2001

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AbstractöThe germinative ventricular zone of embryonic brain contains neural lineage progenitor cells that give rise to neurons, astrocytes and oligodendrocytes. The ability to generate neurons persists at adulthood in restricted brain areas. During development, many growth factors exert their e¡ects by interacting with tyrosine kinase receptors and activate the phosphatidylinositol 3-kinase and the Ras/MAP kinase pathways. By its ability to modulate these pathways, the recently identi¢ed Src homology 2 domain-containing inositol polyphosphate 5-phosphatase 2, SHIP2, has the potential to regulate neuronal development. Using in situ hybridization technique with multiple synthetic oligonucleotides, we demonstrated that SHIP2 mRNA was highly expressed in the ventricular zone at early embryonic stages and subventricular zones at latter stages of brain and spinal cord and in the sympathetic chain. No signi¢cant expression was seen in di¡erentiated ¢elds. This restricted expression was maintained from embryonic day 11.5 to birth. In the periphery, large expression was detected in muscle and kidney and moderate expression in thyroid, pituitary gland, digestive system and bone. In the adult brain, SHIP2 was mainly restricted in structures containing neural stem cells such as the anterior subventricular zone, the rostral migratory stream and the olfactory tubercle. SHIP2 was also detected in the choroid plexuses and the granular layer of the cerebellum. The speci¢city of SHIP2 expression in neural stem cells was further demonstrated by (i) the dramatic increase in SHIP2 mRNA signal in neural cell adhesion molecule (N-CAM)-de¢cient mice, which present an accumulation of progenitor cells in the anterior subventricular zone and the rostral migratory stream, (ii) the abundant expression of 160-kDa SHIP2 by western blotting in proliferating neurospheres in culture and its downregulation in non-proliferating di¡erentiated neurospheres.In conclusion, the close correlation between the pattern of SHIP2 expression in the brain and the proliferative and early di¡erentiative events suggests that the phosphatase SHIP2 may have important roles in neural development. ß

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“…PI3K phosphorylates PI(4,5)P 2 to create PI(3,4,5,)P 3 [33] and SHIP2 is a negative regulator of the PI3K pathway [17] that dephosphorylates PI(3,4,5)P 3 lipids to PI(3,4)P 2 [15]. Importantly, as shown previously by us, Arap3 binds PI(3,4,5,)P 3 stronger than it binds PI(3,4)P 2 [3].…”

Section: Discussionmentioning

confidence: 99%

“…Rabbit polyclonal anti-SHIP2 antibody and sheep anti-Arap3 antibody were described before [3,15]. Where indicated, cells were stimulated with 20 ng/ml EGF (ICN Biomedicals Inc.), 1 μg/ml insulin (Sigma) and 10 μM LY294002 (Sigma).…”

Section: Antibodies and Reagentsmentioning

confidence: 99%

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The PI3K effector Arap3 interacts with the PI(3,4,5)P3 phosphatase SHIP2 in a SAM domain-dependent manner

Raaijmakers

Deneubourg

Rehmann

et al. 2007

Cellular Signalling

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Arap3 is a phosphoinositide (PI) 3 kinase effector that serves as a GTPase activating protein (GAP) for both Arf and Rho G-proteins. The protein has multiple pleckstrin homology (PH) domains that bind preferentially phosphatidyl-inositol-3,4,5-trisphosphate (PI(3,4,5,)P 3 ) to induce translocation of Arap3 to the plasma membrane upon PI3K activation. Arap3 also contains a Ras association (RA) domain that interacts with the small G-protein Rap1 and a sterile alpha motif (SAM) domain of unknown function. In a yeast two-hybrid screen for new interaction partners of Arap3, we identified the PI 5′-phosphatase SHIP2 as an interaction partner of Arap3. The interaction between Arap3 and SHIP2 was observed with endogenous proteins and shown to be mediated by the SAM domain of Arap3 and SHIP2. In vitro, these two domains show specificity for a heterodimeric interaction. Since it was shown previously that Arap3 has a higher affinity for PI(3,4,5,)P 3 than for PI(3,4)P 2 , we propose that the SAM domain of Arap3 can function to recruit a negative regulator of PI3K signaling into the effector complex.

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

Cited by 114 publications

References 14 publications

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

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

The SH2 domain-containing 5-phosphatase SHIP2 is expressed in the germinal layers of embryo and adult mouse brain: increased expression in N-CAM-deficient mice

The PI3K effector Arap3 interacts with the PI(3,4,5)P3 phosphatase SHIP2 in a SAM domain-dependent manner

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