Identification of a Second SH2-Domain-Containing Protein Closely Related to the Phosphatidylinositol Polyphosphate 5-Phosphatase SHIP

Pesesse, Xavier; Deleu, Sandrine; Smedt, Florence De; Drayer, Lyndsay; Erneux, Christophé

doi:10.1006/bbrc.1997.7538

Cited by 218 publications

(207 citation statements)

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“…The sequence of SHIP-2 (Y14385) is taken from [19]. SHIP-1 contains 1188 residues and has a predicted molecular mass of 133 kDa ; SHIP-2 contains 1258 residues and has a predicted molecular mass of 142 kDa.…”

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

confidence: 99%

“…Moreover, SHIP-1k\k splenic Bcells display prolonged Ca# + influx, increased proliferation in itro, and enhanced activation of mitogen-activated protein kinase in response to BCR-FcγRIIB ligation [18]. The cDNA of a second SHIP closely related to SHIP-1 has been cloned [19] (Figure 1). This protein, referred to as SHIP-2, displays enzymic activity comparable to that of SHIP-1.…”

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

confidence: 99%

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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%

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 Src homology 2 (SH2) domain-containing inositol polyphosphate 5-phosphatase (SHIP) family is a recently described subset of type II 5-phosphatase. 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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“…SHIP proteins are SRC homology 2 (SH2)-containing inositol 5′-phosphatase proteins with isozymes, SHIP1 and SHIP2. SHIP1 is present largely in haematopoietic cells, while SHIP2, which can thus be assumed as a major regulator, is found in skeletal muscles, among other insulin-sensitive tissues [27,37]. Studies indicate that mice deficient of SHIP2, are hypoglycemic and sensitized to insulin suggesting that SHIP2 may have an important role in negative insulin signaling [6].…”

Section: Introductionmentioning

confidence: 99%

Insights into structure and function of SHIP2-SH2: homology modeling, docking, and molecular dynamics study

Saqib

Siddiqi

2011

J Chem Biol

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SRC homology 2 (SH2)-containing inositol 5′-phosphatase protein (SHIP2) is a potential target for type 2 diabetes. Its ability to dephosphorylate the lipid messenger phosphatidylinositol 3,4,5-trisphosphate [PtdIns(3,4,5)P3], important for insulin signaling, makes it an important target against type 2 diabetes. The insulin-induced SHIP2 interaction with Shc is very important for the membrane localization and functioning of SHIP2. There is a bidentate relationship between the two proteins where two domains each from SHIP2 and Shc are involved in mutual binding. However in the present study, the SHIP2-SH2 domain binding with the phosphorylated tyrosine 317 on the collagen-homology (CH) domain of Shc, has been studied due to the indispensability of this interaction in SHIP2 localization. In the absence of the crystal structure of SHIP2-SH2, its structural model was developed followed by tracking its molecular interactions with Shc through molecular docking and dynamics studies. This study revealed much about the structural interactions between the SHIP2-SH2 and Shc-CH. Finally, docking study of a nonpeptide inhibitor into the SHIP2-SH2 domain further confirmed the structural interactions involved in ligand binding and also proposed the inhibitor as a major starting point against SHIP2-SH2 inhibition. The insights gained from the current study should prove useful in the design of more potent inhibitors against type 2 diabetes.

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Identification of a Second SH2-Domain-Containing Protein Closely Related to the Phosphatidylinositol Polyphosphate 5-Phosphatase SHIP

Cited by 218 publications

References 24 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

Insights into structure and function of SHIP2-SH2: homology modeling, docking, and molecular dynamics study

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