Multiple forms of an inositol polyphosphate 5-phosphatase form signaling complexes with Shc and Grb2

Kavanaugh, W M; Pot, David; Chin, Sherry; Deuter-Reinhard, Maja; Jefferson, Anne B.; Norris, Frank A.; Masiarz, Frank R.; Cousens, Lawrence S.; Majerus, Philip W.; Williams, Lewis T.

doi:10.1016/s0960-9822(02)00511-0

Cited by 215 publications

(198 citation statements)

References 40 publications

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“…Alternative spliced forms have been described for SHIP1 (Kavanaugh et al, 1996;Rohrschneider et al, 2000; and rat SHIP2 (Ishihara et al, 1999). To test the possibility that the exonic localization of probes may a¡ect the apparent SHIP2 distribution, seven antisense probes widespreadly distributed in the mouse SHIP2 sequence (Schurmans et al, 1999) were prepared (see Experimental procedures).…”

Section: Ship2 Probe Characterization and Signal Speci¢citymentioning

confidence: 99%

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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Section: Ship2 Probe Characterization and Signal Speci¢citymentioning

confidence: 99%

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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“…A novel role for Shc has been suggested in which phosphorylation of Y239/Y240 leads to c-myc induction and suppression of apoptosis in Ba/F3 cells, in a Ras-independent manner (Gotoh et al, 1996). The Shc PTB domain binds directly to the cytoplasmic enzyme SHIP, an SH2 domain-containing inositol 5-phosphatase, in response to growth factor and cytokine stimulation in hematopoetic cells (Damen et al, 1996;Kavanaugh et al, 1996;Lioubin et al, 1996). Furthermore, proline-rich sequences in the Shc CH1 domain are proposed to mediate the interaction between Shc and the SH3 domain of eps8, a tyrosinephosphorylated protein involved in EGF receptormediated signaling (Matoskova et al, 1995;Bon®ni et al, 1996).…”

Section: Introductionmentioning

confidence: 99%

Cloning and characterization of mPAL, a novel Shc SH2 domain-binding protein expressed in proliferating cells

1999

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“…SHIP-1 encodes an inositol polyphosphate 5-phosphatase that uses Ins(1,3,4,5)P % and PtdIns(3,4,5)P $ as substrates. It is a 145 kDa tyrosine-phosphorylated protein with several interesting properties : an N-terminal SH2 domain, a central catalytic domain, two phosphotyrosine-binding (' PTB ') consensus sequences, and three putative SH3 interacting motifs at the Cterminus [9][10][11][12][13] (Figure 1). …”

Section: Introductionmentioning

confidence: 99%

“…PtdIns(3,4,5)P $ levels and Ras activity after stimulation by antigens or cytokines [9][10][11][12][13]. The ligation of BCR to FcγRIIB induces the Src kinase Lyn-dependent phosphorylation of FcγRIIB on its immunoreceptor tyrosine inhibition motif (ITIM), leading to the recruitment of SHIP-1 and its tyrosine phosphorylation [5,14].…”

Section: Introductionmentioning

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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Multiple forms of an inositol polyphosphate 5-phosphatase form signaling complexes with Shc and Grb2

Abstract: These findings strongly implicate the inositol polyphosphate 5-phosphatases in Shc- and Grb2-mediated signal transduction. Furthermore, SIP-110, SIP-130 and SIP-145 prefer 3-phosphorylated substrates, suggesting a link to the phosphatidylinositol 3-kinase signaling pathway.

Cited by 215 publications

References 40 publications

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 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

Cloning and characterization of mPAL, a novel Shc SH2 domain-binding protein expressed in proliferating 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

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