The diversity and possible functions of the inositol polyphosphate 5-phosphatases

Erneux, Christophé; Govaerts, Cédric; Communi, David; Pesesse, Xavier

doi:10.1016/s0005-2760(98)00132-5

Cited by 133 publications

(131 citation statements)

References 91 publications

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“…42,53 It has been proposed that cancer may arise in cells with impaired endocytosis as a result of enhanced cell prolifereation due to prolonging signalling by growth factors. 54 This is consistent with the recent finding that cells expressing dominant negative dynamin mutant resulting in impaired endocytosis exhibited an enhanced proliferative response to epidermal growth factor (EGF).…”

Section: Discussionmentioning

confidence: 99%

The interaction between EEN and Abi-1, two MLLfusion partners, and synaptojanin and dynamin: implications for leukaemogenesis

Cheung

et al. 2000

Leukemia

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The mixed lineage leukaemia gene, MLL (also called HRX, ALL-1) in acute leukaemia is fused to at least 16 identified partner genes that display diverse structural and biochemical properties. Using GST pull down and the yeast two hybrid system, we show that two different MLL fusion partners with SH3 domains, EEN and Abi-1, interact with dynamin and synaptojanin, both of which are involved in endocytosis. Synaptojanin, a member of the inositol phosphatase family that has recently been shown to regulate cell proliferation and survival, is also known to bind to Eps15, the mouse homologue of AF1p, another fusion partner of MLL. Expression studies show that synaptojanin is strongly expressed in bone marrow and immature leukaemic cell lines, very weakly in peripheral blood leukocytes and absent in Raji, a mature B cell line. We found that the SH3 domains of EEN and Abi-1 interact with different proline-rich domains of synaptojanin while the EH domains of Eps15 interact with the NPF motifs of synaptojanin. In vitro competitive binding assays demonstrate that EEN displays stronger binding affinity than Abi-1 and may compete with it for synaptojanin. These findings suggest a potential link between MLL fusion-mediated leukaemogenesis and the inositol-signalling pathway. Leukemia (2000) 14, 594-601.

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Section: Discussionmentioning

confidence: 99%

The interaction between EEN and Abi-1, two MLLfusion partners, and synaptojanin and dynamin: implications for leukaemogenesis

Cheung

et al. 2000

Leukemia

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“…Both SHIP1 and SHIP2 dephosphorylate the critical phospholipid PI(3,4,5)P3. Numerous studies from cell lines and knockout mice indicate that SHIP1 and SHIP2 are negative regulators of signaling, most likely due to their e ect on PI(3,4,5)P3 (Erneux et al, 1998;Helgason et al, 1998). It is puzzling that the Shc:SHIP complex is readily detected and occurs rapidly after engagement of receptors that are mitogenic.…”

Section: Role Of Shc In`negative' Signaling?mentioning

confidence: 99%

Signaling via Shc family adapter proteins

2001

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“…Distinct forms of inositol and phosphatidylinositol 5-phosphatases selectively remove the phosphate from the 5-position of the inositol ring from both soluble and lipid substrates. These enzymes, that terminate the signal transduction processes initiated by PI 3-K, are essential for proper cell function (reviewed in Erneux et al, 1998;Majerus et al, 1999). The Src homology 2 (SH2) domain-containing inositol polyphosphate 5-phosphatase (SHIP) family is a recently described subset of type II 5-phosphatase.…”

mentioning

confidence: 99%

“…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.…”

mentioning

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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The diversity and possible functions of the inositol polyphosphate 5-phosphatases

Cited by 133 publications

References 91 publications

The interaction between EEN and Abi-1, two MLLfusion partners, and synaptojanin and dynamin: implications for leukaemogenesis

The interaction between EEN and Abi-1, two MLLfusion partners, and synaptojanin and dynamin: implications for leukaemogenesis

Signaling via Shc family adapter proteins

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

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