Structure function, and biology of SHIP proteins

Genes and Development

Volumn 14, Issue 5, 2000, Pages 505-520

  Rohrschneider, Larry R ^a   Fuller, John F ^a   Wolf, Ingrid ^a   Liu, Yan ^a   Lucas, David M ^a,b  

^a Fred Hutchinson Cancer Research Center   (United States)

^b OHIO STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

INOSITOL 5 PHOSPHATASE; PHOSPHATASE; UNCLASSIFIED DRUG;

ENZYME ACTIVITY; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN INTERACTION; PROTEIN STRUCTURE; REVIEW;

ANIMALS; B-LYMPHOCYTES; HUMANS; PHOSPHORIC MONOESTER HYDROLASES; PROTEIN ISOFORMS; SRC HOMOLOGY DOMAINS;

EID: 0034163834     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review

References (108)

1. Aman, M.J., T.D. Lamkin, H. Okada, T. Kurosaki, and K.S. Ravichandran. 1998. The inositol phosphatase SHIP inhibits Akt/PKB activation in B cells. J. Biol. Chem. 273: 33922-33928.
2. Attree, O., I.M. Olivos, I. Okabe, L.C. Bailey, D.L. Nelson, R.A. Lewis, R.R. McInnes, and R.L. Nussbaum. 1992. The Lowe's oculocerebrorenal syndrome gene encodes a protein highly homologous to inositol polyphosphate-5-phosphatase. Nature 358: 239-242.
3. Bolland, S., R.N. Pearse, T. Kurosaki, and J.V. Ravetch. 1998. SHIP modulates immune receptor responses by regulating membrane association of Btk. Immunity 8: 509-516.
4. Bruyns, C., X. Pesesse, C. Moreau, D. Blero, and C. Erneux. 1999. The two SH2-domain-containing inositol 5-phosphatases SHIP1 and SHIP2 are coexpressed in human T lymphocytes. Biol. Chem. 380: 969-974.
5. Carlberg, K. and L.R. Rohrschneider. 1997. Characterization of a novel tyrosine phosphorylated 100 kDa protein that binds to SHP-2 and phosphatidylinositol 3′-kinase in hematopoietic cells. J. Biol. Chem. 272: 15943-15950.
6. Chacko, G.W., S. Tridandapani, J.E. Damen, L. Liu, G. Krystal, and K.M. Coggeshall. 1996. Negative signaling in B lymphocytes induces tyrosine phosphorylation of the 145-kDa inositol polyphosphate 5-phosphatase, SHIP. J. Immunol. 157: 2234-2238.
7. Chung, C.D., J. Liao, B. Liu, X. Rao, P. Jay, P. Berta, and K. Shuai. 1997a. Specific inhibition of Stat3 signal transduction by PIAS3. Science 278: 1803-1805.
8. Chung, J.K., F. Sekiya, H.S. Kang, C. Lee, J.S. Han, S.R. Kim, Y.S. Bae, A.J. Morris, and S.G. Rhee. 1997b. Synaptojanin inhibition of phospholipase D activity by hydrolysis of phosphatidylinositol 4,5-bisphosphate. J. Biol. Chem. 272: 15980-15985.
9. Coggeshall, K.M. 1998. Inhibitory signaling by B cell FcgRIIb. Curr. Opin. Immunol. 10: 306-312.
10. Conley, M.E. and J. Rohrer. 1995. The spectrum of mutations in Btk that cause X-linked agammaglobulinemia. Clin. Immunol. Immunopathol. 76: S192-S197.
11. Cremona, O., G. Di Paolo, M.R. Wenk, A. Luthi, W.T. Kim, K. Takei, L. Daniell, Y. Nemoto, S.B. Shears, R.A. Flavell et al. 1999. Essential role of phosphoinositide metabolism in synaptic vesicle recycling. Cell 99: 179-188.
12. Crowley, M.T., S.L. Harmer, and A.L. DeFranco. 1996. Activation-induced association of a 145-kDa tyrosine-phosphorylated protein with Shcand Syk in B lymphocytes and macrophages. J. Biol. Chem. 271: 1145-1152.
13. Damen, J.E., L. Liu, R.L. Cutler, and G. Krystal. 1993. Erythropoietin stimulates the tyrosine phosphorylation of Shc and its association with Grb2 and a 145-Kd tyrosine phosphorylated protein. Blood 82: 2296-2303.
14. Damen, J.E., L. Liu, P. Rosten, R.K. Humphries, A.B. Jefferson, P.W. Majerus, and G. Krystal. 1996. The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase. Proc. Natl. Acad. Sci. 93: 1689-1693.
15. Damen, J.E., L. Liu, M.D. Ware, M. Ermolaeva, P.W. Majerus, and G. Krystal. 1998. Multiple forms of the SH2-containing inositol phosphatase, SHIP, are generated by C-terminal truncation. Blood 92: 1199-1205.
16. Deuter-Reinhard, M., G. Apell, D. Pot, A. Klippel, L.T. Williams, and W.M. Kavanaugh. 1997. SIP/SHIP inhibits Xenopus oocyte maturation induced by insulin and phosphatidylinositol 3-kinase. Mol. Cell. Biol. 17: 2559-2565.
17. Di Cristofano, A., B. Pesce, C. Cardon-Cardo, and P.P. Pandolfi. 1998. Pten is essential for embryonic development and tumour suppression. Nat. Genet. 19: 348-355.
18. Drachman, J.G., J.D. Griffin, and K. Kaushansky. 1995. The c-Mpl ligand (thrombopoietin) stimulates tyrosine phosphorylation of Jak2, Shc, and c-Mpl. J. Biol. Chem. 270: 4979-4982.
19. Drayer, A.L., X. Pesesse, F. De Smedt, R. Woscholski, P. Parker, and C. Erneux. 1996. Cloning and expression of a human placenta inositol 1,3,4,5-tctrakisphosphate and phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase. Biochem. Biophys. Res. Common. 225: 243-249.
20. Durbin, J.E., R. Hackenmiller, M.C. Simon, and D.E. Levy. 1996. Targeted disruption of the mouse Stat1 gene results in compromised innate immunity to viral disease. Cell 84: 443-450.
21. Fauman, E.B. and M.A. Saper. 1996. Structure and function of the protein tyrosine phosphatases. Trends Biochem. Sci. 21: 413-417.
22. Felder, S., M. Zhou, P. Hu, J. Uren̄a, A. Ullrich, M. Chaudhuri, M. White, S.E. Shoelson, and J. Schlessinger. 1993. SH2 domains exhibit high-affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchange. Mol. Cell. Biol. 13: 1449-1455.
23. 2+ following B-cell receptor activation. EMBO J. 17: 1973-1985.
24. Fukuda, M., T. Kojima, H. Kabayama, and K. Mikoshiba. 1996. Mutation of the pleckstrin homology domain of Bruton's tyrosine kinase in immunodeficiency impaired inositol 1,3,4,5-tetrakisphosphate binding capacity. J. Biol. Chem. 271: 30303-30306.
25. Geier, S.J., P.A. Algate, K. Carlberg, D. Flowers, C. Friedman, B. Trask, and L.R. Rohrschneider. 1997. The human SHIP gene is differentially expressed in cell lineages of the bone marrow and blood. Blood 89: 1876-1885.
26. Giuriato, S., B. Payrastre, A.L. Drayer, M. Plantavid, R. Woscholski, P. Parker, C. Erneux, and H. Chap. 1997. Tyrosine phosphorylation and relocation of SHIP are integrin-mediated in thrombin-stimulated human blood platelets. J. Biol. Chem. 272: 26857-26863.
27. Gu, H., J.C. Pratt, S.J. Burakoff, and B.C. Neel. 1998. Cloning of p97/Gab2, the major SHP2-binding protein in hematopoietic cells, reveals a novel pathway for cytokine-induced gene activation. Mol. Cell 2: 729-740.
28. Guilherme, A., J.K. Klarlund, G. Krystal, and M.P. Czech. 1996. Regulation of phosphatidylinositol 3,4,5-trisphosphate 5′-phosphatase activity by insulin. J. Biol. Chem. 271: 29533-29536.
29. Gupta, N., A.M. Scharenberg, D.N. Burshtyn, M.N. Lioubin, L.R. Rohrschneider, J.-P. Kinet, and E.O. Long. 1997. Negative signaling pathways of killer cell inhibitory receptors and FcγRIIb1 require distinct phosphatases. J. Exp. Med. 186: 473-478.
30. Gupta, N., A.M. Scharenberg, D.A. Fruman, L.C. Cantley, J.-P. Kinet, and E.O. Long. 1999. The SH2 domain-containing inositol 5′-phosphatase (SHIP) recruits the p85 subunit of phosphoinositide 3-kinase during FcγRIIb1-mediated inhibition of B cell receptor signaling. J. Biol. Chem. 274: 7489-7494.
31. Harmer, S.L. and A.L. DeFranco. 1999. The src homology domain 2-containing inositol phosphatase SHIP forms a ternary complex with Shcand Grb2 in antigen receptor-stimulated B lymphocytes. J. Biol. Chem. 274: 12183-12191.
32. Hejna, J.A., H. Saito, L.S. Merkens, T.V. Tittle, P.M. Jakobs, M.A. Whitney, M. Grompe, A.S. Friedberg, and R.E. Moses. 1995. Cloning and characterization of a human cDNA (IN-PPL1) sharing homology with inositol polyphosphate phosphatases. Genomics 29: 285-287.
33. Helgason, C.D., J.E. Damen, P. Rosten, R. Grewal, P. Sorenson, S.M. Chappel, A. Borowski, F. Jirik, G. Krystal, and R.K. Humphries. 1998. Targeted disruption of SHIP leads to hemopoietic perturbations, lung pathology, and a shortened life span. Genes & Dev. 12: 1610-1620.
34. 2+ mobilization is integrated by CD19 dephosphorylation. Immunity 7: 49-58.
35. Holgado-Madruga, M., D.R. Emlet, D.K. Moscatello, A.K. Godwin, and A.J. Wong. 1996. A Grb2-associated docking protein in EGF-and insulin-receptor signalling. Nature 379: 560-564.
36. Howell, B.W., L.M. Lanier, R. Frank, F.B. Gertler, and J.A. Cooper. 1999. The disabled 1 phosphotyrosine-binding domain binds to the internalization signals of transmembrane glycoproteins and to phospholipids. Mol. Cell. Biol. 19: 5179-5188.
37. Huber, M., C.D. Helgason, J.E. Damen, L. Liu, R.K. Humphries, and G. Krystal. 1998. The src homology 2-containing inositol phosphatase (SHIP) is the gatekeeper pf mast cell degranulation. Proc. Natl. Acad. Sci. 95: 11330-11335.
38. Huber, M., C.D. Helgason, J.E. Damen, M.P. Scheid, V. Duronio, V. Lam, R.K. Humphries, and G. Krystal. 1999. The role of the SRC homology 2-containing insitol 5′-phosphatase in Fc epsilon R1-induced signaling. Curr. Top. Microbiol. Immunol. 244: 29-41.
39. Huyer, G. and D.R. Alexander. 1999. Immune signalling: SHP-2 docks at multiple ports. Curr. Biol. 9: R129-R132.
40. Ingham, R.J., H. Okada, M. Dang-Lawson, J. Dinglasan, and P. van der Geer. 1999. Tyrosine phosporylation of Shc in response to B cell antigen receptor engagement depends on the SHIP inositol phosphatase. J. Immunol. 163: 5891-5895.
41. Kavanaugh, W.M. and L.T. Williams. 1994. An alternative to SH2 domains for binding tyrosine-phosphorylated proteins. Science 266: 1862-1865.
42. Kavanaugh, W.M., D.A. Pot, S.M. Chin, M. Deuter-Reinhard, A.B. Jefferson, F.A. Norris, F.R. Masiarz, L.S. Cousens, P.W. Majerus, and L.T. Williams. 1996. Multiple forms of an inositol polyphosphate 5-phosphatase form signaling complexes with Shc and Grb2. Curr. Biol. 6: 438-445.
43. Kawano, T., Y. Indo, H. Nakazato, M. Shimadzu, and I. Matsuda. 1998. Oculocerebrorenal syndrome of Lowe: Three mutations in the OCRL1 gene derived from three patients with different phenotypes. Am. J. Med. Genet. 77: 348-355.
44. Khvotchev, M. and T.C. Südhof. 1998. Developmentally regulated alternative splicing in a novel synaptojanin. J. Biol. Chem. 273: 2306-2311.
45. Kiener, P.A., M.N. Lioubin, L.R. Rohrschneider, J.A. Ledbetter, S.G. Nadler, and M.L. Diegel. 1997. Co-ligation of the antigen and Fc receptors gives rise to the selective modulation of intracellular signaling in B cells. J. Biol. Chem. 272: 3838-3844.
46. Kimura, T., H. Sakamoto, E. Appella, and R. P. Siraganian. 1997. The negative signaling molecule SH2 domain-containing inositol-polyphosphate 5-phosphatase (SHIP) binds to the tyrosine-phosphorylated beta subunit of the high affinity IgE receptor. J. Biol. Chem. 272: 13991-13996.
47. Kuroiwa, A., Y. Yamashita, M. Inui, T. Yuasa, M. Ono, A. Nagabukuro, Y. Matsuda, and T. Takai. 1998. Association of tyrosine phosphatases SHP-1 and SHP-2, inositol 5-phosphatase SHIP with gp49B1, and chromosomal assignment of the gene. J. Biol. Chem. 273: 1070-1074.
48. Kurosaki, T. 1999. Genetic analysis of B cell antigen receptor signaling. Annu. Rev. Immunol. 17: 555-592.
49. Lamkin, T.D., S.F. Walk, L. Liu, J.E. Damen, G. Krystal, and K.S. Ravichandran. 1997. Shc interaction with Src homology 2 domain containing isositol phosphatase (SHIP) in vivo requires the Shc-phosphotyrosine binding domain and two specific phosphotyrosines on SHIP. J. Biol. Chem. 272: 10396-10401.
50. Lecoq-Lafon, C., F. Verdier, S. Fichelson, S. Chrétien, S. Gisselbrecht, C. Lacombe, and P. Mayeux. 1999. Erythropoietin induces the tyrosine phosphorylation of GAB1 and its association with SHC, SHP2, SHIP, and phosphatidylinositol 3-kinase. Blood 93: 2578-2585.
51. Lewis, T.S., P.S. Shapiro, and N.G. Ahn. 1998. Signal transduction through MAPK cascades. Adv. Cancer Res. 74: 49-139.
52. Li, J., C. Yen, D. Liaw, K. Podsypanina, S. Bose, S.I. Wang, J. Puc, C. Miliaresis, L. Rodgers, R. McCombie et al. 1997. PTEN, a putative protein tyrosine phosphatase gene mutated in human brain, breast, and prostate cancer. Science 275: 1943-1947.
53. Lioubin, M.N., G.M. Myles, K. Carlberg, D. Bowtell, and L.R. Rohrschneider. 1994. SHC, GRB2, SOS1 and a 150-kilodalton tyrosine-phosphorylated protein form complexes with Fms in hematopoietic cells. Mol. Cell. Biol. 14: 5682-5691.
54. Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity. Genes & Dev. 10: 1084-1095.
55. Liu, B., J. Liao, X. Rao, S.A. Kushner, C.D. Chung, D.D. Chang, and K. Shuai. 1998. Inhibition of Stat1-mediated gene activation by PIAS1. Proc. Natl. Acad. Sci. 95: 10626-10631.
56. Liu, L., J.E. Damen, R.L. Cutler, and G. Krystal. 1994. Multiple cytokines stimulate the binding of a common 145-kilodalton protein to Shc at the Grb2 recognition site of Shc. Mol. Cell. Biol. 14: 6926-6935.
57. Liu, L., J.E. Damen, M.R. Hughes, I. Babic, F.R. Jirik, and G. Krystal. 1997a. The Src homology 2 (SH2) domain of SH2-containing inositol phosphatase (SHIP) is essential for tyrosine phosphorylation of SHIP, its association with Shc, and its induction of apoptosis. J. Biol. Chem. 272: 8983-8988.
58. Liu, L., J. E. Damen, M.D. Ware, and G. Krystal. 1997b. Interleuken-3 induces the association of the inositol 5-phosphatase SHIP with SHP2. J. Biol. Chem. 272: 10998-11001.
59. Liu, Q., Amgen E.S.T. Program, and D.J. Dumont. 1997. Molecular cloning and chromosomal localization in human and mouse of the SH2-containing inositol phosphatase, INPP5D (SHIP). Genomics 39: 109-112.
60. Liu, Q., F. Shalaby, J. Jones, D. Bouchard, and D.J. Dumont. 1998. The SH2-containing inositol polyphosphate 5-phosphatase, Ship, is expressed during hematopoiesis and spermatogenesis. Blood 91: 2753-2759.
61. Liu, Q., T. Sasaki, I. Kozieradzki, A. Wakeham, A. Itie, D.J. Dumont, and J.M. Penninger. 1999. SHIP is a negative regulator of growth factor receptor-mediated PKB/Akt activation and myeloid cell survival. Genes & Dev. 13: 786-791.
62. Lucas, D.M. and L.R. Rohrschneider. 1999. A novel spliced form of SH2-containing inositol phosphatase SHIP is expressed during myeloid development. Blood 93: 1922-1933.
63. Maehama, T. and J.E. Dixon. 1999. PTEN: A tumour suppressor that functions as a phospholid phosphatase. Trends Cell Biol. 9: 125-128.
64. Majerus, P.W., M.V. Kisseleva, and F.A. Norris. 1999. The role of phosphatases in inositol signaling reactions. J. Biol. Chem. 274: 10669-10672.
65. Maresco, D.L., J.M. Osborne, D. Cooney, K.M. Coggeshall, and C.L. Anderson. 1999. The SH2-containing 5′-inositol phosphatase (SHIP) is tyrosine phosphorylated after Fc gamma receptor clustering in monocytes. J. Immunol. 162: 6458-6465.
66. BCR/ABL. J. Biol. Chem. 269: 5016-5021.
67. McPherson, P.S., E.P. Garcia, V.I. Slepnev, C. David, X. Zhang, D. Grabs, W.S. Sossin, R. Bauerfeind, Y. Nemeto, and P. De Camilli. 1996. A presynaptic inositol-5-phosphatase. Nature 379: 353-357.
68. Myers, M.P., J.P. Stolarov, C. Eng, J. Li, S.I. Wang, M.H. Wigler, R. Parsons, and N.K. Tonks. 1997. PTEN, the tumor suppressor from human chromosome 10q23, is a dual-specificity phosphatase. Proc. Natl. Acad. Sci. 94: 9052-9057.
69. Nemoto, Y. and P. De Camilli. 1999. Recruitment of an alternatively spliced form of synaptojanin 2 to mitochondria by the interaction with the PDZ domain of a mitochondrial outer membrane protein. EMBO J. 18: 2991-3006.
70. Nemoto, Y., M. Arribas, C. Haffner, and P. De Camilli. 1997. Synaptojanin 2, a novel synaptojanin isoform with a distinct targeting domain and expression pattern. J. Biol. Chem. 272: 30817-30821.
71. Nishida, K., Y. Yoshida, M. Itoh, T. Fukada, T. Ohtani, T. Shirogane, T. Atsumi, M. Takahashi-Tezuka, K. Ishihara, M. Hibi, and T. Hirano. 1999. Gab-family adapter proteins act downstream of cytokine and growth factor receptors and T-and B-cell antigen receptors. Blood 93: 1809-1816.
72. Norris, F., V. Auethavekiat and P.W. Majerus. 1995. The isolation and characterization of cDNA encoding human and rat brain inositol polyphosphate 4-phosphatase. J. Biol. Chem. 270: 16128-16133.
73. Norris, F. A., R.C. Atkins, and P.W. Majerus. 1997. Inositol polyphosphate 4-phosphatase is inactivated by Calpain-mediated ptoteolysis in stimulated human platelets. J. Biol. Chem. 272: 10987-10989.
74. Odai, H., K. Sasaki, A. Iwamatsu, T. Nakamoto, H. Ueno, T. Yamagata, K. Mitani, Y. Yazaki, and H. Hirai. 1997. Purification and molecular cloning of SH2-and SH3-containing inositol polyphosphate-5-phosphatase, which is involved in the signaling pathway of granulocyte-macrophage colony-stimulating factor, erythropoietin, and Bcr-Abl. Blood 89: 2745-2756.
75. 2+ oscillatory response. J. Immunol. 161: 5129-5132.
76. Ono, M., S. Bolland, P. Tempst, and J. . Ravetch. 1996. Role of the inositol phosphatase SHIP in negative regulation of the immune system by the receptor FcγRIIB. Nature 383: 263-266.
77. Ono, M., H. Okada, S. Bolland, S. Yanagi, T. Kurosaki, and J.V. Ravetch. 1997. Deletion of SHIP or SHP-1 reveals two distinct pathways for inhibitory signaling. Cell 90: 293-301.
78. Osborne, M.A., G. Zenner, M. Lubinus, X. Zhang, Z. Songyang, L.C. Cantley, P. Majerus, P. Burn, and J.P. Kochan. 1996. The inositol 5′-phosphatase SHIP binds to immunoreceptor signaling motifs and responds to high affinity IgE receptor aggregation. J. Biol. Chem. 271: 29271-29278.
79. Pesesse, X., S. Deleu, F. De Smedt, L. Drayer, and C. Erneux. 1997. Identification of a second SH2-domain-containing protein closely related to the phosphatidylinositol polyphosphate 5-phosphatase SHIP. Biochem. Biophys. Res. Comm. 239: 697-700.
80. Podsypanina, K., L.H. Ellenson, A. Nemes, J. Gu, M. Tamura, K.M. Yamada, C. Cordon-Cardo, G. Catoretti, P.E. Fisher, and R. Parsons. 1999. Mutation of Pten/Mmac1 in mice causes neoplasia in multiple organ systems. Proc. Natl. Acad. Sci. 96: 1563-1568.
81. Pradhan, M. and K. M. Coggeshall. 1997. Activation-induced bi-dentate interaction of SHIP and Shc in B lymphocytes. J. Cell. Biochem. 67: 32-42.
82. Rameh, L.E., A.K. Arvidsson, K.L. Carraway III, A.D. Couvillon, G. Rathbun, A. Crompton, B. VanRenterghem, M.P. Czech, K.S. Ravichandran, S.J. Burakoff et al. 1997. A comparative analysis of the phosphoinositide binding specificity of pleckstrin homology domains. J. Biol. Chem. 272: 22059-22066.
83. Rawlings, D.J. and O.N. Witte. 1994. Bruton's tyrosine kinase is a key regulator in B cell development. Immunol. Rev. 138: 105-119.
84. _. 1995. The Btk subfamily of cytoplasmic tyrosine kinases: Structure, regulation, and function. Semin. Immunol. 7: 237-246.
85. Rohrschneider, L.R. and D. Metcalf. 1989. Induction of macrophage colony stimulating factor-dependent growth and differentiation after introduction of the murine c-fms gene into FDC-P1 cells. Mol. Cell. Biol. 9: 5081-5092.
86. Rozakis-Adcock, M., J. McGlade, G. Mbamula, G. Pelicci, R. Daly, W. Li, A. Batzer, S. Thomas, J. Brugge, P. G. Pelicci et al. 1992. Association of the Shcand Grb2/Sem5 SH2-containing proteins is implicated in activation of the Ras pathway by tyrosine kinases. Nature 360: 689-692.
87. Saito, T. 1998. Negative regulation of T cell activation. Curr. Opin. Immunol. 10: 313-321.
88. Salim, K., M.J. Bottomley, E. Querfurth, M.J. Zvelebil, I. Gout, R. Scaife, R.L. Margolis, R. Gigg, C.I.E. Smith, P.C. Driscoll et al. 1996. Distinct specificity in the recognition of phosphoinositides by the pleckstrin homology domains of dynamin and Bruton's tyrosine kinase. EMBO J. 15: 6241-6250.
89. Sattler, M., R. Salgia, G. Shrikhande, S. Verma, J.-L. Choi, L.R. Rohrschneider, and J.D. Griffin. 1997. The phosphatidylinositol polyphosphate 5-phosphatase SHIP and the protein tyrosine phosphatase SHP2 form a complex in hematopoietic cells which can be regulated by BCR/ABL and growth factors. Oncogene 15: 2379-2384.
90. Sattler, M., S. Verma, C.H. Byrne, G. Shrikhande, T. Winkler, P.A. Algate, L.R. Rohrschneider, and J.D. Griffin. 1999. BCR/ABL directly inhibits expression of SHIP, an SH2-containing polyinositol-5-phosphatase involved in the regulation of hematopoiesis. Mol. Cell. Biol. 19: 7473-7480.
91. Saxton, T.M., I. van Oostveen, D. Bowtell, R. Aebersold, and M.R. Gold. 1994. B cell antigen receptor cross-linking induces phosphorylation of the p21iras oncoprotein activators SHC and mSOS1 as well as assembly of complexes containing SHC, GRB-2, mSOS1, and a 145-kDa tyrosine-phosphorylated protein. J. Immunol. 153: 623-636.
92. Schaffhausen, B. 1995. SH2 domain structure and function. Biochim. Biophys. Acta 1242: 61-75.
93. 3)/Tec kinase-dependent calcium signaling pathway: A target for SHIP-mediated inhibitory signals. EMBO J. 17: 1961-1972.
94. Seet, L.F., S. Cho, A. Hessel, and D.J. Dumont. 1998. Molecular cloning of multiple isoforms of synaptojanin 2 and assignment of the gene to mouse chromosome 17A2-3.1. Biochem. Biophys. Res. Comm. 247: 116-122.
95. Songyang, Z., S.E. Shoelson, M. Chaudhuri, G. Gish, T. Pawson, W.G. Haser, F. King, T. Roberts, S. Ratnofsky, R.J. Lechleider et al. 1993. SH2 domains recognize specific phosphopeptide sequences. Cell 72: 767-778.
96. Steck, P.A., M.A. Pershouse, S.A. Jasser, W.K.A. Yung, H. Lin, A.H. Ligon, L.A. Langford, M.L. Baumgard, T. Hattier, T. Davis et al. 1997. Identification of a candidate tumor suppressor gene, MMAC1, at chromosome 10q23.3 that is mutated in multiple advanced cancers. Nat. Genet. 15: 356-362.
97. Stephens, L., K. Anderson, D. Stokoe, H. Erdjument-Bromage, G.F. Painter, A.B. Holmes, P.R.J. Gaffney, C.B. Reese, F. McCormick, P. Tempst et al. 1998. Protein kinase B kinases that mediate phosphatidylInositol 3,4,5-trisphosphate-dependent activation of protein kinase B. Science 279: 710-715.
98. Suzuki, A., J.L. de la Pompa, V. Stambolic, A.J. Elia, T. Sasaki, I.d.B. Barrantes, A. Ho, A. Wakeham, A. Itie, W. Khoo et al. 1998. High cancer susceptibility and embryonic lethality associated with mutation of the PTEN tumor suppressor gene in mice. Curr. Biol. 8: 1169-1178.
99. Tridandapani, S., G.W. Chacko, J.R. Van Brocklyn, and K.M. Coggeshall. 1997. Negative signalling in B cells causes reduced Ras activity by reducing Shc-Grb2 interactions. J. Immunol. 158: 1125-1132.
100. Tridandapani, S., M. Pradhan, J.R. LaDine, S. Garber, C.L. Anderson, and K.M. Coggeshall. 1999. Protein interactions of Src homology 2 (SH2) domain-containing inositol phosphatase (SHIP): Association with Shcdisplaces SHIP from FcγRIIb in B cells. J. Immunol. 162: 1408-1414.
101. Unkeless, J.C. and J. Jin. 1997. Inhibitory receptors, ITIM sequences and phospatases. Curr. Opin. Immunol. 9: 338-343.
102. van der Geer, P. and T. Pawson. 1995. The PTB domain: A new protein module implicated in signal transduction. Trends Biochem. Sci. 20: 277-280.
103. Vély, F., S. Olivero, L. Olcese, A. Moretta, J.E. Damen, L. Liu, G. Krystal, J.C. Cambier, M. Daëron, and E. Vivier. 1997. Differential association of phosphatases with hematopoietic co-receptors bearing immunoreceptor tyrosine-based inhibition motifs. Eur. J. Immunol. 27: 1994-2000.
104. Ware, M.D., P. Rosten, J.E. Damen, L. Liu, K. Humphries, and G. Krystal. 1996. Cloning and characterization of human SHIP, the 145-kD inositol 5-phosphatase that associates with SHC after cytokine stimulation. Blood 88: 2833-2840.
105. Wisniewski, D., A. Strife, S. Swendeman, H. Erdjument-Bromage, S. Geromanos, W.M. Kavanaugh, P. Tempst, and B. Clarkson. 1999. A novel SH2-containing phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase (SHIP2) is constitutively tyrosine phosphorylated and associated with src homologous and collagen gene (SHC) in chronic myelogenous leukemia progenitor cells. Blood 93: 2707-2720.
106. dok in negative regulation of B cell receptor-mediated signaling. Genes & Dev. 14: 11-16.
107. 5Arg catalytic motif in phosphoester hydrolysis. Biochemistry 33: 15266-15270.
108. 124 in the dual specificity phosphatase VHR. J. Biol. Chem. 269: 28084-28090.