Enzymatic and non-enzymatic activities of SHIP-1 in signal transduction and cancer

Biochemical Pharmacology

Volumn 82, Issue 10, 2011, Pages 1320-1334

  Condé, Claude ^a   Gloire, Geoffrey ^a   Piette, Jacques ^a  

^a UNIVERSITY OF LIÈGE   (Belgium)

Author keywords

Dok 1 2; Grb2; immune response; Shc; SHIP 1

Indexed keywords

B LYMPHOCYTE RECEPTOR; CD28 ANTIGEN; CD3 ANTIGEN; COLONY STIMULATING FACTOR 1; ENDOTOXIN; FC RECEPTOR IIB; IMMUNOGLOBULIN E; INTERLEUKIN 4; ISOPROTEIN; MICRORNA; MICRORNA 155; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3 KINASE SHIP1; PROTEIN KINASE LYN; PROTEIN SH2; PROTEIN SHC; RAS PROTEIN; STRESS ACTIVATED PROTEIN KINASE; UNCLASSIFIED DRUG; CD16 ANTIGEN; FC RECEPTOR; FC RECEPTOR I; INOSITOL 1,4,5 TRISPHOSPHATE 5 PHOSPHATASE; INOSITOL TRISPHOSPHATE; LAT PROTEIN; PHOSPHATIDYL INOSITOL TRIPHOSPHATE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 5 PHOSPHATASE 1; PHOSPHORYLASE; PHOSPHORYLASE ITIM; PROLINE; PROTEIN TYROSINE PHOSPHATASE SHP;

B LYMPHOCYTE; BONE MARROW TRANSPLANTATION; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CONFERENCE PAPER; CYTOTOXICITY; ENZYME ACTIVATION; ENZYME ACTIVITY; HUMAN; MACROPHAGE; MAST CELL; MONOCYTE; MULTIPLE MYELOMA; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN PHOSPHORYLATION; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION; SPLICEOSOME; T LYMPHOCYTE ACTIVATION; CELL ACTIVATION; ENZYME PHOSPHORYLATION; ENZYME STRUCTURE; IMMUNOCOMPETENT CELL; MACROPHAGE ACTIVATION; NATURAL KILLER CELL; REGULATORY MECHANISM;

ANIMALS; GENE EXPRESSION REGULATION, NEOPLASTIC; HUMANS; ISOENZYMES; MICRORNAS; NEOPLASMS; PHOSPHORIC MONOESTER HYDROLASES; SIGNAL TRANSDUCTION;

EID: 80054678671     PISSN: 00062952     EISSN: 18732968     Source Type: Journal    
DOI: 10.1016/j.bcp.2011.05.031     Document Type: Conference Paper

References (102)

1. B.D. Manning, and L.C. Cantley AKT/PKB signaling: navigating downstream Cell 129 2007 1261 1274 (Pubitemid 46962095)
2. P. Liu, H. Cheng, T.M. Roberts, and J.J. Zhao Targeting the phosphoinositide 3-kinase pathway in cancer Nat Rev Drug Discov 8 2009 627 644
3. L.M. Sly, M.J. Rauh, J. Kalesnikoff, T. Buchse, and G. Krystal SHIP, SHIP2, and PTEN activities are regulated in vivo by modulation of their protein levels: SHIP is up-regulated in macrophages and mast cells by lipopolysaccharide Exp Hematol 31 2003 1170 1181 (Pubitemid 37510021)
4. L. Liu, J.E. Damen, R.L. Cutler, and G. Krystal Multiple cytokines stimulate the binding of a common 145-kD protein to Shc at the Grb2 recognition site of Shc Mol Cell Biol 14 1994 6926 6935 (Pubitemid 24299762)
5. M.N. Lioubin, G.M. Myles, K. Carlberg, D. Bowtell, and L.R. Rohrschneider Shc, Grb2, Sos1, and a 150-kD tyrosine-phosphorylated protein form complexes with Fms in hematopoietic cells Mol Cell Biol 14 1994 5682 5691 (Pubitemid 24264396)
6. J.E. Damen, L. Liu, P. Rosten, R.K. Humphries, A.B. Jefferson, and P.W. Majerus The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-triphosphate 5-phosphatase Proc Natl Acad Sci USA 93 1996 1689 1693
7. M.N. Lioubin, P.A. Algate, S. Tsai, K. Carlberg, A. Aebersold, and L.R. Rohrschneider p150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity Genes Dev 10 1996 1084 1095
8. W.M. Kavanaugh, D.A. Pot, S.M. Chin, M. Deuter-Reinhard, A.B. Jefferson, and F.A. Norris Multiple forms of an inositol polyphosphate 5-phosphatase form signaling complexes with Shc and Grb2 Curr Biol 6 1996 438 445 (Pubitemid 126656291)
9. A.M. Brauweiler, I. Tamir, and J.C. Cambier Bilevel control of B-cell activation by the inositol 5-phosphatase SHIP Immunol Rev 176 2000 69 74
10. I. Daigle, S. Yousefi, M. Colonna, D.R. Green, and H.U. Simon Death receptors bind SHP-1 and block cytokine-induced anti-apoptotic signaling in neutrophils Nat Med 8 2002 61 67 (Pubitemid 34101730)
11. Q. Liu, A.J. Oliveira-Dos-Santos, S. Mariathasan, D. Bouchard, J. Jones, and R. Sarao The inositol polyphosphate 5-phosphatase ship is a crucial negative regulator of B cell antigen receptor signaling J Exp Med 188 1998 1333 1342 (Pubitemid 28478021)
12. R.N. Pearse, T. Kawabe, S. Bolland, R. Guinamard, T. Kurosaki, and J.V. Ravetch SHIP recruitment attenuates Fc gamma RIIB-induced B cell apoptosis Immunity 10 1999 753 760 (Pubitemid 29302928)
13. M.A. Osborne, G. Zenner, M. Lubinus, X. Zhang, Z. Songyang, and L.C. Cantley The inositol 5′-phosphatase SHIP binds to immunoreceptor signaling motifs and responds to high affinity IgE receptor aggregation J Biol Chem 271 1996 29271 29278 (Pubitemid 26382640)
14. J.D. Robson, D. Davidson, and A. Veillette Inhibition of the Jun N-terminal protein kinase pathway by SHIP-1, a lipid phosphatase that interacts with the adaptor molecule Dok-3 Mol Cell Biol 24 2004 2332 2343 (Pubitemid 38325990)
15. H. Odai, K. Sasaki, A. Iwamatsu, T. Nakamoto, H. Ueno, and T. Yamagata 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 1997 2745 2756 (Pubitemid 27172559)
16. M.J. Aman, S.F. Walk, M.E. March, H.P. Su, D.J. Carver, and K.S. Ravichandran Essential role for the C-terminal noncatalytic region of SHIP in FcgammaRIIB1-mediated inhibitory signaling Mol Cell Biol 20 2000 3576 3589 (Pubitemid 30243903)
17. J.E. Damen, M.D. Ware, J. Kalesnikoff, M.R. Hughes, and G. Krystal SHIP's C-terminus is essential for its hydrolysis of PIP3 and inhibition of mast cell degranulation Blood 97 2001 1343 1351 (Pubitemid 32183758)
18. T.D. Lamkin, S.F. Walk, L. Liu, J.E. Damen, G. Krystal, and K.S. Ravichandran Shc interaction with Src homology 2 domain containing inositol phosphatase (SHIP) in vivo requires the Shc-phosphotyrosine binding domain and two specific phosphotyrosines on SHIP J Biol Chem 272 1997 10396 10401
19. S. Dong, B. Corre, E. Foulon, E. Dufour, A. Veillette, and O. Acuto T cell receptor for antigen induces linker for activation of T cell-dependent activation of a negative signaling complex involving Dok-2 SHIP-1, and Grb-2 J Exp Med 203 2006 2509 2518 (Pubitemid 44664620)
20. I. Tamir, J.C. Stolpa, C.D. Helgason, K. Nakamura, P. Bruhns, and M. Daeron The RasGAP-binding protein p62dok is a mediator of inhibitory FcgammaRIIB signals in B cells Immunity 12 2000 347 358
21. A.K. Boer, A.L. Drayer, and E. Vellenga Effects of overexpression of the SH2-containing inositol phosphatase SHIP on proliferation and apoptosis of erythroid AS-E2 cells Leukemia 15 2001 1750 1757 (Pubitemid 33061843)
22. H. Phee, A. Jacob, and K.M. Coggeshall Enzymatic activity of the Src homology 2 domain-containing inositol phosphatase is regulated by a plasma membrane location J Biol Chem 275 2000 19090 19097 (Pubitemid 30422877)
23. C.P. Baran, S. Tridandapani, C.D. Helgason, R.K. Humphries, G. Krystal, and C.B. Marsh The inositol 5′-phosphatase SHIP-1 and the Src kinase Lyn negatively regulate macrophage colony-stimulating factor-induced Akt activity J Biol Chem 278 2003 38628 38636 (Pubitemid 37221760)
24. J. Ruschmann, V. Ho, F. Antignano, E. Kuroda, V. Lam, and M. Ibaraki Tyrosine phosphorylation of SHIP promotes its proteasomal degradation Exp Hematol 38 2010 392 402
25. C.J. Ong, A. Ming-Lum, M. Nodwell, A. Ghanipour, L. Yang, and D.E. Williams Small-molecule agonists of SHIP1 inhibit the phosphoinositide 3-kinase pathway in hematopoietic cells Blood 110 2007 1942 1949 (Pubitemid 47443908)
26. Q. Liu, F. Shalaby, J. Jones, D. Bouchard, and D.J. Dumont The SH2-containing inositol polyphosphate 5-phosphatase, SHIP, is expressed during hematopoiesis and spermatogenesis Blood 91 1998 2753 2759 (Pubitemid 28227525)
27. S.J. Geier, P.A. Algate, K. Carlberg, D. Flowers, C. Friedman, and B. Trask The human SHIP gene is differentially expressed in cell lineages of the bone marrow and blood Blood 89 1997 1876 1885 (Pubitemid 27132101)
28. D.M. Lucas, and L.R. Rohrschneider A novel spliced form of SH2-containing inositol phosphatase is expressed during myeloid development Blood 93 1999 1922 1933 (Pubitemid 29128494)
29. I. Wolf, D.M. Lucas, P.A. Algate, and L.R. Rohrschneider Cloning of the genomic locus of mouse SH2 containing inositol 5-phosphatase (SHIP) and a novel 110-kDa splice isoform, SHIPdelta Genomics 69 2000 104 112
30. Z. Tu, J.M. Ninos, Z. Ma, J.W. Wang, M.P. Lemos, and C. Desponts Embryonic and hematopoietic stem cells express a novel SH2-containing inositol 5′-phosphatase isoform that partners with the Grb2 adapter protein Blood 98 2001 2028 2038
31. L.R. Rohrschneider, J.M. Custodio, T.A. Anderson, C.P. Miller, and H. Gu The intron 5/6 promoter region of the SHIP1 gene regulates expression in stem/progenitor cells of the mouse embryo Dev Biol 283 2005 503 521 (Pubitemid 40977966)
32. N.Y. Nguyen, M.J. Maxwell, L.M. Ooms, E.M. Davies, A.A. Hilton, and J.E. Collinge An ENU-induced mouse mutant of SHIP1 reveals a critical role of the stem cell isoform for suppression of macrophage activation Blood 2011
33. J.E. Damen, L. Liu, M.D. Ware, M. Ermolaeva, P.W. Majerus, and G. Krystal Multiple forms of the SH2-containing inositol phosphatase, SHIP, are generated by C-terminal truncation Blood 92 1998 1199 1205 (Pubitemid 28369033)
34. S. Horn, J. Meyer, J. Heukeshoven, B. Fehse, C. Schulze, and S. Li The inositol 5-phosphatase SHIP is expressed as 145 and 135 kDa proteins in blood and bone marrow cells in vivo, whereas carboxyl-truncated forms of SHIP are generated by proteolytic cleavage in vitro Leukemia 15 2001 112 120 (Pubitemid 32124075)
35. X. Pesesse, S. Deleu, F. De Smedt, L. Drayer, and C. Erneux Identification of a second SH2-domain-containing protein closely related to the phosphatidylinositol polyphosphate 5-phosphatase SHIP Biochem Biophys Res Commun 239 1997 697 700 (Pubitemid 27504164)
36. J.M. Dyson, A.M. Kong, F. Wiradjaja, M.V. Astle, R. Gurung, and C.A. Mitchell The SH2 domain containing inositol polyphosphate 5-phosphatase-2: SHIP2 Int J Biochem Cell Biol 37 2005 2260 2265 (Pubitemid 41207398)
37. T. Wada, T. Sasaoka, M. Funaki, H. Hori, S. Murakami, and M. Ishiki Overexpression of SH2-containing inositol phosphatase 2 results in negative regulation of insulin-induced metabolic actions in 3T3-L1 adipocytes via its 5′-phosphatase catalytic activity Mol Cell Biol 21 2001 1633 1646 (Pubitemid 32156383)
38. S. Kagawa, Y. Soeda, H. Ishihara, T. Oya, M. Sasahara, and S. Yaguchi Impact of transgenic overexpression of SH2-containing inositol 5′-phosphatase 2 on glucose metabolism and insulin signaling in mice Endocrinology 149 2008 642 650 (Pubitemid 351159340)
39. T. Sasaoka, H. Hori, T. Wada, M. Ishiki, T. Haruta, and H. Ishihara SH2-containing inositol phosphatase 2 negatively regulates insulin-induced glycogen synthesis in L6 myotubes Diabetologia 44 2001 1258 1267 (Pubitemid 33010502)
40. S. Clement, U. Krause, F. Desmedt, J.F. Tanti, J. Behrends, and X. Pesesse The lipid phosphatase SHIP2 controls insulin sensitivity Nature 409 2001 92 97 (Pubitemid 32098631)
41. S. Clement, U. Krause, F. Desmedt, J.F. Tanti, J. Behrends, and X. Pesesse Corrigendum: The lipid phosphatase SHIP2 controls insulin sensitivity Nature 431 2004 878 (Pubitemid 39434087)
42. M.W. Sleeman, K.E. Wortley, K.M. Lai, L.C. Gowen, J. Kintner, and W.O. Kline Absence of the lipid phosphatase SHIP2 confers resistance to dietary obesity Nat Med 11 2005 199 205 (Pubitemid 40321356)
43. C.D. Helgason, J.E. Damen, P. Rosten, R. Grewal, P. Sorensen, and S.M. Chappel Targeted disruption of SHIP leads to hemopoietic perturbations, lung pathology, and a shortened life span Genes Dev 12 1998 1610 1620 (Pubitemid 28299513)
44. Q. Liu, T. Sasaki, I. Kozieradzki, A. Wakeham, A. Itie, and D.J. Dumont SHIP is a negative regulator of growth factor receptor-mediated PKB/Akt activation and myeloid cell survival Genes Dev 13 1999 786 791 (Pubitemid 29169837)
45. C.D. Helgason, C.P. Kalberer, J.E. Damen, S.M. Chappel, N. Pineault, and G. Krystal A dual role for Src homology 2 domain-containing inositol-5- phosphatase (SHIP) in immunity: aberrant development and enhanced function of b lymphocytes in ship -/- mice J Exp Med 191 2000 781 794
46. N.R. Fortenbery, K.H. Paraiso, M. Taniguchi, C. Brooks, L. Ibrahim, and W.G. Kerr SHIP influences signals from CD48 and MHC class I ligands that regulate NK cell homeostasis, effector function, and repertoire formation J Immunol 184 2010 5065 5074
47. J.W. Wang, J.M. Howson, T. Ghansah, C. Desponts, J.M. Ninos, and S.L. May Influence of SHIP on the NK repertoire and allogeneic bone marrow transplantation Science 295 2002 2094 2097 (Pubitemid 34229475)
48. M.M. Collazo, D. Wood, K.H. Paraiso, E. Lund, R.W. Engelman, and C.T. Le SHIP limits immunoregulatory capacity in the T-cell compartment Blood 113 2009 2934 2944
49. M. Kashiwada, G. Cattoretti, L. McKeag, T. Rouse, B.M. Showalter, and U. Al-Alem Downstream of tyrosine kinases-1 and Src homology 2-containing inositol 5′-phosphatase are required for regulation of CD4+ CD25+ T cell development J Immunol 176 2006 3958 3965 (Pubitemid 44264373)
50. E. Charlier, C. Conde, J. Zhang, L. Deneubourg, E. Di Valentin, and S. Rahmouni SHIP-1 inhibits CD95/APO-1/Fas-induced apoptosis in primary T lymphocytes and T leukemic cells by promoting CD95 glycosylation independently of its phosphatase activity Leukemia 24 2010 821 832
51. N.R. Locke, S.J. Patterson, M.J. Hamilton, L.M. Sly, G. Krystal, and M.K. Levings SHIP regulates the reciprocal development of T regulatory and Th17 cells J Immunol 183 2009 975 983
52. T. Tarasenko, H.K. Kole, A.W. Chi, M.M. Mentink-Kane, T.A. Wynn, and S. Bolland T cell-specific deletion of the inositol phosphatase SHIP reveals its role in regulating Th1/Th2 and cytotoxic responses Proc Natl Acad Sci USA 104 2007 11382 11387 (Pubitemid 47175149)
53. P.S. Eis, W. Tam, L. Sun, A. Chadburn, Z. Li, and M.F. Gomez Accumulation of miR-155 and BIC RNA in human B cell lymphomas Proc Natl Acad Sci USA 102 2005 3627 3632 (Pubitemid 40354662)
54. S. Costinean, N. Zanesi, Y. Pekarsky, E. Tili, S. Volinia, and N. Heerema Pre-B cell proliferation and lymphoblastic leukemia/high-grade lymphoma in E(mu)-miR155 transgenic mice Proc Natl Acad Sci USA 103 2006 7024 7029
55. S. Costinean, S.K. Sandhu, I.M. Pedersen, E. Tili, R. Trotta, and D. Perrotti Src homology 2 domain-containing inositol-5-phosphatase and CCAAT enhancer-binding protein beta are targeted by miR-155 in B cells of Emicro-MiR-155 transgenic mice Blood 114 2009 1374 1382
56. R.M. O'Connell, A.A. Chaudhuri, D.S. Rao, and D. Baltimore Inositol phosphatase SHIP1 is a primary target of miR-155 Proc Natl Acad Sci USA 106 2009 7113 7118
57. I.M. Pedersen, D. Otero, E. Kao, A.V. Miletic, C. Hother, and E. Ralfkiaer Onco-miR-155 targets SHIP1 to promote TNFalpha-dependent growth of B cell lymphomas EMBO Mol Med 1 2009 288 295
58. R.M. O'Connell, D.S. Rao, A.A. Chaudhuri, M.P. Boldin, K.D. Taganov, and J. Nicoll Sustained expression of microRNA-155 in hematopoietic stem cells causes a myeloproliferative disorder J Exp Med 205 2008 585 594 (Pubitemid 351439306)
59. J.M. Luo, H. Yoshida, S. Komura, N. Ohishi, L. Pan, and K. Shigeno Possible dominant-negative mutation of the SHIP gene in acute myeloid leukemia Leukemia 17 2003 1 8 (Pubitemid 36175881)
60. 2+ mobilization is integrated by CD19 dephosphorylation Immunity 7 1997 49 58 (Pubitemid 27357264)
61. K. Okkenhaug, and B. Vanhaesebroeck PI3K in lymphocyte development, differentiation and activation Nat Rev Immunol 3 2003 317 330 (Pubitemid 37328684)
62. S. Tridandapani, M. Pradhan, J.R. LaDine, S. Garber, C.L. Anderson, and K.M. Coggeshall Protein interactions of Src homology 2 (SH2) domain-containing inositol phosphatase (SHIP): association with Shc displaces SHIP from FcgammaRIIb in B cells J Immunol 162 1999 1408 1414 (Pubitemid 29307012)
63. I. Isnardi, P. Bruhns, G. Bismuth, W.H. Fridman, and M. Daeron The SH2 domain-containing inositol 5-phosphatase SHIP1 is recruited to the intracytoplasmic domain of human FcgammaRIIB and is mandatory for negative regulation of B cell activation Immunol Lett 104 2006 156 165 (Pubitemid 43330722)
64. S. Bolland, R.N. Pearse, T. Kurosaki, and J.V. Ravetch SHIP modulates immune receptor responses by regulating membrane association of Btk Immunity 8 1998 509 516 (Pubitemid 28196804)
65. S. Tridandapani, H. Phee, L. Shivakumar, T.W. Kelley, and K.M. Coggeshall Role of SHIP in FcgammaRIIb-mediated inhibition of Ras activation in B cells Mol Immunol 35 1998 1135 1146 (Pubitemid 29057152)
66. K. Neumann, T. Oellerich, I. Heine, H. Urlaub, and M. Engelke Fc gamma receptor IIb modulates the molecular Grb2 interaction network in activated B cells Cell Signal 23 2011 893 900
67. C.H. Ng, S. Xu, and K.P. Lam Dok-3 plays a nonredundant role in negative regulation of B-cell activation Blood 110 2007 259 266 (Pubitemid 47026843)
68. M. Karin, and E. Gallagher From JNK to pay dirt: jun kinases, their biochemistry, physiology and clinical importance IUBMB Life 57 2005 283 295 (Pubitemid 40904256)
69. C. Edmunds, R.V. Parry, S.J. Burgess, B. Reaves, and S.G. Ward CD28 stimulates tyrosine phosphorylation, cellular redistribution and catalytic activity of the inositol lipid 5-phosphatase SHIP Eur J Immunol 29 1999 3507 3515 (Pubitemid 29527798)
70. R. Galandrini, I. Tassi, S. Morrone, L. Lanfrancone, P. Pelicci, and M. Piccoli The adaptor protein shc is involved in the negative regulation of NK cell-mediated cytotoxicity Eur J Immunol 31 2001 2016 2025 (Pubitemid 32640717)
71. R. Galandrini, I. Tassi, G. Mattia, L. Lenti, M. Piccoli, and L. Frati SH2-containing inositol phosphatase (SHIP-1) transiently translocates to raft domains and modulates CD16-mediated cytotoxicity in human NK cells Blood 100 2002 4581 4589 (Pubitemid 35429701)
72. R. Parihar, R. Trotta, J.M. Roda, A.K. Ferketich, S. Tridandapani, and M.A. Caligiuri Src homology 2-containing inositol 5′-phosphatase 1 negatively regulates IFN-gamma production by natural killer cells stimulated with antibody-coated tumor cells and interleukin-12 Cancer Res 65 2005 9099 9107 (Pubitemid 41377403)
73. V. Kumar, and A. Sharma Mast cells: emerging sentinel innate immune cells with diverse role in immunity Mol Immunol 48 2010 14 25
74. J. Kalesnikoff, V. Lam, and G. Krystal SHIP represses mast cell activation and reveals that IgE alone triggers signaling pathways which enhance normal mast cell survival Mol Immunol 38 2002 1201 1206 (Pubitemid 35253753)
75. J. Kalesnikoff, N. Baur, M. Leitges, M.R. Hughes, J.E. Damen, and M. Huber SHIP negatively regulates IgE + antigen-induced IL-6 production in mast cells by inhibiting NF-kappa B activity J Immunol 168 2002 4737 4746 (Pubitemid 34441382)
76. K. Gimborn, E. Lessmann, S. Kuppig, G. Krystal, and M. Huber SHIP down-regulates FcepsilonR1-induced degranulation at supraoptimal IgE or antigen levels J Immunol 174 2005 507 516 (Pubitemid 40007441)
77. K. Roget, M. Malissen, O. Malbec, B. Malissen, and M. Daeron Non-T cell activation linker promotes mast cell survival by dampening the recruitment of SHIP1 by linker for activation of T cells J Immunol 180 2008 3689 3698
78. C. Ulivieri, D. Fanigliulo, G. Masi, M.T. Savino, A. Gamberucci, and P.G. Pelicci p66Shc is a negative regulator of Fc{varepsilon}RI-dependent signaling in mast cells J Immunol 2011
79. V.L. Ott, I. Tamir, M. Niki, P.P. Pandolfi, and J.C. Cambier Downstream of kinase, p62(dok), is a mediator of Fc gamma IIB inhibition of Fc epsilon RI signaling J Immunol 168 2002 4430 4439 (Pubitemid 34441344)
80. A. Mantovani, A. Sica, and M. Locati Macrophage polarization comes of age Immunity 23 2005 344 346 (Pubitemid 41443435)
81. M.J. Rauh, V. Ho, C. Pereira, A. Sham, L.M. Sly, and V. Lam SHIP represses the generation of alternatively activated macrophages Immunity 23 2005 361 374 (Pubitemid 41443438)
82. E. Kuroda, V. Ho, J. Ruschmann, F. Antignano, M. Hamilton, and M.J. Rauh SHIP represses the generation of IL-3-induced M2 macrophages by inhibiting IL-4 production from basophils J Immunol 183 2009 3652 3660
83. S.B. Weisser, K.W. McLarren, N. Voglmaier, C.J. van Netten-Thomas, A. Antov, and R.A. Flavell Alternative activation of macrophages by IL-4 requires SHIP degradation Eur J Immunol 2011
84. S.K. Biswas, and E. Lopez-Collazo Endotoxin tolerance: new mechanisms, molecules and clinical significance Trends Immunol 30 2009 475 487
85. S. Akira, and K. Takeda Toll-like receptor signalling Nat Rev Immunol 4 2004 499 511 (Pubitemid 38931765)
86. L.M. Sly, M.J. Rauh, J. Kalesnikoff, C.H. Song, and G. Krystal LPS-induced upregulation of SHIP is essential for endotoxin tolerance Immunity 21 2004 227 239 (Pubitemid 39094052)
87. H. Pan, E. Ding, M. Hu, A.S. Lagoo, M.B. Datto, and S.A. Lagoo-Deenadayalan SMAD4 is required for development of maximal endotoxin tolerance J Immunol 184 2010 5502 5509
88. H. An, H. Xu, M. Zhang, J. Zhou, T. Feng, and C. Qian Src homology 2 domain-containing inositol-5-phosphatase 1 (SHIP1) negatively regulates TLR4-mediated LPS response primarily through a phosphatase activity- and PI-3K-independent mechanism Blood 105 2005 4685 4692 (Pubitemid 40807290)
89. L.M. Sly, M.J. Hamilton, E. Kuroda, V.W. Ho, F.L. Antignano, and S.L. Omeis SHIP prevents lipopolysaccharide from triggering an antiviral response in mice Blood 113 2009 2945 2954
90. J.N. Gabhann, R. Higgs, K. Brennan, W. Thomas, J.E. Damen, and N. Ben Larbi Absence of SHIP-1 results in constitutive phosphorylation of tank-binding kinase 1 and enhanced TLR3-dependent IFN-beta production J Immunol 184 2010 2314 2320
91. J.M. Luo, Z.L. Liu, H.L. Hao, F.X. Wang, Z.R. Dong, and R. Ohno Mutation analysis of SHIP gene in acute leukemia Zhongguo Shi Yan Xue Ye Xue Za Zhi 12 2004 420 426
92. T.C. Lo, L.M. Barnhill, Y. Kim, E.A. Nakae, A.L. Yu, and M.B. Diccianni Inactivation of SHIP1 in T-cell acute lymphoblastic leukemia due to mutation and extensive alternative splicing Leuk Res 33 2009 1562 1566
93. M. Sattler, S. Verma, C.H. Byrne, G. Shrikhande, T. Winkler, and P.A. Algate BCR/ABL directly inhibits expression of SHIP, an SH2-containing polyinositol-5-phosphatase involved in the regulation of hematopoiesis Mol Cell Biol 19 1999 7473 7480 (Pubitemid 29493410)
94. M. Sattler, R. Salgia, G. Shrikhande, S. Verma, J.L. Choi, and L.R. Rohrschneider The phosphatidylinositol polyphosphate 5-phosphatase SHIP and the protein tyrosine phosphatase SHP-2 form a complex in hematopoietic cells which can be regulated by BCR/ABL and growth factors Oncogene 15 1997 2379 2384 (Pubitemid 27496988)
95. R. Fukuda, A. Hayashi, A. Utsunomiya, Y. Nukada, R. Fukui, and K. Itoh Alteration of phosphatidylinositol 3-kinase cascade in the multilobulated nuclear formation of adult T cell leukemia/lymphoma (ATLL) Proc Natl Acad Sci USA 102 2005 15213 15218 (Pubitemid 41513361)
96. R.I. Fukuda, K. Tsuchiya, K. Suzuki, K. Itoh, J. Fujita, and A. Utsunomiya Human T-cell leukemia virus type I tax down-regulates the expression of phosphatidylinositol 3,4,5-trisphosphate inositol phosphatases via the NF-kappaB pathway J Biol Chem 284 2009 2680 2689
97. G.K. Lakhanpal, L.M. Vecchiarelli-Federico, Y.J. Li, J.W. Cui, M.L. Bailey, and D.E. Spaner The inositol phosphatase SHIP-1 is negatively regulated by Fli-1 and its loss accelerates leukemogenesis Blood 116 2010 428 436
98. M. Kennah, T.Y. Yau, M. Nodwell, G. Krystal, R.J. Andersen, and C.J. Ong Activation of SHIP via a small molecule agonist kills multiple myeloma cells Exp Hematol 37 2009 1274 1283
99. W.D. Shlomchik Graft-versus-host disease Nat Rev Immunol 7 2007 340 352 (Pubitemid 46674485)
100. T. Ghansah, K.H. Paraiso, S. Highfill, C. Desponts, S. May, and J.K. McIntosh Expansion of myeloid suppressor cells in SHIP-deficient mice represses allogeneic T cell responses J Immunol 173 2004 7324 7330 (Pubitemid 39628170)
101. K.H. Paraiso, T. Ghansah, A. Costello, R.W. Engelman, W.G. Kerr, and Induced SHIP deficiency expands myeloid regulatory cells and abrogates graft-versus-host disease J Immunol 178 2007 2893 2900 (Pubitemid 46333167)
102. R. Brooks, G.M. Fuhler, S. Iyer, M.J. Smith, M.Y. Park, and K.H. Paraiso SHIP1 inhibition increases immunoregulatory capacity and triggers apoptosis of hematopoietic cancer cells J Immunol 184 2010 3582 3589