Regulation of the immune response by SHIP

Seminars in Immunology

Volumn 14, Issue 1, 2002, Pages 37-47

  March, Michael E ^a   Ravichandran, Kodi ^a  

^a UNIVERSITY OF VIRGINIA   (United States)

Author keywords

Fc ; Inhibitory signaling; Inositol phosphatase; PIP3; RIIB1; SHIP

Indexed keywords

FC RECEPTOR; PROTEIN; PROTEIN SHIP1; UNCLASSIFIED DRUG;

CELL DIFFERENTIATION; CELL LINEAGE; CELL PROLIFERATION; CELL SURVIVAL; HEMATOPOIETIC CELL; HUMAN; IMMUNE RESPONSE; IMMUNE SYSTEM; IMMUNOREGULATION; NONHUMAN; PROTEIN ANALYSIS; PROTEIN FAMILY; PROTEIN STRUCTURE; REVIEW;

EID: 0036196812     PISSN: 10445323     EISSN: None     Source Type: Journal    
DOI: 10.1006/smim.2001.0340     Document Type: Article

References (78)

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2. Negative signaling in B lymphocytes induces tyrosine phosphorylation of the 145-kDa inositol polyphosphate 5-phosphatase, SHIP
3. The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5- triphosphate 5-phosphatase
4. Multiple forms of an inositol polyphosphate 5-phosphatase form signaling complexes with Shc and Grb2
5. p150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity
6. SHC and SHIP phosphorylation and interaction in response to activation of the FLT3 receptor
7. The inositol 5′-phosphatase SHIP binds to immunoreceptor signaling motifs and responds to high affinity IgE receptor aggregation
8. Cloning and characterization of human SHIP, the 145-kD inositol 5-phosphatase that associates with SHC after cytokine stimulation
9. The Lowe's oculocerebrorenal syndrome gene encodes a protein highly homologous to inositol polyphosphate-5-phosphatase
10. Cloning and expression of hurnan brain type I inositol 1,4,5-trisphosphate 5-phosphatase. High levels of mRNA in cerebellar Purkinje cells
11. Cloning and characterization of a human cDNA (INPPL1) sharing homology with inositol polyphosphate phosphatases
12. Characterization of a cDNA encoding the 43-kDa membrane-associated inositol-polyphosphate 5-phosphatase
13. Cloning and expression of human 75-kDa inositol polyphosphate-5- phosphatase
14. Mutation of the conserved domains of two inositol polyphosphate 5-phosphatases
15. Properties of type II inositol polypbosphate 5-phosphatase
16. Cloning and expression of a human placenta inositol 1,3,4,5-tetrakisphosphate and phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase
17. Signaling inositol polyphosphate-5-phosphatase. Characterization of activity and effect of GRB2 association
18. An essential role for the C-terminal non-catalytic region of SHIP in FcgRIIB 1-mediated inhibitory signaling
19. The human SHIP gene is differentially expressed in cell lineages of the bone marrow and blood
20. A novel spliced form of SH2-containing inositol phosphatase is expressed during myeloid development
21. Cloning of the genomic locus of mouse SH2 containing inositol 5-phosphatase (SHIP) and a novel 110-kDa splice isoform, SHIPdelta
22. p135 src homology 2 domain-containing inositol 5′-phosphatase (SHIPbeta) isoform can substitute for p145 SHIP in fcgamma RIIB1-mediated inhibitory signaling in B cells
23. Identification of a second SH2-domain-containing protein closely related to tine phosphatidylinositol polyphosphate 5-phosphatase SHIP
24. 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
25. The two SH2-domain-containing inositol 5-phosphatases SHIP1 and SHIP2 are coexpressed in human T lymphocytes
26. Partially distinct molecular mechanisms mediate inhibitory FcgammaRIIB signaling in resting and activated B cells
27. The SH2 domain containing inositol 5-phosphatase SHIP2 displays phosphatidylinositol 3,4,5-trisphosphate and inositol 1,3,4,5-tetrakisphosphate 5-phosphatase activity
28. Role of the inositol phosphatase SHIP in negative regulation of the immune system by tine receptor Fcγ RIIB
29. The SHIP phosphatase becomes associated with Fc gammaRIIB1 and is tyrosine phosphorylated during 'negative' signaling
30. Selective in vivo recruitment of the phosphatidylinositol phosphatase SHIP by phosphorylated Fc gammaRIIB during negative regulation of IgE-dependent mouse mast cell activation
31. Association of tyrosine phosphatases SHP-1 and SHP-2, inositol 5-phosphatase SHIP with gp49B1, and chromosomal assignment of the gene
32. Negative signaling pathways of the killer cell inhibitory receptor and Fc gamma RIIb1 require distinct phosphatases
33. Deletion of SHIP or SHP-1 reveals two distinct pathways for inhibitory signaling
34. Src homology, 2-containing inositol 5-phosphatase 1 binds to the multifunctional docking site of c-Met and potentiates hepatocyte growth factor-induced branching tubulogenesis
35. CDw150 associates with src-homology 2-containing inositol phosphatase and modulates CD95-mediated apoptosis
36. The SH2 inositol 5-phosphatase Ship1 is recruited in an SH2-dependent manner to the erythropoietin receptor
37. The role of erythropoietin receptor tyrosine phosphorylation in erythropoietin-induced proliferation
38. 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
39. 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
40. Activation-induced bidentate interaction of SHIP and Shc in B lymphocytes
41. 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
42. The RasGAP-binding protein p62dok is a mediator of inhibitory FcgammaRIIB signals in B cells
43. Bilevel control of B cell activation by the inositol 5-phosphatase SHIP
44. Dok-3, a novel adapter molecule involved in the negative regulation of immunoreceptor signaling
45. The disabled 1 phosphotyrosine-binding domain binds to the internalization signals of transmembrane glycoproteins and to phospholipids
46. p85 subunit of PI3 kinase does not bind to human Flt3 receptor, but associates with SHP2, SHIP, and a tyrosine-phosphorylated 100-kDa protein in Flt3 ligand-stimulated hematopoietic cells
47. The SH2 domain-containing inositol 5′-phosphatase (SHIP) recruits the p85 subunit of phosphoinositide 3-kinase during FcgammaRIIb1-mediated inhibition of B cell receptor signaling
48. The src homology domain 2-containing inositol phosphatase SHIP forms a ternary complex with Shc and Grb2 in antigen receptor-stimulated B lymphocytes
49. 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
50. SH2-containing inositol 5′-phosphatase SHIPS associates with the p130 (Cas) adapter protein and regulates cellular adhesion and spreading
51. Targeted disruption of SHIP leads to hemopoietic perturbations, lung pathology, and a shortened life span
52. The inositol polyphosphate 5-phosphatase ship is a crucial negative regulator of B cell antigen receptor signaling
53. SHIP is a negative regulator of growth factor receptor-mediated PKB/Akt activation and myeloid cell survival
54. The inositol phosphatase SHIP inhibits Akt/PKB activation in B cells
55. Deletion of fcgamma receptor IIB renders H-2(b) mice susceptible to collagen-induced arthritis
56. Spontaneous autoimmune disease in Fc(gamma)RIIB-deficient mice results from strain-specific epistasis
57. 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
58. The src homology 2-containing inositol phosphatase (SHIP) is the gatekeeper of mast cell degranulation
59. Targeted disruption of SHIP leads to Steel factor-induced degranulation of mast cells
60. A regulatory role for Src homology 2 domain-containing inositol 5′-phosphatase (SHIP) in phagocytosis mediated by Fc gamma receptors and complement receptor 3 (alpha(M)beta(2); CD11b/CD18)
61. Altered responsiveness to chemokines due to targeted disruption of SHIP
62. Positive regulation of interleukin-4-mediated proliferation by the SH2- containing inositol-5′-phosphatase
63. SHIP modulates immune receptor responses by regulating membrane association of Btk
64. Phosphatidylinositol-3,4,5-trisphosphate (PtdIns-3,4,5-P3)/Tec kinase-dependent calcium signaling pathway: A target tor SHIP-mediated inhibitory signals
65. The dynamics of protein kinase B regulation during B cell antigen receptor engagement
66. Phosphatidylinositol 3-kinase links the interleukin-2 receptor to protein kinase B and p70 S6 kinase
67. Dual role of phosphatidylinositol-3,4,5-trisphosphate in the activation of protein kinase B
68. Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate
69. Protein kinase B kinases that mediate phosphatidylinositol 3,4,5- trisphosphate-dependent activation of protein kinase B
70. SHIP inhibits Akt activation in B cells through regulation of Akt membrane localization
71. Involvement of guanosine triphosphatases and phospholipase C-gamma2 in extracellular signal-regulated kinase, c-Jun NH2-terminal kinase, and p38mitogen-activated protein kinase activation by the B cell antigen receptor
72. Negative signaling in B cells: SHIP Grbs Shc
73. SHIP recruitment attenuates Fc gamma RIIB-induced B cell apoptosis
74. SHIP's C-terminus is essential for its hydrolysis of PIP3 and inhibition of mast cell degranulation
75. Mutational analysis reveals multiple distinct sites within Fc gamma receptor IIB that function in inhibitory signaling
76. Transient translocation of the B cell receptor and Src homology, 2 domain-containing inositol phosphatase to lipid rafts: Evidence toward a role in calcium regulation
77. Gene expression physiology and pathophysiology of the immune system
78. Specificity determinants in phosphoinositide dephosphorylation: Crystal structure of an archetypal inositol polyphosphate 5-phosphatase