메뉴 건너뛰기




Volumn 186, Issue 8, 2011, Pages 4936-4945

Evidence that the lipid phosphatase SHIP-1 regulates T lymphocyte morphology and motility

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINO 6 [2 [[4 (DIETHYLAMINO) 1 METHYLBUTYL]AMINO] 6 METHYL 4 PYRIMIDINYL] 2 METHYLQUINOLINE; CXCL11 CHEMOKINE; EZRIN; GLYCOGEN SYNTHASE KINASE 3BETA; LIPID PHOSPHATASE SHIP 1; MOESIN; PHOSPHATASE; PROTEIN KINASE B; RADIXIN; UNCLASSIFIED DRUG;

EID: 79955013111     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.1002350     Document Type: Article
Times cited : (21)

References (71)
  • 2
    • 33947239891 scopus 로고    scopus 로고
    • SHIP-deficient mice provide insights into the regulation of dendritic cell development and function
    • DOI 10.1016/j.exphem.2007.01.048, PII S0301472X07000604
    • Neill, L., A. H. Tien, J. Rey-Ladino, and C. D. Helgason. 2007. SHIP-deficient mice provide insights into the regulation of dendritic cell development and function. Exp. Hematol. 35:627-639. (Pubitemid 46427971)
    • (2007) Experimental Hematology , vol.35 , Issue.4 , pp. 627-639
    • Neill, L.1    Tien, A.H.2    Rey-Ladino, J.3    Helgason, C.D.4
  • 3
    • 0036838678 scopus 로고    scopus 로고
    • The Src homology 2 domain-containing inositol 5-phosphatase negatively regulates Fcγ receptor-mediated phagocytosis through immunoreceptor tyrosine-based activation motif-bearing phagocytic receptors
    • DOI 10.1182/blood-2002-03-0787
    • Nakamura, K., A. Malykhin, and K. M. Coggeshall. 2002. The Src homology 2 domain-containing inositol 5-phosphatase negatively regulates Fcgamma receptor-mediated phagocytosis through immunoreceptor tyrosine-based activation motif-bearing phagocytic receptors. Blood 100:3374-3382. (Pubitemid 35217090)
    • (2002) Blood , vol.100 , Issue.9 , pp. 3374-3382
    • Nakamura, K.1    Malykhin, A.2    Mark Coggeshall, K.3
  • 4
    • 40049084080 scopus 로고    scopus 로고
    • Inappropriate recruitment and activity by the Src homology region 2 domain-containing phosphatase 1 (SHP1) is responsible for receptor dominance in the SHIP-deficient NK cell
    • Wahle, J. A., K. H. T. Paraiso, R. D. Kendig, H. R. Lawrence, L. Chen, J. Wu, and W. G. Kerr. 2007. Inappropriate recruitment and activity by the Src homology region 2 domain-containing phosphatase 1 (SHP1) is responsible for receptor dominance in the SHIP-deficient NK cell. J. Immunol. 179:8009-8015.
    • (2007) J. Immunol. , vol.179 , pp. 8009-8015
    • Wahle, J.A.1    Paraiso, K.H.T.2    Kendig, R.D.3    Lawrence, H.R.4    Chen, L.5    Wu, J.6    Kerr, W.G.7
  • 6
    • 0037324144 scopus 로고    scopus 로고
    • FcγRIIB activation leads to inhibition of signalling by independently ligated receptors
    • Brauweiler, A. M., and J. C. Cambier. 2003. Fc gamma RIIB activation leads to inhibition of signalling by independently ligated receptors. Biochem. Soc. Trans. 31:281-285. (Pubitemid 36241445)
    • (2003) Biochemical Society Transactions , vol.31 , Issue.1 , pp. 281-285
    • Brauweiler, A.M.1    Cambier, J.C.2
  • 8
    • 77951931275 scopus 로고    scopus 로고
    • Absence of SHIP-1 results in constitutive phosphorylation of tank-binding kinase 1 and enhanced TLR3-dependent IFN-beta production
    • Gabhann, J. N., R. Higgs, K. Brennan, W. Thomas, J. E. Damen, N. Ben Larbi, G. Krystal, and C. A. Jefferies. 2010. Absence of SHIP-1 results in constitutive phosphorylation of tank-binding kinase 1 and enhanced TLR3-dependent IFN-beta production. J. Immunol. 184:2314-2320.
    • (2010) J. Immunol. , vol.184 , pp. 2314-2320
    • Gabhann, J.N.1    Higgs, R.2    Brennan, K.3    Thomas, W.4    Damen, J.E.5    Larbi, N.B.6    Krystal, G.7    Jefferies, C.A.8
  • 9
    • 4143102310 scopus 로고    scopus 로고
    • LPS-induced upregulation of SHIP is essential for endotoxin tolerance
    • DOI 10.1016/j.immuni.2004.07.010, PII S1074761304001931
    • Sly, L. M., M. J. Rauh, J. Kalesnikoff, C. H. Song, and G. Krystal. 2004. LPS-induced upregulation of SHIP is essential for endotoxin tolerance. Immunity 21:227-239. (Pubitemid 39094052)
    • (2004) Immunity , vol.21 , Issue.2 , pp. 227-239
    • Sly, L.M.1    Rauh, M.J.2    Kalesnikoff, J.3    Song, C.H.4    Krystal, G.5
  • 12
    • 70349331525 scopus 로고    scopus 로고
    • 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
    • Costinean, S., S. K. Sandhu, I. M. Pedersen, E. Tili, R. Trotta, D. Perrotti, D. Ciarlariello, P. Neviani, J. Harb, L. R. Kauffman, et al. 2009. 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 114:1374-1382.
    • (2009) Blood , vol.114 , pp. 1374-1382
    • Costinean, S.1    Sandhu, S.K.2    Pedersen, I.M.3    Tili, E.4    Trotta, R.5    Perrotti, D.6    Ciarlariello, D.7    Neviani, P.8    Harb, J.9    Kauffman, L.R.10
  • 14
    • 0032702790 scopus 로고    scopus 로고
    • CD28 stimulates tyrosine phosphorylation, cellular redistribution and catalytic activity of the inositol lipid 5-phosphatase SHIP
    • DOI 10.1002/(SICI)1521-4141(199911)29:11<3507::AID-IMMU3507>3.0. CO;2-9
    • Edmunds, C., R. V. Parry, S. J. Burgess, B. Reaves, and S. G. Ward. 1999. CD28 stimulates tyrosine phosphorylation, cellular redistribution and catalytic activity of the inositol lipid 5-phosphatase SHIP. Eur. J. Immunol. 29:3507-3515. (Pubitemid 29527798)
    • (1999) European Journal of Immunology , vol.29 , Issue.11 , pp. 3507-3515
    • Edmunds, C.1    Parry, R.V.2    Burgess, S.J.3    Reaves, B.4    Ward, S.G.5
  • 15
    • 0037111475 scopus 로고    scopus 로고
    • Evidence that SHIP-1 contributes to phosphatidylinositol 3,4,5-trisphosphate metabolism in T lymphocytes and can regulate novel phosphoinositide 3-kinase effectors
    • Freeburn, R. W., K. L. Wright, S. J. Burgess, E. Astoul, D. A. Cantrell, and S. G. Ward. 2002. Evidence that SHIP-1 contributes to phosphatidylinositol 3, 4, 5-trisphosphate metabolism in T lymphocytes and can regulate novel phosphoinositide 3-kinase effectors. J. Immunol. 169:5441-5450. (Pubitemid 35291641)
    • (2002) Journal of Immunology , vol.169 , Issue.10 , pp. 5441-5450
    • Freeburn, R.W.1    Wright, K.L.2    Burgess, S.J.3    Astoul, E.4    Cantrell, D.A.5    Ward, S.G.6
  • 16
    • 11244353237 scopus 로고    scopus 로고
    • SHIP family inositol phosphatases interact with and negatively regulate the Tec tyrosine kinase
    • DOI 10.1074/jbc.M408141200
    • Tomlinson, M. G., V. L. Heath, C. W. Turck, S. P. Watson, and A. Weiss. 2004. SHIP family inositol phosphatases interact with and negatively regulate the Tec tyrosine kinase. J. Biol. Chem. 279:55089-55096. (Pubitemid 40066501)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.53 , pp. 55089-55096
    • Tomlinson, M.G.1    Heath, V.L.2    Turck, C.W.3    Watson, S.P.4    Weiss, A.5
  • 17
    • 33750530393 scopus 로고    scopus 로고
    • 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
    • DOI 10.1084/jem.20060650
    • Dong, S., B. Corre, E. Foulon, E. Dufour, A. Veillette, O. Acuto, and F. Michel. 2006. 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. 203:2509-2518. (Pubitemid 44664620)
    • (2006) Journal of Experimental Medicine , vol.203 , Issue.11 , pp. 2509-2518
    • Dong, S.1    Corre, B.2    Foulon, E.3    Dufour, E.4    Veillette, A.5    Acuto, O.6    Michel, F.7
  • 18
    • 33748433789 scopus 로고    scopus 로고
    • Restoration of SHIP-1 activity in human leukemic cells modifies NF-κB activation pathway and cellular survival upon oxidative stress
    • DOI 10.1038/sj.onc.1209542, PII 1209542
    • Gloire, G., E. Charlier, S. Rahmouni, C. Volanti, A. Chariot, C. Erneux, and J. Piette. 2006. Restoration of SHIP-1 activity in human leukemic cells modifies NF-[kappa]B activation pathway and cellular survival upon oxidative stress. Oncogene 25:5485-5494. (Pubitemid 44344099)
    • (2006) Oncogene , vol.25 , Issue.40 , pp. 5485-5494
    • Gloire, G.1    Charlier, E.2    Rahmouni, S.3    Volanti, C.4    Chariot, A.5    Erneux, C.6    Piette, J.7
  • 19
    • 41149095078 scopus 로고    scopus 로고
    • Nonadherent cells switch to a Rac-mediated, SHIP regulated, Akt activation mode for survival
    • DOI 10.1038/sj.onc.1210830, PII 1210830
    • Chaigne-Delalande, B., G. Anies, I. Kramer, and E. Genot. 2008. Nonadherent cells switch to a Rac-mediated, SHIP regulated, Akt activation mode for survival. Oncogene 27:1876-1885. (Pubitemid 351430824)
    • (2008) Oncogene , vol.27 , Issue.13 , pp. 1876-1885
    • Chaigne-Delalande, B.1    Anies, G.2    Kramer, I.3    Genot, E.4
  • 24
    • 41449094548 scopus 로고    scopus 로고
    • Phosphoinositide lipid phosphatases: Natural regulators of phosphoinositide 3-kinase signaling in T lymphocytes
    • Harris, S. J., R. V. Parry, J. Westwick, and S. G. Ward. 2008. Phosphoinositide lipid phosphatases: natural regulators of phosphoinositide 3-kinase signaling in T lymphocytes. J. Biol. Chem. 283:2465-2469.
    • (2008) J. Biol. Chem. , vol.283 , pp. 2465-2469
    • Harris, S.J.1    Parry, R.V.2    Westwick, J.3    Ward, S.G.4
  • 25
    • 75349096225 scopus 로고    scopus 로고
    • Fine tuning T lymphocytes: A role for the lipid phosphatase SHIP-1
    • Parry, R. V., S. J. Harris, and S. G. Ward. 2010. Fine tuning T lymphocytes: a role for the lipid phosphatase SHIP-1. Biochim. Biophys. Acta 1804:592-597.
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 592-597
    • Parry, R.V.1    Harris, S.J.2    Ward, S.G.3
  • 26
    • 0036310982 scopus 로고    scopus 로고
    • The immunosuppressant rapamycin mimics a starvation-like signal distinct from amino acid and glucose deprivation
    • DOI 10.1128/MCB.22.15.5575-5584.2002
    • Peng, T., T. R. Golub, and D. M. Sabatini. 2002. The immunosuppressant rapamycin mimics a starvation-like signal distinct from amino acid and glucose deprivation. Mol. Cell. Biol. 22:5575-5584. (Pubitemid 34755766)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.15 , pp. 5575-5584
    • Peng, T.1    Golub, T.R.2    Sabatini, D.M.3
  • 27
    • 0842346270 scopus 로고    scopus 로고
    • Do phosphoinositide 3-kinases direct lymphocyte navigation?
    • DOI 10.1016/j.it.2003.12.003
    • Ward, S. G. 2004. Do phosphoinositide 3-kinases direct lymphocyte navigation? Trends Immunol. 25:67-74. (Pubitemid 38167487)
    • (2004) Trends in Immunology , vol.25 , Issue.2 , pp. 67-74
    • Ward, S.G.1
  • 28
    • 32344449778 scopus 로고    scopus 로고
    • T lymphocytes on the move: Chemokines, PI 3-kinase and beyond
    • DOI 10.1016/j.it.2005.12.004, PII S1471490605002954
    • Ward, S. G. 2006. T lymphocytes on the move: chemokines, PI 3-kinase and beyond. Trends Immunol. 27:80-87. (Pubitemid 43221974)
    • (2006) Trends in Immunology , vol.27 , Issue.2 , pp. 80-87
    • Ward, S.G.1
  • 29
    • 59849114020 scopus 로고    scopus 로고
    • Mechanisms of chemokine and antigen-dependent T-lymphocyte navigation
    • Ward, S. G., and F. M. Marelli-Berg. 2009. Mechanisms of chemokine and antigen-dependent T-lymphocyte navigation. Biochem. J. 418:13-27.
    • (2009) Biochem. J. , vol.418 , pp. 13-27
    • Ward, S.G.1    Marelli-Berg, F.M.2
  • 31
    • 22144497435 scopus 로고    scopus 로고
    • Heterologous regulation of chemokine receptor signaling by the lipid phosphatase SHIP in lymphocytes
    • DOI 10.1016/j.cellsig.2004.12.009, PII S0898656804002943
    • Wain, C. M., J. Westwick, and S. G. Ward. 2005. Heterologous regulation of chemokine receptor signaling by the lipid phosphatase SHIP in lymphocytes. Cell. Signal. 17:1194-1202. (Pubitemid 40982610)
    • (2005) Cellular Signalling , vol.17 , Issue.10 , pp. 1194-1202
    • Wain, C.M.1    Westwick, J.2    Ward, S.G.3
  • 33
    • 0038545370 scopus 로고    scopus 로고
    • L, and IL-2 expression in primary human CD4 T lymphocytes
    • Parry, R. V., C. A. Rumbley, L. H. Vandenberghe, C. H. June, and J. L. Riley. 2003. CD28 and inducible costimulatory protein Src homology 2 binding domains show distinct regulation of phosphatidylinositol 3-kinase, Bcl-xL, and IL-2 expression in primary human CD4 T lymphocytes. J. Immunol. 171:166-174. (Pubitemid 36745285)
    • (2003) Journal of Immunology , vol.171 , Issue.1 , pp. 166-174
    • Parry, R.V.1    Rumbley, C.A.2    Vandenberghe, L.H.3    June, C.H.4    Riley, J.L.5
  • 34
    • 35148819807 scopus 로고    scopus 로고
    • PI3Kγ is the dominant isoform involved in migratory responses of human T lymphocytes: Effects of ex vivo maintenance and limitations of non-viral delivery of siRNA
    • DOI 10.1016/j.cellsig.2007.08.006, PII S0898656807002537
    • Smith, L. D., E. S. Hickman, R. V. Parry, J. Westwick, and S. G. Ward. 2007. PI3Kgamma is the dominant isoform involved in migratory responses of human T lymphocytes: effects of ex vivo maintenance and limitations of non-viral delivery of siRNA. Cell. Signal. 19:2528-2539. (Pubitemid 47542298)
    • (2007) Cellular Signalling , vol.19 , Issue.12 , pp. 2528-2539
    • Smith, L.D.1    Hickman, E.S.2    Parry, R.V.3    Westwick, J.4    Ward, S.G.5
  • 37
    • 0035367805 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinases in T lymphocyte activation
    • DOI 10.1016/S0952-7915(00)00223-5
    • Ward, S. G., and D. A. Cantrell. 2001. Phosphoinositide 3-kinases in T lymphocyte activation. Curr. Opin. Immunol. 13:332-338. (Pubitemid 32537705)
    • (2001) Current Opinion in Immunology , vol.13 , Issue.3 , pp. 332-338
    • Ward, S.G.1    Cantrell, D.A.2
  • 39
    • 0344826472 scopus 로고    scopus 로고
    • Chemokine stimulation of human peripheral blood T lymphocytes induces rapid dephosphorylation of ERM proteins, which facilitates loss of microvilli and polarization
    • DOI 10.1182/blood-2002-12-3807
    • Brown, M. J., R. Nijhara, J. A. Hallam, M. Gignac, K. M. Yamada, S. L. Erlandsen, J. Delon, M. Kruhlak, and S. Shaw. 2003. Chemokine stimulation of human peripheral blood T lymphocytes induces rapid dephosphorylation of ERM proteins, which facilitates loss of microvilli and polarization. Blood 102:3890-3899. (Pubitemid 37486967)
    • (2003) Blood , vol.102 , Issue.12 , pp. 3890-3899
    • Brown, M.J.1    Nijhara, R.2    Hallam, J.A.3    Gignac, M.4    Yamada, K.M.5    Erlandsen, S.L.6    Delon, J.7    Kruhlak, M.8    Shaw, S.9
  • 40
    • 33846781779 scopus 로고    scopus 로고
    • Regulation of ezrin localization by Rac1 and PIPK in human epithelial cells
    • DOI 10.1016/j.yexcr.2006.12.002, PII S0014482706005003
    • Auvinen, E., N. Kivi, and A. Vaheri. 2007. Regulation of ezrin localization by Rac1 and PIPK in human epithelial cells. Exp. Cell Res. 313:824-833. (Pubitemid 46206076)
    • (2007) Experimental Cell Research , vol.313 , Issue.4 , pp. 824-833
    • Auvinen, E.1    Kivi, N.2    Vaheri, A.3
  • 42
  • 43
    • 79954988668 scopus 로고    scopus 로고
    • Inhibition of the Rho GTPase, Rac, differentially inhibits proliferation of AML cell lines and may serve as a novel molecular target
    • Schore, R. J., Y. Zheng, D. A. Williams, and Y. Gu. 2005. Inhibition of the Rho GTPase, Rac, differentially inhibits proliferation of AML cell lines and may serve as a novel molecular target. Blood (ASH Annual Meeting Abstracts) 106:1205.
    • (2005) Blood (ASH Annual Meeting Abstracts) , vol.106 , pp. 1205
    • Schore, R.J.1    Zheng, Y.2    Williams, D.A.3    Gu, Y.4
  • 46
    • 0030728077 scopus 로고    scopus 로고
    • Presentation of integrins on leukocyte microvilli: A role for the extracellular domain in determining membrane localization
    • DOI 10.1083/jcb.139.2.563
    • Abitorabi, M. A., R. K. Pachynski, R. E. Ferrando, M. Tidswell, and D. J. Erle. 1997. Presentation of integrins on leukocyte microvilli: a role for the extracellular domain in determining membrane localization. J. Cell Biol. 139:563-571. (Pubitemid 27459326)
    • (1997) Journal of Cell Biology , vol.139 , Issue.2 , pp. 563-571
    • Abitorabi, M.A.1    Pachynski, R.K.2    Ferrando, R.E.3    Tidswell, M.4    Erle, D.J.5
  • 48
    • 0038549067 scopus 로고    scopus 로고
    • PI3K in lymphocyte development, differentiation and activation
    • Okkenhaug, K., and B. Vanhaesebroeck. 2003. PI3K in lymphocyte development, differentiation and activation. Nat. Rev. Immunol. 3:317-330. (Pubitemid 37328684)
    • (2003) Nature Reviews Immunology , vol.3 , Issue.4 , pp. 317-330
    • Okkenhaug, K.1    Vanhaesebroeck, B.2
  • 49
    • 33644513730 scopus 로고    scopus 로고
    • Beyond PTEN mutations: The PI3K pathway as an integrator of multiple inputs during tumorigenesis
    • DOI 10.1038/nrc1819, PII N1819
    • Cully, M., H. You, A. J. Levine, and T. W. Mak. 2006. Beyond PTEN mutations: the PI3K pathway as an integrator of multiple inputs during tumorigenesis. Nat. Rev. Cancer 6:184-192. (Pubitemid 43292562)
    • (2006) Nature Reviews Cancer , vol.6 , Issue.3 , pp. 184-192
    • Cully, M.1    You, H.2    Levine, A.J.3    Mak, T.W.4
  • 51
    • 0030663034 scopus 로고    scopus 로고
    • 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
    • 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 SHP-2 form a complex in hematopoietic cells which can be regulated by BCR/ABL and growth factors. Oncogene 15:2379-2384. (Pubitemid 27496988)
    • (1997) Oncogene , vol.15 , Issue.19 , pp. 2379-2384
    • Sattler, M.1    Salgia, R.2    Shrikhande, G.3    Verma, S.4    Choi, J.-L.5    Rohrschneider, L.R.6    Griffin, J.D.7
  • 52
    • 8844258034 scopus 로고    scopus 로고
    • Restoration of SHIP activity in a human leukemia cell line downregulates constitutively activated phosphatidylinositol 3-kinase/Akt/GSK-3β signaling and leads to an increased transit time through the G1 phase of the cell cycle
    • DOI 10.1038/sj.leu.2403529
    • Horn, S., E. Endl, B. Fehse, M. M. Weck, G. W. Mayr, and M. Jücker. 2004. Restoration of SHIP activity in a human leukemia cell line downregulates constitutively activated phosphatidylinositol 3-kinase/Akt/GSK-3beta signaling and leads to an increased transit time through the G1 phase of the cell cycle. Leukemia 18:1839-1849. (Pubitemid 39530015)
    • (2004) Leukemia , vol.18 , Issue.11 , pp. 1839-1849
    • Horn, S.1    Endl, E.2    Fehse, B.3    Weck, M.M.4    Mayr, G.W.5    Jucker, M.6
  • 55
    • 77951624382 scopus 로고    scopus 로고
    • SHIP1 inhibition increases immunoregulatory capacity and triggers apoptosis of hematopoietic cancer cells
    • Brooks, R., G. M. Fuhler, S. Iyer, M. J. Smith, M. Y. Park, K. H. Paraiso, R. W. Engelman, and W. G. Kerr. 2010. SHIP1 inhibition increases immunoregulatory capacity and triggers apoptosis of hematopoietic cancer cells. J. Immunol. 184:3582-3589.
    • (2010) J. Immunol. , vol.184 , pp. 3582-3589
    • Brooks, R.1    Fuhler, G.M.2    Iyer, S.3    Smith, M.J.4    Park, M.Y.5    Paraiso, K.H.6    Engelman, R.W.7    Kerr, W.G.8
  • 56
    • 34250788809 scopus 로고    scopus 로고
    • AKT/PKB Signaling: Navigating Downstream
    • DOI 10.1016/j.cell.2007.06.009, PII S0092867407007751
    • Manning, B. D., and L. C. Cantley. 2007. AKT/PKB signaling: navigating downstream. Cell 129:1261-1274. (Pubitemid 46962095)
    • (2007) Cell , vol.129 , Issue.7 , pp. 1261-1274
    • Manning, B.D.1    Cantley, L.C.2
  • 59
    • 77950937721 scopus 로고    scopus 로고
    • 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
    • Charlier, E., C. Condé, J. Zhang, L. Deneubourg, E. Di Valentin, S. Rahmouni, A. Chariot, P. Agostinis, P. C. Pang, S. M. Haslam, et al. 2010. 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 24:821-832.
    • (2010) Leukemia , vol.24 , pp. 821-832
    • Charlier, E.1    Condé, C.2    Zhang, J.3    Deneubourg, L.4    Di Valentin, E.5    Rahmouni, S.6    Chariot, A.7    Agostinis, P.8    Pang, P.C.9    Haslam, S.M.10
  • 60
    • 11144234519 scopus 로고    scopus 로고
    • The phosphoinositol 3,4-bisphosphate-binding protein TAPP1 interacts with syntrophins and regulates actin cytoskeletal organization
    • DOI 10.1074/jbc.M410654200
    • Hogan, A., Y. Yakubchyk, J. Chabot, C. Obagi, E. Daher, K. Maekawa, and S. H. Gee. 2004. The phosphoinositol 3, 4-bisphosphate-binding protein TAPP1 interacts with syntrophins and regulates actin cytoskeletal organization. J. Biol. Chem. 279:53717-53724. (Pubitemid 40051880)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.51 , pp. 53717-53724
    • Hogan, A.1    Yakubchyk, Y.2    Chabot, J.3    Obagi, C.4    Daher, E.5    Maekawa, K.6    Gee, S.H.7
  • 61
    • 73949099919 scopus 로고    scopus 로고
    • TAPP2 links phosphoinositide 3-kinase signaling to B-cell adhesion through interaction with the cytoskeletal protein utrophin: Expression of a novel cell adhesion-promoting complex in B-cell leukemia
    • Costantini, J. L., S. M. Cheung, S. Hou, H. Li, S. K. Kung, J. B. Johnston, J. A. Wilkins, S. B. Gibson, and A. J. Marshall. 2009. TAPP2 links phosphoinositide 3-kinase signaling to B-cell adhesion through interaction with the cytoskeletal protein utrophin: expression of a novel cell adhesion-promoting complex in B-cell leukemia. Blood 114:4703-4712.
    • (2009) Blood , vol.114 , pp. 4703-4712
    • Costantini, J.L.1    Cheung, S.M.2    Hou, S.3    Li, H.4    Kung, S.K.5    Johnston, J.B.6    Wilkins, J.A.7    Gibson, S.B.8    Marshall, A.J.9
  • 62
    • 0031841211 scopus 로고    scopus 로고
    • Involvement of phosphoinositide 3-kinase and Rac in membrane ruffling induced by IL-2 in T cells
    • DOI 10.1002/(SICI)1521-4141(199806)28:06<1877::AID-IMMU1877>3.0. CO;2-I
    • Arrieumerlou, C., E. Donnadieu, P. Brennan, G. Keryer, G. Bismuth, D. Cantrell, and A. Trautmann. 1998. Involvement of phosphoinositide 3-kinase and Rac in membrane ruffling induced by IL-2 in T cells. Eur. J. Immunol. 28:1877-1885. (Pubitemid 28271704)
    • (1998) European Journal of Immunology , vol.28 , Issue.6 , pp. 1877-1885
    • Arrieumerlou, C.1    Donnadieu, E.2    Brennan, P.3    Keryer, G.4    Bismuth, G.5    Cantrell, D.6    Trautmann, A.7
  • 63
    • 0034306279 scopus 로고    scopus 로고
    • Regulation of the Rac1-specific exchange factor Tiam1 involves both phosphoinositide 3-kinase-dependent and-independent components
    • Fleming, I. N., A. Gray, and C. P. Downes. 2000. Regulation of the Rac1-specific exchange factor Tiam1 involves both phosphoinositide 3-kinase-dependent and-independent components. Biochem. J. 351:173-182.
    • (2000) Biochem. J. , vol.351 , pp. 173-182
    • Fleming, I.N.1    Gray, A.2    Downes, C.P.3
  • 64
    • 33745967013 scopus 로고    scopus 로고
    • FcγR-induced production of superoxide and inflammatory cytokines is differentially regulated by SHIP through its influence on PI3K and/or Ras/Erk pathways
    • DOI 10.1182/blood-2005-09-3889
    • Ganesan, L. P., T. Joshi, H. Fang, V. K. Kutala, J. Roda, R. Trotta, A. Lehman, P. Kuppusamy, J. C. Byrd, W. E. Carson, et al. 2006. FcgammaR-induced production of superoxide and inflammatory cytokines is differentially regulated by SHIP through its influence on PI3K and/or Ras/Erk pathways. Blood 108:718-725. (Pubitemid 44061375)
    • (2006) Blood , vol.108 , Issue.2 , pp. 718-725
    • Ganesan, L.P.1    Joshi, T.2    Fang, H.3    Kutala, V.K.4    Roda, J.5    Trotta, R.6    Lehman, A.7    Kuppusamy, P.8    Byrd, J.C.9    Carson, W.E.10    Caligiuri, M.A.11    Tridandapani, S.12
  • 65
    • 0031065146 scopus 로고    scopus 로고
    • Negative Signaling in B Cells Causes Reduced Ras Activity by Reducing Shc-Grb2 Interactions
    • Tridandapani, S., G. W. Chacko, J. R. Van Brocklyn, and K. M. Coggeshall. 1997. Negative signaling in B cells causes reduced Ras activity by reducing Shc-Grb2 interactions. J. Immunol. 158:1125-1132. (Pubitemid 127469933)
    • (1997) Journal of Immunology , vol.158 , Issue.3 , pp. 1125-1132
    • Tridandapani, S.1    Chacko, G.W.2    Van Brooklyn, J.R.3    Coggeshall, K.M.4
  • 66
    • 0033710778 scopus 로고    scopus 로고
    • The RasGAP-binding protein p62dok is a mediator of inhibitory FcgammaRIIB signals in B cells
    • Tamir, I., J. C. Stolpa, C. D. Helgason, K. Nakamura, P. Bruhns, M. Daeron, and J. C. Cambier. 2000. The RasGAP-binding protein p62dok is a mediator of inhibitory FcgammaRIIB signals in B cells. Immunity 12:347-358.
    • (2000) Immunity , vol.12 , pp. 347-358
    • Tamir, I.1    Stolpa, J.C.2    Helgason, C.D.3    Nakamura, K.4    Bruhns, P.5    Daeron, M.6    Cambier, J.C.7
  • 69
    • 34247361650 scopus 로고    scopus 로고
    • Chemotaxis in the Absence of PIP3 Gradients
    • DOI 10.1016/j.cub.2007.04.004, PII S0960982207012109
    • Hoeller, O., and R. R. Kay. 2007. Chemotaxis in the absence of PIP3 gradients. Curr. Biol. 17:813-817. (Pubitemid 46635122)
    • (2007) Current Biology , vol.17 , Issue.9 , pp. 813-817
    • Hoeller, O.1    Kay, R.R.2
  • 70
    • 70449368599 scopus 로고    scopus 로고
    • PI3K isoforms as drug targets in inflammatory diseases: Lessons from pharmacological and genetic strategies
    • Harris, S. J., J. G. Foster, and S. G. Ward. 2009. PI3K isoforms as drug targets in inflammatory diseases: lessons from pharmacological and genetic strategies. Curr. Opin. Investig. Drugs 10:1151-1162.
    • (2009) Curr. Opin. Investig. Drugs , vol.10 , pp. 1151-1162
    • Harris, S.J.1    Foster, J.G.2    Ward, S.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.