메뉴 건너뛰기




Volumn 48, Issue 1, 2008, Pages 240-252

Different roles of SHIP1 according to the cell context: The example of blood platelets

Author keywords

[No Author keywords available]

Indexed keywords

INOSITOL 1,4,5 TRISPHOSPHATE 5 PHOSPHATASE; INOSITOL-1,4,5-TRISPHOSPHATE 5-PHOSPHATASE; ISOENZYME; PHOSPHATASE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3,4 BISPHOSPHATE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE; PHOSPHATIDYLINOSITOL 3,4,5-TRIPHOSPHATE; PHOSPHATIDYLINOSITOL 3,4-DIPHOSPHATE; POLYPHOSPHOINOSITIDE;

EID: 51549083000     PISSN: 00652571     EISSN: None     Source Type: Book Series    
DOI: 10.1016/j.advenzreg.2007.11.004     Document Type: Article
Times cited : (15)

References (85)
  • 1
    • 11144274446 scopus 로고    scopus 로고
    • Role of the adaptor proteins Bam32, TAPP1 and TAPP2 in lymphocyte activation
    • Allam A., and Marshall A.J. Role of the adaptor proteins Bam32, TAPP1 and TAPP2 in lymphocyte activation. Immunol Lett 97 (2005) 7-17
    • (2005) Immunol Lett , vol.97 , pp. 7-17
    • Allam, A.1    Marshall, A.J.2
  • 2
    • 0032545343 scopus 로고    scopus 로고
    • The inositol phosphatase SHIP inhibits Akt/PKB activation in B cells
    • Aman M.J., Lamkin T.D., Okada H., Kurosaki T., and Ravichandran K.S. The inositol phosphatase SHIP inhibits Akt/PKB activation in B cells. J Biol Chem 273 (1998) 33922-33928
    • (1998) J Biol Chem , vol.273 , pp. 33922-33928
    • Aman, M.J.1    Lamkin, T.D.2    Okada, H.3    Kurosaki, T.4    Ravichandran, K.S.5
  • 3
    • 34547114477 scopus 로고    scopus 로고
    • The inositol polyphosphate 5-phosphatases: traffic controllers, waistline watchers and tumour suppressors?
    • Astle M.V., Horan K.A., Ooms L.M., and Mitchell C.A. The inositol polyphosphate 5-phosphatases: traffic controllers, waistline watchers and tumour suppressors?. Biochem Soc Symp 74 (2007) 161-181
    • (2007) Biochem Soc Symp , vol.74 , pp. 161-181
    • Astle, M.V.1    Horan, K.A.2    Ooms, L.M.3    Mitchell, C.A.4
  • 4
    • 33747592164 scopus 로고    scopus 로고
    • Regulation of phosphoinositide signaling by the inositol polyphosphate 5-phosphatases
    • Astle M.V., Seaton G., Davies E.M., Fedele C.G., Rahman P., Arsala L., et al. Regulation of phosphoinositide signaling by the inositol polyphosphate 5-phosphatases. IUBMB Life 58 (2006) 451-456
    • (2006) IUBMB Life , vol.58 , pp. 451-456
    • Astle, M.V.1    Seaton, G.2    Davies, E.M.3    Fedele, C.G.4    Rahman, P.5    Arsala, L.6
  • 5
    • 0037702455 scopus 로고    scopus 로고
    • The termination of PI3K signaling by SHIP1 and SHIP2 inositol 5-phosphatases
    • Backers K., Blero D., Paternotte N., Zhang J., and Erneux C. The termination of PI3K signaling by SHIP1 and SHIP2 inositol 5-phosphatases. Adv Enzyme Regul 43 (2003) 15-28
    • (2003) Adv Enzyme Regul , vol.43 , pp. 15-28
    • Backers, K.1    Blero, D.2    Paternotte, N.3    Zhang, J.4    Erneux, C.5
  • 6
    • 0032495874 scopus 로고    scopus 로고
    • Biphasic activation of PKBalpha/Akt in platelets. Evidence for stimulation both by phosphatidylinositol 3,4-bisphosphate, produced via a novel pathway, and by phosphatidylinositol 3,4,5-trisphosphate
    • Banfic H., Downes C.P., and Rittenhouse S.E. Biphasic activation of PKBalpha/Akt in platelets. Evidence for stimulation both by phosphatidylinositol 3,4-bisphosphate, produced via a novel pathway, and by phosphatidylinositol 3,4,5-trisphosphate. J Biol Chem 273 (1998) 11630-11637
    • (1998) J Biol Chem , vol.273 , pp. 11630-11637
    • Banfic, H.1    Downes, C.P.2    Rittenhouse, S.E.3
  • 7
    • 35048897386 scopus 로고    scopus 로고
    • The control of phosphatidylinositol 3,4-bisphosphate concentrations by activation of the Src homology 2 domain containing inositol polyphosphate 5-phosphatase 2, SHIP2
    • Batty I.H., Van der Kaay J., Gray A., Telfer J.F., Dixon M.J., and Downes C.P. The control of phosphatidylinositol 3,4-bisphosphate concentrations by activation of the Src homology 2 domain containing inositol polyphosphate 5-phosphatase 2, SHIP2. Biochem J 407 (2007) 255-266
    • (2007) Biochem J , vol.407 , pp. 255-266
    • Batty, I.H.1    Van der Kaay, J.2    Gray, A.3    Telfer, J.F.4    Dixon, M.J.5    Downes, C.P.6
  • 8
    • 34548643512 scopus 로고    scopus 로고
    • Phosphoinositide phosphatases in a network of signaling reactions
    • Blero D., Payrastre B., Schurmans S., and Erneux C. Phosphoinositide phosphatases in a network of signaling reactions. Pflugers Arch 455 (2007) 31-44
    • (2007) Pflugers Arch , vol.455 , pp. 31-44
    • Blero, D.1    Payrastre, B.2    Schurmans, S.3    Erneux, C.4
  • 9
    • 31044453282 scopus 로고    scopus 로고
    • Minding the gaps to promote thrombus growth and stability
    • Brass L.F., Zhu L., and Stalker T.J. Minding the gaps to promote thrombus growth and stability. J Clin Invest 115 (2005) 3385-3392
    • (2005) J Clin Invest , vol.115 , pp. 3385-3392
    • Brass, L.F.1    Zhu, L.2    Stalker, T.J.3
  • 10
    • 0037323803 scopus 로고    scopus 로고
    • A critical role of lipid rafts in the organization of a key FcgammaRIIa-mediated signaling pathway in human platelets
    • Bodin S., Viala C., Ragab A., and Payrastre B. A critical role of lipid rafts in the organization of a key FcgammaRIIa-mediated signaling pathway in human platelets. Thromb Haemost 89 (2003) 318-330
    • (2003) Thromb Haemost , vol.89 , pp. 318-330
    • Bodin, S.1    Viala, C.2    Ragab, A.3    Payrastre, B.4
  • 11
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • Cantley L.C. The phosphoinositide 3-kinase pathway. Science 296 (2002) 1655-1657
    • (2002) Science , vol.296 , pp. 1655-1657
    • Cantley, L.C.1
  • 12
    • 0034663163 scopus 로고    scopus 로고
    • SHIP inhibits Akt activation in B cells through regulation of Akt membrane localization
    • Carver D.J., Aman M.J., and Ravichandran K.S. SHIP inhibits Akt activation in B cells through regulation of Akt membrane localization. Blood 96 (2000) 1449-1456
    • (2000) Blood , vol.96 , pp. 1449-1456
    • Carver, D.J.1    Aman, M.J.2    Ravichandran, K.S.3
  • 13
    • 4444269330 scopus 로고    scopus 로고
    • Impaired platelet responses to thrombin and collagen in AKT-1-deficient mice
    • Chen J., De S., Damron D.S., Chen W.S., Hay N., and Byzova T.V. Impaired platelet responses to thrombin and collagen in AKT-1-deficient mice. Blood 104 (2004) 1703-1710
    • (2004) Blood , vol.104 , pp. 1703-1710
    • Chen, J.1    De, S.2    Damron, D.S.3    Chen, W.S.4    Hay, N.5    Byzova, T.V.6
  • 14
    • 0029856247 scopus 로고    scopus 로고
    • Early events in erythropoietin-induced signaling
    • Damen J.E., and Krystal G. Early events in erythropoietin-induced signaling. Exp Hematol 24 (1996) 1455-1459
    • (1996) Exp Hematol , vol.24 , pp. 1455-1459
    • Damen, J.E.1    Krystal, G.2
  • 15
    • 0030948401 scopus 로고    scopus 로고
    • SIP/SHIP inhibits Xenopus oocyte maturation induced by insulin and phosphatidylinositol 3-kinase
    • Deuter-Reinhard M., Apell G., Pot D., Klippel A., Williams L.T., and Kavanaugh W.M. SIP/SHIP inhibits Xenopus oocyte maturation induced by insulin and phosphatidylinositol 3-kinase. Cell Biol 17 (1997) 2559-2565
    • (1997) Cell Biol , vol.17 , pp. 2559-2565
    • Deuter-Reinhard, M.1    Apell, G.2    Pot, D.3    Klippel, A.4    Williams, L.T.5    Kavanaugh, W.M.6
  • 16
    • 33749836234 scopus 로고    scopus 로고
    • Phosphoinositides in cell regulation and membrane dynamics
    • Di Paolo G., and De Camilli P. Phosphoinositides in cell regulation and membrane dynamics. Nature 443 (2006) 651-657
    • (2006) Nature , vol.443 , pp. 651-657
    • Di Paolo, G.1    De Camilli, P.2
  • 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
    • Dong S., Corre B., Foulon E., Dufour E., Veillette A., Acuto O., et al. 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
    • (2006) J Exp Med , vol.203 , pp. 2509-2518
    • Dong, S.1    Corre, B.2    Foulon, E.3    Dufour, E.4    Veillette, A.5    Acuto, O.6
  • 18
    • 0042744852 scopus 로고    scopus 로고
    • SHIP-2 forms a tetrameric complex with filamin, actin, and GPIb-IX-V: localization of SHIP-2 to the activated platelet actin cytoskeleton
    • Dyson J.M., Munday A.D., Kong A.M., Huysmans R.D., Matzaris M., Layton M.J., et al. SHIP-2 forms a tetrameric complex with filamin, actin, and GPIb-IX-V: localization of SHIP-2 to the activated platelet actin cytoskeleton. Blood 102 (2003) 940-948
    • (2003) Blood , vol.102 , pp. 940-948
    • Dyson, J.M.1    Munday, A.D.2    Kong, A.M.3    Huysmans, R.D.4    Matzaris, M.5    Layton, M.J.6
  • 19
    • 0035842901 scopus 로고    scopus 로고
    • The SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2, binds filamin and regulates submembraneous actin
    • Dyson J.M., O'Malley C.J., Becanovic J., Munday A.D., Berndt M.C., Coghill I.D., et al. The SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2, binds filamin and regulates submembraneous actin. J Cell Biol 155 (2001) 1065-1079
    • (2001) J Cell Biol , vol.155 , pp. 1065-1079
    • Dyson, J.M.1    O'Malley, C.J.2    Becanovic, J.3    Munday, A.D.4    Berndt, M.C.5    Coghill, I.D.6
  • 20
    • 33746257209 scopus 로고    scopus 로고
    • The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism
    • Engelman J.A., Luo J.I., and Cantley L.C. The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism. Nature Rev Genet 7 (2006) 606-619
    • (2006) Nature Rev Genet , vol.7 , pp. 606-619
    • Engelman, J.A.1    Luo, J.I.2    Cantley, L.C.3
  • 21
    • 0034657239 scopus 로고    scopus 로고
    • pp60c-src Associates with the SH2-containing inositol-5-phosphatase SHIP1 and is involved in its tyrosine phosphorylation downstream of alphaIIbbeta3 integrin in human platelets
    • Giuriato S., Bodin S., Erneux C., Woscholski R., Plantavid M., Chap H., et al. pp60c-src Associates with the SH2-containing inositol-5-phosphatase SHIP1 and is involved in its tyrosine phosphorylation downstream of alphaIIbbeta3 integrin in human platelets. Biochem J 348 (2000) 107-112
    • (2000) Biochem J , vol.348 , pp. 107-112
    • Giuriato, S.1    Bodin, S.2    Erneux, C.3    Woscholski, R.4    Plantavid, M.5    Chap, H.6
  • 22
    • 0030783120 scopus 로고    scopus 로고
    • Tyrosine phosphorylation and relocation of SHIP are integrin-mediated in thrombin-stimulated human blood platelets
    • Giuriato S., Payrastre B., Drayer A.L., Plantavid M., Woscholski R., Parker P., et al. Tyrosine phosphorylation and relocation of SHIP are integrin-mediated in thrombin-stimulated human blood platelets. J Biol Chem 272 (1997) 26857-26863
    • (1997) J Biol Chem , vol.272 , pp. 26857-26863
    • Giuriato, S.1    Payrastre, B.2    Drayer, A.L.3    Plantavid, M.4    Woscholski, R.5    Parker, P.6
  • 23
    • 0345688084 scopus 로고    scopus 로고
    • SH2-containing inositol 5-phosphatases 1 and 2 in blood platelets: their interactions and roles in the control of phosphatidylinositol 3,4,5-trisphosphate levels
    • Giuriato S., Pesesse X., Bodin S., Sasaki T., Viala C., Marion E., et al. SH2-containing inositol 5-phosphatases 1 and 2 in blood platelets: their interactions and roles in the control of phosphatidylinositol 3,4,5-trisphosphate levels. Biochem J 376 (2003) 199-207
    • (2003) Biochem J , vol.376 , pp. 199-207
    • Giuriato, S.1    Pesesse, X.2    Bodin, S.3    Sasaki, T.4    Viala, C.5    Marion, E.6
  • 24
    • 33748433789 scopus 로고    scopus 로고
    • Restoration of SHIP-1 activity in human leukemic cells modifies NF-kappaB activation pathway and cellular survival upon oxidative stress
    • Gloire G., Charlier E., Rahmouni S., Volanti C., Chariot A., Erneux C., et al. Restoration of SHIP-1 activity in human leukemic cells modifies NF-kappaB activation pathway and cellular survival upon oxidative stress. Oncogene 25 (2006) 5485-5494
    • (2006) Oncogene , vol.25 , pp. 5485-5494
    • Gloire, G.1    Charlier, E.2    Rahmouni, S.3    Volanti, C.4    Chariot, A.5    Erneux, C.6
  • 25
    • 34247154340 scopus 로고    scopus 로고
    • The role of SHIP1 in T-lymphocyte life and death
    • Gloire G., Erneux C., and Piette J. The role of SHIP1 in T-lymphocyte life and death. Biochem Soc Trans 35 (2007) 277-280
    • (2007) Biochem Soc Trans , vol.35 , pp. 277-280
    • Gloire, G.1    Erneux, C.2    Piette, J.3
  • 26
    • 0034668382 scopus 로고    scopus 로고
    • FcgammaRIIA requires a Gi-dependent pathway for an efficient stimulation of phosphoinositide 3-kinase, calcium mobilization, and platelet aggregation
    • Gratacap M.P., Herault J.P., Viala C., Ragab A., Savi P., Herbert J.M., et al. FcgammaRIIA requires a Gi-dependent pathway for an efficient stimulation of phosphoinositide 3-kinase, calcium mobilization, and platelet aggregation. Blood 96 (2000) 3439-3446
    • (2000) Blood , vol.96 , pp. 3439-3446
    • Gratacap, M.P.1    Herault, J.P.2    Viala, C.3    Ragab, A.4    Savi, P.5    Herbert, J.M.6
  • 27
    • 0032544546 scopus 로고    scopus 로고
    • Phosphatidylinositol 3,4,5-trisphosphate-dependent stimulation of phospholipase C-gamma2 is an early key event in FcgammaRIIA-mediated activation of human platelets
    • Gratacap M.P., Payrastre B., Viala C., Mauco G., Plantavid M., and Chap H. Phosphatidylinositol 3,4,5-trisphosphate-dependent stimulation of phospholipase C-gamma2 is an early key event in FcgammaRIIA-mediated activation of human platelets. J Biol Chem 273 (1998) 24314-24321
    • (1998) J Biol Chem , vol.273 , pp. 24314-24321
    • Gratacap, M.P.1    Payrastre, B.2    Viala, C.3    Mauco, G.4    Plantavid, M.5    Chap, H.6
  • 28
    • 0028951464 scopus 로고
    • Integrin-dependent translocation of phosphoinositide 3-kinase to the cytoskeleton of thrombin-activated platelets involves specific interactions of p85 alpha with actin filaments and focal adhesion kinase
    • Guinebault C., Payrastre B., Racaud-Sultan C., Mazarguil H., Breton M., Mauco G., et al. Integrin-dependent translocation of phosphoinositide 3-kinase to the cytoskeleton of thrombin-activated platelets involves specific interactions of p85 alpha with actin filaments and focal adhesion kinase. J Cell Biol 129 (1995) 831-842
    • (1995) J Cell Biol , vol.129 , pp. 831-842
    • Guinebault, C.1    Payrastre, B.2    Racaud-Sultan, C.3    Mazarguil, H.4    Breton, M.5    Mauco, G.6
  • 29
    • 0030474160 scopus 로고    scopus 로고
    • D3 phosphoinositides and outside-in integrin signaling by glycoprotein IIb-IIIa mediate platelet actin assembly and filopodial extension induced by phorbol 12-myristate 13-acetate
    • Hartwig J.H., Kung S., Kovacsovics T., Janmey P.A., Cantley L.C., Stossel T.P., et al. D3 phosphoinositides and outside-in integrin signaling by glycoprotein IIb-IIIa mediate platelet actin assembly and filopodial extension induced by phorbol 12-myristate 13-acetate. J Biol Chem 271 (1996) 32986-32993
    • (1996) J Biol Chem , vol.271 , pp. 32986-32993
    • Hartwig, J.H.1    Kung, S.2    Kovacsovics, T.3    Janmey, P.A.4    Cantley, L.C.5    Stossel, T.P.6
  • 30
    • 0242495010 scopus 로고    scopus 로고
    • Homeostasis and regeneration of the hematopoietic stem cell pool are altered in SHIP-deficient mice
    • Helgason C.D., Antonchuk J., Bodner C., and Humphries R.K. Homeostasis and regeneration of the hematopoietic stem cell pool are altered in SHIP-deficient mice. Blood 102 (2003) 3541-3547
    • (2003) Blood , vol.102 , pp. 3541-3547
    • Helgason, C.D.1    Antonchuk, J.2    Bodner, C.3    Humphries, R.K.4
  • 31
    • 2642684541 scopus 로고    scopus 로고
    • Targeted disruption of SHIP leads to hematopoietic perturbations, lung pathology, and shortened life span
    • Helgason C.D., Damen J.E., Rosten P., Grewal R., Sorensen P., Chappel S.M., et al. Targeted disruption of SHIP leads to hematopoietic perturbations, lung pathology, and shortened life span. Genes Dev 12 (1998) 1610-1620
    • (1998) Genes Dev , vol.12 , pp. 1610-1620
    • Helgason, C.D.1    Damen, J.E.2    Rosten, P.3    Grewal, R.4    Sorensen, P.5    Chappel, S.M.6
  • 34
    • 0032535647 scopus 로고    scopus 로고
    • Targeted disruption of SHIP leads to Steel factor-induced degranulation of mast cells
    • Huber M., Helgason C.D., Scheid M.P., Duronio V., Humphries R.K., and Krystal G. Targeted disruption of SHIP leads to Steel factor-induced degranulation of mast cells. EMBO J 17 (1998) 7311-7319
    • (1998) EMBO J , vol.17 , pp. 7311-7319
    • Huber, M.1    Helgason, C.D.2    Scheid, M.P.3    Duronio, V.4    Humphries, R.K.5    Krystal, G.6
  • 35
    • 0032530195 scopus 로고    scopus 로고
    • The src homology 2-containing inositol phosphatase (SHIP) is the gatekeeper of mast cell degranulation
    • Huber M., Helgason C.D., Damen J.E., Liu L., Humphries R.K., and Krystal G. The src homology 2-containing inositol phosphatase (SHIP) is the gatekeeper of mast cell degranulation. Proc Natl Acad Sci U S A 95 (1998) 11330-11335
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 11330-11335
    • Huber, M.1    Helgason, C.D.2    Damen, J.E.3    Liu, L.4    Humphries, R.K.5    Krystal, G.6
  • 37
    • 2342486055 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinases and the regulation of platelet function
    • Jackson S.P., Yap C.L., and Anderson K.E. Phosphoinositide 3-kinases and the regulation of platelet function. Biochem Soc Trans 32 (2004) 387-392
    • (2004) Biochem Soc Trans , vol.32 , pp. 387-392
    • Jackson, S.P.1    Yap, C.L.2    Anderson, K.E.3
  • 40
    • 0030113662 scopus 로고    scopus 로고
    • Multiple forms of an inositol polyphosphate 5-phosphatase form signaling complexes with Shc and Grb2
    • Kavanaugh W.M., Pot D.A., Chin S.M., Deuter-Reinhard M., Jefferson A.B., Norris F.A., et al. Multiple forms of an inositol polyphosphate 5-phosphatase form signaling complexes with Shc and Grb2. Curr Biol 6 (1996 Apr 1) 438-445
    • (1996) Curr Biol , vol.6 , pp. 438-445
    • Kavanaugh, W.M.1    Pot, D.A.2    Chin, S.M.3    Deuter-Reinhard, M.4    Jefferson, A.B.5    Norris, F.A.6
  • 41
    • 0029050557 scopus 로고
    • Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation
    • Kovacsovics T.J., Bachelot C., Toker A., Vlahos C.J., Duckworth B., Cantley L.C., et al. Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets but reverses platelet aggregation. J Biol Chem 270 (1995) 11358-11366
    • (1995) J Biol Chem , vol.270 , pp. 11358-11366
    • Kovacsovics, T.J.1    Bachelot, C.2    Toker, A.3    Vlahos, C.J.4    Duckworth, B.5    Cantley, L.C.6
  • 42
    • 5044244482 scopus 로고    scopus 로고
    • Lamellipodin, an Ena/VASP ligand, is implicated in the regulation of lamellipodial dynamics
    • Krause M., Leslie J.D., Stewart M., Lafuente E.M., Valderrama F., Jagannathan R., et al. Lamellipodin, an Ena/VASP ligand, is implicated in the regulation of lamellipodial dynamics. Dev Cell 7 (2004) 571-583
    • (2004) Dev Cell , vol.7 , pp. 571-583
    • Krause, M.1    Leslie, J.D.2    Stewart, M.3    Lafuente, E.M.4    Valderrama, F.5    Jagannathan, R.6
  • 43
    • 0034623228 scopus 로고    scopus 로고
    • Dual regulation of platelet protein kinase B
    • Kroner C., Eybrechts K., and Akkerman J.-W. Dual regulation of platelet protein kinase B. J Biol Chem 275 (2000) 27790-27798
    • (2000) J Biol Chem , vol.275 , pp. 27790-27798
    • Kroner, C.1    Eybrechts, K.2    Akkerman, J.-W.3
  • 44
    • 0030610802 scopus 로고    scopus 로고
    • 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
    • Lamkin T.D., Walk S.F., Liu L., Damen J.E., Krystal G., and Ravichandran K.S. 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
    • (1997) J Biol Chem , vol.272 , pp. 10396-10401
    • Lamkin, T.D.1    Walk, S.F.2    Liu, L.3    Damen, J.E.4    Krystal, G.5    Ravichandran, K.S.6
  • 45
    • 0038281249 scopus 로고    scopus 로고
    • Phosphoinositide recognition domains
    • Lemmon M.A. Phosphoinositide recognition domains. Traffic 4 (2003) 201-213
    • (2003) Traffic , vol.4 , pp. 201-213
    • Lemmon, M.A.1
  • 46
    • 0036181869 scopus 로고    scopus 로고
    • PTEN: The down side of PI 3-kinase signalling
    • Leslie N.R., and Downes C.P. PTEN: The down side of PI 3-kinase signalling. Cell Signal 14 (2002) 285-295
    • (2002) Cell Signal , vol.14 , pp. 285-295
    • Leslie, N.R.1    Downes, C.P.2
  • 47
    • 12444339342 scopus 로고    scopus 로고
    • Dynamic interaction of Fc gamma receptor IIB with filamin-bound SHIP1 amplify filamentous actin-dependent negative regulation of Fc epsilon receptor I signaling
    • Lesourne R., Fridman W.H., and Daeron M. Dynamic interaction of Fc gamma receptor IIB with filamin-bound SHIP1 amplify filamentous actin-dependent negative regulation of Fc epsilon receptor I signaling. J. Immunol 174 (2005) 1365-1373
    • (2005) J. Immunol , vol.174 , pp. 1365-1373
    • Lesourne, R.1    Fridman, W.H.2    Daeron, M.3
  • 48
    • 0029665083 scopus 로고    scopus 로고
    • p150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity
    • Lioubin M.N., Algate P.A., Tsai S., Carlberg K., Aebersold A., and Rohrschneider L.R. p150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity. Genes Dev 10 (1996) 1084-1095
    • (1996) Genes Dev , vol.10 , pp. 1084-1095
    • Lioubin, M.N.1    Algate, P.A.2    Tsai, S.3    Carlberg, K.4    Aebersold, A.5    Rohrschneider, L.R.6
  • 49
    • 0030975468 scopus 로고    scopus 로고
    • 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
    • Liu L., Damen J.E., Hughes M.R., Babic I., Jirik F.R., and Krystal G. 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 (1997) 8983-8988
    • (1997) J Biol Chem , vol.272 , pp. 8983-8988
    • Liu, L.1    Damen, J.E.2    Hughes, M.R.3    Babic, I.4    Jirik, F.R.5    Krystal, G.6
  • 50
    • 0036196812 scopus 로고    scopus 로고
    • Regulation of the immune response by SHIP
    • March M.E., and Ravichandran K. Regulation of the immune response by SHIP. Semin Immunol 14 (2002) 37-47
    • (2002) Semin Immunol , vol.14 , pp. 37-47
    • March, M.E.1    Ravichandran, K.2
  • 51
    • 3543010757 scopus 로고    scopus 로고
    • SHIP1 and Lyn kinase negatively regulate integrin alpha IIb beta 3 signaling in platelets
    • Maxwell M.J., Yuan Y., Anderson K.E., Hibbs M.L., Salem H.H., and Jackson S.P. SHIP1 and Lyn kinase negatively regulate integrin alpha IIb beta 3 signaling in platelets. J Biol Chem 279 (2004) 32196-32204
    • (2004) J Biol Chem , vol.279 , pp. 32196-32204
    • Maxwell, M.J.1    Yuan, Y.2    Anderson, K.E.3    Hibbs, M.L.4    Salem, H.H.5    Jackson, S.P.6
  • 52
    • 33845889090 scopus 로고    scopus 로고
    • Control of cell polarity and motility by the PtdIns(3,4,5)P3 phosphatase SHIP1
    • Nishio M., Watanabe K., Sasaki J., Taya C., Takasuga S., Iizuka R., et al. Control of cell polarity and motility by the PtdIns(3,4,5)P3 phosphatase SHIP1. Nat Cell Biol 9 (2007) 36-44
    • (2007) Nat Cell Biol , vol.9 , pp. 36-44
    • Nishio, M.1    Watanabe, K.2    Sasaki, J.3    Taya, C.4    Takasuga, S.5    Iizuka, R.6
  • 53
    • 0030890880 scopus 로고    scopus 로고
    • Inositol polyphosphate 4-phosphatase is inactivated by calpain-mediated proteolysis in stimulated human platelets
    • Norris F.A., Atkins R.C., and Majerus P.W. Inositol polyphosphate 4-phosphatase is inactivated by calpain-mediated proteolysis in stimulated human platelets. J Biol Chem 272 (1997) 10987-10989
    • (1997) J Biol Chem , vol.272 , pp. 10987-10989
    • Norris, F.A.1    Atkins, R.C.2    Majerus, P.W.3
  • 54
    • 34548330713 scopus 로고    scopus 로고
    • Small molecule agonists of SHIP1 inhibit the phosphoinositide 3-kinase pathway in hematopoietic cells
    • Ong C.J., Ming-Lum A., Nodwell M., Ghanipour A., Yang L., Williams D.E., et al. Small molecule agonists of SHIP1 inhibit the phosphoinositide 3-kinase pathway in hematopoietic cells. Blood 110 (2007) 1942-1949
    • (2007) Blood , vol.110 , pp. 1942-1949
    • Ong, C.J.1    Ming-Lum, A.2    Nodwell, M.3    Ghanipour, A.4    Yang, L.5    Williams, D.E.6
  • 55
    • 0029803010 scopus 로고    scopus 로고
    • The inositol 5′-phosphatase SHIP binds to immunoreceptor signaling motifs and responds to high affinity IgE receptor aggregation
    • Osborne M.A., Zenner G., Lubinus M., Zhang X., Songyang Z., Cantley L.C., et al. 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
    • (1996) J Biol Chem , vol.271 , pp. 29271-29278
    • Osborne, M.A.1    Zenner, G.2    Lubinus, M.3    Zhang, X.4    Songyang, Z.5    Cantley, L.C.6
  • 57
    • 0033567185 scopus 로고    scopus 로고
    • A collagen-related peptide regulates phospholipase Cgamma2 via phosphatidylinositol 3-kinase in human platelets
    • Pasquet J.M., Bobe R., Gross B., Gratacap M.P., Tomlinson M.G., Payrastre B., et al. A collagen-related peptide regulates phospholipase Cgamma2 via phosphatidylinositol 3-kinase in human platelets. Biochem J 342 (1999) 171-177
    • (1999) Biochem J , vol.342 , pp. 171-177
    • Pasquet, J.M.1    Bobe, R.2    Gross, B.3    Gratacap, M.P.4    Tomlinson, M.G.5    Payrastre, B.6
  • 58
    • 0034660077 scopus 로고    scopus 로고
    • Phosphatidylinositol 3,4,5-trisphosphate regulates Ca(2+) entry via btk in platelets and megakaryocytes without increasing phospholipase C activity
    • Pasquet J.M., Quek L., Stevens C., Bobe R., Huber M., Duronio V., et al. Phosphatidylinositol 3,4,5-trisphosphate regulates Ca(2+) entry via btk in platelets and megakaryocytes without increasing phospholipase C activity. EMBO J 15 19 (2000) 2793-2802
    • (2000) EMBO J , vol.15 , Issue.19 , pp. 2793-2802
    • Pasquet, J.M.1    Quek, L.2    Stevens, C.3    Bobe, R.4    Huber, M.5    Duronio, V.6
  • 62
    • 33748205100 scopus 로고    scopus 로고
    • SHIP1/2 interaction with tyrosine phosphorylated peptides mimicking an immunoreceptor signaling motif
    • Pesesse X., Backers K., Moreau C., Zhang J., Blero D., Paternotte N., et al. SHIP1/2 interaction with tyrosine phosphorylated peptides mimicking an immunoreceptor signaling motif. Adv Enzyme Regul 46 (2006) 142-153
    • (2006) Adv Enzyme Regul , vol.46 , pp. 142-153
    • Pesesse, X.1    Backers, K.2    Moreau, C.3    Zhang, J.4    Blero, D.5    Paternotte, N.6
  • 63
    • 0031590449 scopus 로고    scopus 로고
    • Identification of a second SH2-domain-containing protein closely related to the phosphatidylinositol polyphosphate 5-phosphatase SHIP
    • Pesesse X., Deleu S., De Smedt F., Drayer L., and Erneux C. 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
    • (1997) Biochem Biophys Res Commun , vol.239 , pp. 697-700
    • Pesesse, X.1    Deleu, S.2    De Smedt, F.3    Drayer, L.4    Erneux, C.5
  • 64
    • 7944228843 scopus 로고    scopus 로고
    • Subversion of phosphoinositide metabolism by intracellular bacterial pathogens
    • Pizarro-Cerda J., and Cossart P. Subversion of phosphoinositide metabolism by intracellular bacterial pathogens. Nat Cell Biol 6 (2004) 1026-1033
    • (2004) Nat Cell Biol , vol.6 , pp. 1026-1033
    • Pizarro-Cerda, J.1    Cossart, P.2
  • 65
    • 22244469478 scopus 로고    scopus 로고
    • Eph kinases and ephrins support thrombus growth and stability by regulating integrin outside-in signaling in platelets
    • Prevost N., Woulfe D.S., Jiang H., Stalker T.J., Marchese P., Ruggeri Z.M., et al. Eph kinases and ephrins support thrombus growth and stability by regulating integrin outside-in signaling in platelets. Proc Natl Acad Sci U S A 102 (2005) 9820-9825
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 9820-9825
    • Prevost, N.1    Woulfe, D.S.2    Jiang, H.3    Stalker, T.J.4    Marchese, P.5    Ruggeri, Z.M.6
  • 66
    • 51549087313 scopus 로고    scopus 로고
    • Ragab A, Severin S, Gratacap MP, Aguado E, Malissen M, Jandrot-Perrus M, et al. Roles of the C-terminal tyrosine residues of LAT in GPVI-induced platelet activation; insights in the mechanism of PLC{gamma}2 activation. Blood, in press.
    • Ragab A, Severin S, Gratacap MP, Aguado E, Malissen M, Jandrot-Perrus M, et al. Roles of the C-terminal tyrosine residues of LAT in GPVI-induced platelet activation; insights in the mechanism of PLC{gamma}2 activation. Blood, in press.
  • 68
    • 0032055484 scopus 로고    scopus 로고
    • Phosphatidylinositol-3,4,5-trisphosphate (PtdIns-3,4,5-P3)/Tec kinase-dependent calcium signaling pathway: a target for SHIP-mediated inhibitory signals
    • Scharenberg A.M., El-Hillal O., Fruman D.A., Beitz L.O., Li Z., Lin S., et al. Phosphatidylinositol-3,4,5-trisphosphate (PtdIns-3,4,5-P3)/Tec kinase-dependent calcium signaling pathway: a target for SHIP-mediated inhibitory signals. EMBO J 17 (1998) 1961-1972
    • (1998) EMBO J , vol.17 , pp. 1961-1972
    • Scharenberg, A.M.1    El-Hillal, O.2    Fruman, D.A.3    Beitz, L.O.4    Li, Z.5    Lin, S.6
  • 69
    • 0037088681 scopus 로고    scopus 로고
    • Phosphatidylinositol (3,4,5)P3 is essential but not sufficient for protein kinase B (PKB) activation; phosphatidylinositol (3,4)P2 is required for PKB phosphorylation at Ser-473: studies using cells from SH2-containing inositol-5-phosphatase knockout mice
    • Scheid M.P., Huber M., Damen J.E., Hughes M., Kang V., Neilsen P., et al. Phosphatidylinositol (3,4,5)P3 is essential but not sufficient for protein kinase B (PKB) activation; phosphatidylinositol (3,4)P2 is required for PKB phosphorylation at Ser-473: studies using cells from SH2-containing inositol-5-phosphatase knockout mice. J Biol Chem 277 (2002) 9027-9035
    • (2002) J Biol Chem , vol.277 , pp. 9027-9035
    • Scheid, M.P.1    Huber, M.2    Damen, J.E.3    Hughes, M.4    Kang, V.5    Neilsen, P.6
  • 70
    • 34147111417 scopus 로고    scopus 로고
    • Deficiency of Src homology 2 domain-containing inositol 5-phosphatase 1 affects platelet responses and thrombus growth
    • Severin S., Gratacap M.P., Lenain N., Alvarez L., Hollande E., Penninger J.M., et al. Deficiency of Src homology 2 domain-containing inositol 5-phosphatase 1 affects platelet responses and thrombus growth. J Clin Invest 117 (2007) 944-952
    • (2007) J Clin Invest , vol.117 , pp. 944-952
    • Severin, S.1    Gratacap, M.P.2    Lenain, N.3    Alvarez, L.4    Hollande, E.5    Penninger, J.M.6
  • 71
    • 0345097326 scopus 로고    scopus 로고
    • 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
    • Sly L.M., Rauh M.J., Kalesnikoff J., Büchse T., and Krystal G. 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
    • (2003) Exp Hematol , vol.31 , pp. 1170-1181
    • Sly, L.M.1    Rauh, M.J.2    Kalesnikoff, J.3    Büchse, T.4    Krystal, G.5
  • 72
    • 0035793622 scopus 로고    scopus 로고
    • 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
    • Stefan M., Koch A., Mancini A., Mohr A., Weidner K.M., Niemann H., et al. 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. J Biol Chem 276 (2001) 3017-3023
    • (2001) J Biol Chem , vol.276 , pp. 3017-3023
    • Stefan, M.1    Koch, A.2    Mancini, A.3    Mohr, A.4    Weidner, K.M.5    Niemann, H.6
  • 73
    • 0026354977 scopus 로고
    • Involvement of platelet glycoprotein IIb-IIIa (alpha IIb-beta 3 integrin) in thrombin-induced synthesis of phosphatidylinositol 3′,4′-bisphosphate
    • Sultan C., Plantavid M., Bachelot C., Grondin P., Breton M., Mauco G., et al. Involvement of platelet glycoprotein IIb-IIIa (alpha IIb-beta 3 integrin) in thrombin-induced synthesis of phosphatidylinositol 3′,4′-bisphosphate. J Biol Chem 266 (1991) 23554-23557
    • (1991) J Biol Chem , vol.266 , pp. 23554-23557
    • Sultan, C.1    Plantavid, M.2    Bachelot, C.3    Grondin, P.4    Breton, M.5    Mauco, G.6
  • 74
    • 0036280038 scopus 로고    scopus 로고
    • Phosphoinositides and signal transduction
    • Toker A. Phosphoinositides and signal transduction. Cell Mol Life Sci 59 (2002) 761-779
    • (2002) Cell Mol Life Sci , vol.59 , pp. 761-779
    • Toker, A.1
  • 75
    • 11244353237 scopus 로고    scopus 로고
    • SHIP family inositol phosphatases interact with and negatively regulate the Tec tyrosine kinase
    • Tomlinson M.G., Heath V.L., Turck C.W., Watson S.P., and Weiss A. SHIP family inositol phosphatases interact with and negatively regulate the Tec tyrosine kinase. J Biol Chem 279 (2004) 55089-55096
    • (2004) J Biol Chem , vol.279 , pp. 55089-55096
    • Tomlinson, M.G.1    Heath, V.L.2    Turck, C.W.3    Watson, S.P.4    Weiss, A.5
  • 77
    • 0030854757 scopus 로고    scopus 로고
    • Recruitment and phosphorylation of SH2-containing inositol phosphatase and Shc to the B-cell Fc gamma immunoreceptor tyrosine-based inhibition motif peptide motif
    • Tridandapani S., Kelley T., Pradhan M., Cooney D., Justement L.B., and Coggeshall K.M. Recruitment and phosphorylation of SH2-containing inositol phosphatase and Shc to the B-cell Fc gamma immunoreceptor tyrosine-based inhibition motif peptide motif. Mol Cell Biol 17 (1997) 4305-4311
    • (1997) Mol Cell Biol , vol.17 , pp. 4305-4311
    • Tridandapani, S.1    Kelley, T.2    Pradhan, M.3    Cooney, D.4    Justement, L.B.5    Coggeshall, K.M.6
  • 78
  • 79
    • 13044263119 scopus 로고    scopus 로고
    • A key role of adenosine diphosphate in the irreversible platelet aggregation induced by the PAR1-activating peptide through the late activation of phosphoinositide 3-kinase
    • Trumel C., Payrastre B., Plantavid M., Hechler B., Viala C., Presek P., et al. A key role of adenosine diphosphate in the irreversible platelet aggregation induced by the PAR1-activating peptide through the late activation of phosphoinositide 3-kinase. Blood 94 (1999) 4156-4165
    • (1999) Blood , vol.94 , pp. 4156-4165
    • Trumel, C.1    Payrastre, B.2    Plantavid, M.3    Hechler, B.4    Viala, C.5    Presek, P.6
  • 80
    • 33750336748 scopus 로고    scopus 로고
    • The influence of anionic lipids on SHIP2 phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase activity
    • Vandeput F., Backers K., Villeret V., Pesesse X., and Erneux C. The influence of anionic lipids on SHIP2 phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase activity. Cell Signal 18 (2006) 2193-2199
    • (2006) Cell Signal , vol.18 , pp. 2193-2199
    • Vandeput, F.1    Backers, K.2    Villeret, V.3    Pesesse, X.4    Erneux, C.5
  • 81
    • 18044388905 scopus 로고    scopus 로고
    • Preclinical and clinical studies with selective reversible direct P2Y12 antagonists
    • Van Giezen J.J., and Humphries R.G. Preclinical and clinical studies with selective reversible direct P2Y12 antagonists. Semin Thromb Hemost 31 (2005) 195-204
    • (2005) Semin Thromb Hemost , vol.31 , pp. 195-204
    • Van Giezen, J.J.1    Humphries, R.G.2
  • 83
    • 0029859565 scopus 로고    scopus 로고
    • Cloning and characterization of human SHIP, the 145-kD inositol 5-phosphatase that associates with SHC after cytokine stimulation
    • Ware M.D., Rosten P., Damen J.E., Liu L., Humphries R.K., and Krystal G. Cloning and characterization of human SHIP, the 145-kD inositol 5-phosphatase that associates with SHC after cytokine stimulation. Blood 88 (1996) 2833-2840
    • (1996) Blood , vol.88 , pp. 2833-2840
    • Ware, M.D.1    Rosten, P.2    Damen, J.E.3    Liu, L.4    Humphries, R.K.5    Krystal, G.6
  • 84
    • 1542317617 scopus 로고    scopus 로고
    • Defects in secretion, aggregation, and thrombus formation in platelets from mice lacking Akt2
    • Woulfe D., Jiang H., Morgans A., Monks R., Birnbaum M., and Brass L.F. Defects in secretion, aggregation, and thrombus formation in platelets from mice lacking Akt2. J Clin Invest 113 (2004) 441-450
    • (2004) J Clin Invest , vol.113 , pp. 441-450
    • Woulfe, D.1    Jiang, H.2    Morgans, A.3    Monks, R.4    Birnbaum, M.5    Brass, L.F.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.