메뉴 건너뛰기




Volumn 162, Issue 3, 1999, Pages 1408-1414

Protein interactions of Src homology 2 (SH2) domain-containing inositol phosphatase (SHIP): Association with Shc displaces SHIP from FcγRIIb in B cells

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDE; PHOSPHATASE; PROTEIN;

EID: 0033083194     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (55)

References (40)
  • 1
    • 0030831199 scopus 로고    scopus 로고
    • The complexity of signaling pathways activated by the BCR
    • DeFranco, A. L. 1997. The complexity of signaling pathways activated by the BCR. Curr. Opin. Immunol. 9:296.
    • (1997) Curr. Opin. Immunol. , vol.9 , pp. 296
    • DeFranco, A.L.1
  • 3
    • 0030891713 scopus 로고    scopus 로고
    • ITIMs and ITAMs. The yin and yang of antigen and Fc receptor-linked signaling machinery
    • Isakov, N. 1997. ITIMs and ITAMs. The yin and yang of antigen and Fc receptor-linked signaling machinery. Immunol. Res. 16:85-100.
    • (1997) Immunol. Res. , vol.16 , pp. 85-100
    • Isakov, N.1
  • 4
    • 0030293986 scopus 로고    scopus 로고
    • The She adaptor protein is highly phosphorylated at conserved, twin tyrosine residues (Y239/240) that mediate protein-protein interactions
    • van der Geer, P., S. Wiley, G. G. Gish, and T. Pawson. 1996. The She adaptor protein is highly phosphorylated at conserved, twin tyrosine residues (Y239/240) that mediate protein-protein interactions. Curr. Biol. 6:1435.
    • (1996) Curr. Biol. , vol.6 , pp. 1435
    • Van Der Geer, P.1    Wiley, S.2    Gish, G.G.3    Pawson, T.4
  • 5
    • 0028049245 scopus 로고
    • Epidermal growth factor-receptor mutant lacking the autophosphorylation sites induces phosphorylation of She protein and Shc-Grb2/ASH association and retains mitogenic activity
    • Gotoh, N., A. Tojo, K. Muroya, Y. Hashimoto, S. Hattori, S. Nakamura, T. Takenawa, Y. Yazaki, and M. Shibuya. 1994. Epidermal growth factor-receptor mutant lacking the autophosphorylation sites induces phosphorylation of She protein and Shc-Grb2/ASH association and retains mitogenic activity. Proc. Natl. Acad. Sci. USA 91:167.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 167
    • Gotoh, N.1    Tojo, A.2    Muroya, K.3    Hashimoto, Y.4    Hattori, S.5    Nakamura, S.6    Takenawa, T.7    Yazaki, Y.8    Shibuya, M.9
  • 6
    • 0000374718 scopus 로고    scopus 로고
    • The Grb2-mSosl complex binds phosphopeplides with higher affinity than Grb2
    • Chook, Y. M., G. D. Gish, C. M. Kay, E. F, Pai, and T. Pawson. 1996. The Grb2-mSosl complex binds phosphopeplides with higher affinity than Grb2. J. Biol. Chem. 271:30472.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30472
    • Chook, Y.M.1    Gish, G.D.2    Kay, C.M.3    Pai, E.F.4    Pawson, T.5
  • 7
    • 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., J. E. Damen, M. R. Hughes, I. Babic, F. R. Jirik, and G. Krystal. 1997. The Src homology 2 (SH2) domain of SH2-containing inositol phosphatase (SHIP) is essential for tyrosine phosphorylation of SHIP, its association with Shc and its induction of apoptosis. J. Biol. Chem. 272:8983.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8983
    • Liu, L.1    Damen, J.E.2    Hughes, M.R.3    Babic, I.4    Jirik, F.R.5    Krystal, G.6
  • 8
    • 0030923454 scopus 로고    scopus 로고
    • Activation-induced bi-dentate SHIP and Shc interaction in B lymphocytes
    • Pradhan, M., and K. M. Coggeshall. 1997. Activation-induced bi-dentate SHIP and Shc interaction in B lymphocytes. J. Cell. Biochem. 67:32.
    • (1997) J. Cell. Biochem. , vol.67 , pp. 32
    • Pradhan, M.1    Coggeshall, K.M.2
  • 9
    • 0030962699 scopus 로고    scopus 로고
    • She contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes
    • Harmer, S. L., and A. L. DeFranco. 1997. She contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes. Mol. Cell. Biol. 17:4087.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4087
    • Harmer, S.L.1    DeFranco, A.L.2
  • 10
    • 0027931640 scopus 로고
    • Membrane targeting of the nucleotide exchange factor Sos is sufficient for activating the Ras signaling pathway
    • Aronheim, A., D. Engelberg, N. Li, N. al-Alawi, J. Sehlessinger, and M. Karin. 1994. Membrane targeting of the nucleotide exchange factor Sos is sufficient for activating the Ras signaling pathway. Cell 78:949.
    • (1994) Cell , vol.78 , pp. 949
    • Aronheim, A.1    Engelberg, D.2    Li, N.3    Al-Alawi, N.4    Sehlessinger, J.5    Karin, M.6
  • 11
    • 0029880630 scopus 로고    scopus 로고
    • SH2 domain protein interaction and possibilities for pharmacological intervention
    • Beattie, J. 1996. SH2 domain protein interaction and possibilities for pharmacological intervention. Cell Signal 8:75.
    • (1996) Cell Signal , vol.8 , pp. 75
    • Beattie, J.1
  • 12
    • 0028895156 scopus 로고
    • SH2 and SH3 domains: Potential targets for anti-cancer drug design
    • Smithgall, T. E. 1995. SH2 and SH3 domains: Potential targets for anti-cancer drug design. J. Pharmacol. Toxicol. Methods 34:125.
    • (1995) J. Pharmacol. Toxicol. Methods , vol.34 , pp. 125
    • Smithgall, T.E.1
  • 13
    • 0029117881 scopus 로고
    • SH2 domain specificity determination using oriented phosphopeptide library
    • Zhou, S., and L. C. Cantley. 1995. SH2 domain specificity determination using oriented phosphopeptide library. Methods Ezymol. 254:523.
    • (1995) Methods Ezymol. , vol.254 , pp. 523
    • Zhou, S.1    Cantley, L.C.2
  • 14
    • 0029810421 scopus 로고    scopus 로고
    • Distinct mechanisms mediate Shc association with the activated and resting B cell antigen receptor
    • D'Ambrosio, D., K. L. Hippen, and J. C. Cambier. 1996. Distinct mechanisms mediate Shc association with the activated and resting B cell antigen receptor. Eur. J. Immunol. 26:1960.
    • (1996) Eur. J. Immunol. , vol.26 , pp. 1960
    • D'Ambrosio, D.1    Hippen, K.L.2    Cambier, J.C.3
  • 16
    • 0030587116 scopus 로고    scopus 로고
    • Negative signaling in B-lymphocytes induces tyrosine phosphorylation of the 145-kDa inositol polyphosphate 5-phosphatase, SHIP
    • Chacko, G. W., S. Tridandapani, J. Darnen, L. Liu, G. Krystal, and K. M. Coggeshall. 1996. Negative signaling in B-lymphocytes induces tyrosine phosphorylation of the 145-kDa inositol polyphosphate 5-phosphatase, SHIP. J. Immunol. 157:2234.
    • (1996) J. Immunol. , vol.157 , pp. 2234
    • Chacko, G.W.1    Tridandapani, S.2    Darnen, J.3    Liu, L.4    Krystal, G.5    Coggeshall, K.M.6
  • 17
    • 0030566667 scopus 로고    scopus 로고
    • The SHIP phosphatase becomes associated with FcγRIIB1 and is tyrosine phosphorylated during "negative" signaling
    • D'Ambrosio, D., D. C. Fong, and J. C. Cambier. 1996. The SHIP phosphatase becomes associated with FcγRIIB1 and is tyrosine phosphorylated during "negative" signaling. Immunol. Lett. 54:77.
    • (1996) Immunol. Lett. , vol.54 , pp. 77
    • D'Ambrosio, D.1    Fong, D.C.2    Cambier, J.C.3
  • 18
    • 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. v. Brocklyn, and K. M. Coggeshall. 1997. Negative signaling in B cells causes reduced Ras activity by reducing Shc-Grb2 interactions. J. Immunol. 158:1125.
    • (1997) J. Immunol. , vol.158 , pp. 1125
    • Tridandapani, S.1    Chacko, G.W.2    Brocklyn, J.R.V.3    Coggeshall, K.M.4
  • 20
    • 0029803856 scopus 로고    scopus 로고
    • Human type II Fcγ receptors inhibit B cell activation by interacting with the p21(ras)-dependent pathway
    • Sarmay, G., G. Koncz, and J. Gergely. 1996. Human type II Fcγ receptors inhibit B cell activation by interacting with the p21(ras)-dependent pathway. J. Biol. Chem. 271:30499.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30499
    • Sarmay, G.1    Koncz, G.2    Gergely, J.3
  • 21
    • 0030892128 scopus 로고    scopus 로고
    • Interleukin-3 induces the association of the inositol 5-phosphatase SHIP with SHP2
    • Liu, L., J. E. Damen, M. D. Ware, and G. Krystal. 1997. Interleukin-3 induces the association of the inositol 5-phosphatase SHIP with SHP2. J. Biol. Chem. 272: 10998.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10998
    • Liu, L.1    Damen, J.E.2    Ware, M.D.3    Krystal, G.4
  • 22
    • 0029835940 scopus 로고    scopus 로고
    • Role of the inositol phosphatase SHIP in negative regulation of the immune system by the receptor FcγRIIB
    • Ono, M., S. Bolland, P. Tempst. and J. V. Ravetch. 1996. Role of the inositol phosphatase SHIP in negative regulation of the immune system by the receptor FcγRIIB. Nature 383:263.
    • (1996) Nature , vol.383 , pp. 263
    • Ono, M.1    Bolland, S.2    Tempst, P.3    Ravetch, J.V.4
  • 23
    • 0031033886 scopus 로고    scopus 로고
    • Co-ligation of the antigen and Fc receptors gives rise to the selective modulation of intracellular signaling in B cells: Regulation of the association of phosphatidylinositol 3-kinase and inositol 5'-phosphatase with the antigen receptor complex
    • Kiener, P. A., M. N. Lioubin, L. R. Rohrschneider, J. A. Ledbetter, S. G. Nadler, and M. L. Diegel. 1997. Co-ligation of the antigen and Fc receptors gives rise to the selective modulation of intracellular signaling in B cells: regulation of the association of phosphatidylinositol 3-kinase and inositol 5'-phosphatase with the antigen receptor complex. J. Biol. Chem. 272:3838.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3838
    • Kiener, P.A.1    Lioubin, M.N.2    Rohrschneider, L.R.3    Ledbetter, J.A.4    Nadler, S.G.5    Diegel, M.L.6
  • 24
    • 0030792093 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase SHP-1 is dispensable for FcγRIIB-mediated inhibition of B cell antigen receptor activation
    • Nadler, M. J. S., B. Chen, J. S. Anderson, H. H. Wortis, and B. G. Neel. 1997. Protein-tyrosine phosphatase SHP-1 is dispensable for FcγRIIB-mediated inhibition of B cell antigen receptor activation. J. Biol. Chem. 272:20038.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20038
    • Nadler, M.J.S.1    Chen, B.2    Anderson, J.S.3    Wortis, H.H.4    Neel, B.G.5
  • 26
    • 0025340989 scopus 로고
    • Organization of the human and mouse low-affinity FcγR genes: Duplication and recombination
    • Qiu, W. Q., D. de Bruin, B. H. Brownstein, R. Pearse, and J. V. Ravetch. 1990. Organization of the human and mouse low-affinity FcγR genes: duplication and recombination. Science 248:732.
    • (1990) Science , vol.248 , pp. 732
    • Qiu, W.Q.1    De Bruin, D.2    Brownstein, B.H.3    Pearse, R.4    Ravetch, J.V.5
  • 30
    • 0032524993 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase and SH2-containing inositol phosphatase (SHIP) are recruited by distinct positive and negative growth regulatory domains in the granulocyte colony-stimulating factor receptor
    • Hunter, M. G., and B. R. Avalos. 1998. Phosphatidylinositol 3-kinase and SH2-containing inositol phosphatase (SHIP) are recruited by distinct positive and negative growth regulatory domains in the granulocyte colony-stimulating factor receptor. J. Immunol. 160:4979.
    • (1998) J. Immunol. , vol.160 , pp. 4979
    • Hunter, M.G.1    Avalos, B.R.2
  • 31
    • 0029665083 scopus 로고    scopus 로고
    • P150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity
    • N., A., T. S., R.
    • Lioubin, M., N., P. Algate, A., T. S., K. Carlberg, R. Aebersold, and L. Rohrschneider, R. 1996. p150Ship, a signal transduction molecule with inositol polyphosphate-5-phosphatase activity. Genes Dev. 10:1084.
    • (1996) Genes Dev. , vol.10 , pp. 1084
    • Lioubin, M.1    Algate, P.2    Carlberg, K.3    Aebersold, R.4    Rohrschneider, L.5
  • 32
    • 0343307005 scopus 로고    scopus 로고
    • Deletion of SHIP or SHP-1 reveals two distinct pathways for inhibitory signaling
    • Ono, M., H. Okada, S. Bolland, S. Yanagi, T. Kurosaki, and J. V. Ravetch. 1997. Deletion of SHIP or SHP-1 reveals two distinct pathways for inhibitory signaling. Cell 90:293.
    • (1997) Cell , vol.90 , pp. 293
    • Ono, M.1    Okada, H.2    Bolland, S.3    Yanagi, S.4    Kurosaki, T.5    Ravetch, J.V.6
  • 33
    • 0029943191 scopus 로고    scopus 로고
    • Tyrosine 425 within the activated erythropoietin receptor binds Syp, reduces the erythropoietin required for Syp tyrosine phosphorylation, and promotes mitogenesis
    • Tauchi, T., J. E. Damen, K. Toyama, G. S. Feng, H. E. Broxmeyer, and G. Krystal. 1996. Tyrosine 425 within the activated erythropoietin receptor binds Syp, reduces the erythropoietin required for Syp tyrosine phosphorylation, and promotes mitogenesis. Blood 87:4495.
    • (1996) Blood , vol.87 , pp. 4495
    • Tauchi, T.1    Damen, J.E.2    Toyama, K.3    Feng, G.S.4    Broxmeyer, H.E.5    Krystal, G.6
  • 34
    • 0028896991 scopus 로고
    • Protein-tyrosine-phosphatase SHPTP2 is a required positive effector for insulin down-stream signaling
    • Yamauchi, K., K. L. Milarski, A. R. Saltiel, and J. E. Pessin. 1995. Protein-tyrosine-phosphatase SHPTP2 is a required positive effector for insulin down-stream signaling. Proc. Natl. Acad. Sci. USA 92:664.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 664
    • Yamauchi, K.1    Milarski, K.L.2    Saltiel, A.R.3    Pessin, J.E.4
  • 36
    • 0030066326 scopus 로고    scopus 로고
    • Activation-induced association of a 145-kDa tyrosine-phosphorylated protein with Shc and Syk in B lymphocytes and macrophages
    • Crowley, M. T., S. L. Harmer, and A. L. DeFranco. 1996. Activation-induced association of a 145-kDa tyrosine-phosphorylated protein with Shc and Syk in B lymphocytes and macrophages. J. Biol Chem. 271:1145.
    • (1996) J. Biol Chem. , vol.271 , pp. 1145
    • Crowley, M.T.1    Harmer, S.L.2    DeFranco, A.L.3
  • 37
    • 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., S. F. Walk, L. Liu, J. E. Damen, G. Krystal, and K. S. Ravichandran. 1997. 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. 272:10396.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10396
    • Lamkin, T.D.1    Walk, S.F.2    Liu, L.3    Damen, J.E.4    Krystal, G.5    Ravichandran, K.S.6
  • 38
    • 0032055485 scopus 로고    scopus 로고
    • SHIP modulates immune receptor responses by regulating membrane association of Btk
    • Bolland, S., R. N. Pearse, T. Kurosaki, and J. V. Ravetch. 1998. SHIP modulates immune receptor responses by regulating membrane association of Btk. Immunity 8:509.
    • (1998) Immunity , vol.8 , pp. 509
    • Bolland, S.1    Pearse, R.N.2    Kurosaki, T.3    Ravetch, J.V.4
  • 39
    • 0032055484 scopus 로고    scopus 로고
    • Phosphatidylinositol-3,4,5-trisphosphate (Ptdlns-3,4,5-P3)/Tec kinase-dependent calcium signaling pathways: A target for SHIP-mediated inhibitory signals
    • Scharenberg, A. M., O. El-Hillal, D. A. Fruman, L. O. Beitz, Z. Li, S. Lin, I. Gout, L. C. Cantley, D. J. Rawlings, and J.-P. Kinet. 1998. Phosphatidylinositol-3,4,5-trisphosphate (Ptdlns-3,4,5-P3)/Tec kinase-dependent calcium signaling pathways: a target for SHIP-mediated inhibitory signals. EMBO J. 17:1961.
    • (1998) EMBO J. , vol.17 , pp. 1961
    • Scharenberg, A.M.1    El-Hillal, O.2    Fruman, D.A.3    Beitz, L.O.4    Li, Z.5    Lin, S.6    Gout, I.7    Cantley, L.C.8    Rawlings, D.J.9    Kinet, J.-P.10
  • 40
    • 0031471231 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase-γ activates Bruton's tyrosine kinase in concert with Src family kinases
    • Li, Z., M. I. Wahl, A. Eguinoa, L. R. Stephens, P. T. Hawkins, and O. N. Witte. 1997. Phosphatidylinositol 3-kinase-γ activates Bruton's tyrosine kinase in concert with Src family kinases. Proc. Natl. Acad. Sci. USA 94:13820.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13820
    • Li, Z.1    Wahl, M.I.2    Eguinoa, A.3    Stephens, L.R.4    Hawkins, P.T.5    Witte, O.N.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.