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Volumn 205, Issue 4, 2008, Pages 853-868

Phospholipase C-γ2 and Vav cooperate within signaling microclusters to propagate B cell spreading in response to membrane-bound antigen

Author keywords

[No Author keywords available]

Indexed keywords

B LYMPHOCYTE RECEPTOR; BRUTON TYROSINE KINASE; MEMBRANE ANTIGEN; PHOSPHOLIPASE C GAMMA2; PROTEIN KINASE LYN; PROTEIN KINASE SYK; VAV PROTEIN; ANTIGEN; INOSITOL 1,4,5 TRISPHOSPHATE RECEPTOR; LYN PROTEIN-TYROSINE KINASE; PHOSPHOLIPASE C GAMMA; PROTEIN TYROSINE KINASE; SIGNAL PEPTIDE;

EID: 42249090333     PISSN: 00221007     EISSN: 00221007     Source Type: Journal    
DOI: 10.1084/jem.20072619     Document Type: Article
Times cited : (144)

References (82)
  • 2
    • 0030890949 scopus 로고    scopus 로고
    • Initiation and processing of signals from the B cell antigen receptor
    • Reth, M., and J. Wienands. 1997. Initiation and processing of signals from the B cell antigen receptor. Annu. Rev. Immunol. 15:453-479.
    • (1997) Annu. Rev. Immunol , vol.15 , pp. 453-479
    • Reth, M.1    Wienands, J.2
  • 3
    • 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. 9:296-308.
    • (1997) Curr. Opin. Immunol , vol.9 , pp. 296-308
    • DeFranco, A.L.1
  • 4
    • 0033712984 scopus 로고    scopus 로고
    • Xid-like phenotypes: A B cell signalosome takes shape
    • Fruman, D.A., A.B. Satterthwaite, and O.N. Witte. 2000. Xid-like phenotypes: a B cell signalosome takes shape. Immunity. 13:1-3.
    • (2000) Immunity , vol.13 , pp. 1-3
    • Fruman, D.A.1    Satterthwaite, A.B.2    Witte, O.N.3
  • 5
    • 0035374695 scopus 로고    scopus 로고
    • Vav and the B cell signalosome
    • DeFranco, A.L. 2001. Vav and the B cell signalosome. Nat. Immunol. 2:482-484.
    • (2001) Nat. Immunol , vol.2 , pp. 482-484
    • DeFranco, A.L.1
  • 6
    • 0036584284 scopus 로고    scopus 로고
    • Regulation of B-cell signal transduction by adaptor proteins
    • Kurosaki, T. 2002. Regulation of B-cell signal transduction by adaptor proteins. Nat. Rev. Immunol. 2:354-363.
    • (2002) Nat. Rev. Immunol , vol.2 , pp. 354-363
    • Kurosaki, T.1
  • 9
    • 0036884819 scopus 로고    scopus 로고
    • Regulation of B-cell fate by antigen-receptor signals
    • Niiro, H., and E. Clark. 2002. Regulation of B-cell fate by antigen-receptor signals. Nat. Rev. Immunol. 2:945-956.
    • (2002) Nat. Rev. Immunol , vol.2 , pp. 945-956
    • Niiro, H.1    Clark, E.2
  • 10
    • 4344671730 scopus 로고    scopus 로고
    • Vav-dependent and vav-independent phosphatidylinositol 3-kinase activation in murine B cells determined by the nature of the stimulus
    • Vigorito, E., G. Bardi, J. Glassford, E. Lam, E. Clayton, and M. Turner. 2004. Vav-dependent and vav-independent phosphatidylinositol 3-kinase activation in murine B cells determined by the nature of the stimulus. J. Immunol. 173:3209-3214.
    • (2004) J. Immunol , vol.173 , pp. 3209-3214
    • Vigorito, E.1    Bardi, G.2    Glassford, J.3    Lam, E.4    Clayton, E.5    Turner, M.6
  • 11
    • 42249095588 scopus 로고    scopus 로고
    • B cell antigen receptor-induced Rac1 activation and Rac1-dependent spreading are impaired in transitional immature B cells due to levels of membrane cholesterol
    • Brezski, R.J., and J.G. Monroe. 2007. B cell antigen receptor-induced Rac1 activation and Rac1-dependent spreading are impaired in transitional immature B cells due to levels of membrane cholesterol. J. Immunol. 179:4464-4472.
    • (2007) J. Immunol , vol.179 , pp. 4464-4472
    • Brezski, R.J.1    Monroe, J.G.2
  • 12
    • 0036604966 scopus 로고    scopus 로고
    • Regulation of B cell fates by BCR signaling components
    • Kurosaki, T. 2002. Regulation of B cell fates by BCR signaling components. Curr. Opin. Immunol. 14:341-347.
    • (2002) Curr. Opin. Immunol , vol.14 , pp. 341-347
    • Kurosaki, T.1
  • 13
    • 0023858085 scopus 로고
    • A novel in vivo follicular dendritic cell-dependent iccosome-mediated mechanism for delivery of antigen to antigen-processing cells
    • Szakal, A.K., M.H. Kosco, and J.G. Tew. 1988. A novel in vivo follicular dendritic cell-dependent iccosome-mediated mechanism for delivery of antigen to antigen-processing cells. J. Immunol. 140:341-353.
    • (1988) J. Immunol , vol.140 , pp. 341-353
    • Szakal, A.K.1    Kosco, M.H.2    Tew, J.G.3
  • 14
    • 0030587821 scopus 로고    scopus 로고
    • Follicular dendritic cell-derived antigen and accessory activity in initiation of memory IgG responses in vitro
    • Wu, J., D. Qin, G. Burton, A. Szakal, and J. Tew. 1996. Follicular dendritic cell-derived antigen and accessory activity in initiation of memory IgG responses in vitro. J. Immunol. 157:3404-3411.
    • (1996) J. Immunol , vol.157 , pp. 3404-3411
    • Wu, J.1    Qin, D.2    Burton, G.3    Szakal, A.4    Tew, J.5
  • 15
    • 0032145432 scopus 로고    scopus 로고
    • Dendritic cells interact directly with naive B lymphocytes to transfer antigen and initiate class switching in a primary T-dependent response
    • Wykes, M., A. Pombo, C. Jenkins, and G. MacPherson. 1998. Dendritic cells interact directly with naive B lymphocytes to transfer antigen and initiate class switching in a primary T-dependent response. J. Immunol. 161:1313-1319.
    • (1998) J. Immunol , vol.161 , pp. 1313-1319
    • Wykes, M.1    Pombo, A.2    Jenkins, C.3    MacPherson, G.4
  • 16
    • 0036754302 scopus 로고    scopus 로고
    • Bal á zs, M., F. Martin, T. Zhou, and J. Kearney. 2002. Blood dendritic cells interact with splenic marginal zone B cells to initiate T-independent immune responses. Immunity. 17:341-352.
    • Bal á zs, M., F. Martin, T. Zhou, and J. Kearney. 2002. Blood dendritic cells interact with splenic marginal zone B cells to initiate T-independent immune responses. Immunity. 17:341-352.
  • 17
    • 34447623566 scopus 로고    scopus 로고
    • B cells acquire particulate antigen in a macrophage-rich area at the boundary between the follicle and the subcapsular sinus of the lymph node
    • Carrasco, Y.R., and F.D. Batista. 2007. B cells acquire particulate antigen in a macrophage-rich area at the boundary between the follicle and the subcapsular sinus of the lymph node. Immunity. 27:160-171.
    • (2007) Immunity , vol.27 , pp. 160-171
    • Carrasco, Y.R.1    Batista, F.D.2
  • 18
    • 34548044827 scopus 로고    scopus 로고
    • Subcapsular encounter and complement-dependent transport of immune complexes by lymph node B cells
    • Phan, T.G., I. Grigorova, T. Okada, and J.G. Cyster. 2007. Subcapsular encounter and complement-dependent transport of immune complexes by lymph node B cells. Nat. Immunol. 8:992-1000.
    • (2007) Nat. Immunol , vol.8 , pp. 992-1000
    • Phan, T.G.1    Grigorova, I.2    Okada, T.3    Cyster, J.G.4
  • 20
    • 0035942781 scopus 로고    scopus 로고
    • B cells acquire antigen from target cells after synapse formation
    • Batista, F.D., D. Iber, and M.S. Neuberger. 2001. B cells acquire antigen from target cells after synapse formation. Nature. 411:489-494.
    • (2001) Nature , vol.411 , pp. 489-494
    • Batista, F.D.1    Iber, D.2    Neuberger, M.S.3
  • 21
    • 0032480279 scopus 로고    scopus 로고
    • Three-dimensional segregation of supramolecular activation clusters in T cells
    • Monks, C.R., B.A. Freiberg, H. Kupfer, N. Sciaky, and A. Kupfer. 1998. Three-dimensional segregation of supramolecular activation clusters in T cells. Nature. 395:82-86.
    • (1998) Nature , vol.395 , pp. 82-86
    • Monks, C.R.1    Freiberg, B.A.2    Kupfer, H.3    Sciaky, N.4    Kupfer, A.5
  • 22
    • 0033538574 scopus 로고    scopus 로고
    • The immunological synapse: A molecular machine controlling T cell activation
    • Grakoui, A., S. Bromley, C. Sumen, M. Davis, A. Shaw, P. Allen, and M. Dustin. 1999. The immunological synapse: a molecular machine controlling T cell activation. Science. 285:221-227.
    • (1999) Science , vol.285 , pp. 221-227
    • Grakoui, A.1    Bromley, S.2    Sumen, C.3    Davis, M.4    Shaw, A.5    Allen, P.6    Dustin, M.7
  • 23
    • 33646454106 scopus 로고    scopus 로고
    • B cell ligand discrimination through a spreading and contraction response
    • Fleire, S.J., J.P. Goldman, Y.R. Carrasco, M. Weber, D. Bray, and F.D. Batista. 2006. B cell ligand discrimination through a spreading and contraction response. Science. 312:738-741.
    • (2006) Science , vol.312 , pp. 738-741
    • Fleire, S.J.1    Goldman, J.P.2    Carrasco, Y.R.3    Weber, M.4    Bray, D.5    Batista, F.D.6
  • 24
    • 34548041173 scopus 로고    scopus 로고
    • Mechanistic insight into lymphocyte activation through quantitative imaging and theoretical modelling
    • Treanor, B., and F. Batista. 2007. Mechanistic insight into lymphocyte activation through quantitative imaging and theoretical modelling. Curr. Opin. Immunol. 19:476-483.
    • (2007) Curr. Opin. Immunol , vol.19 , pp. 476-483
    • Treanor, B.1    Batista, F.2
  • 26
    • 27544441784 scopus 로고    scopus 로고
    • Actin and agonist MHC - peptide complex-dependent T cell receptor microclusters as scaffolds for signaling
    • Campi, G., R. Varma, and M. Dustin. 2005. Actin and agonist MHC - peptide complex-dependent T cell receptor microclusters as scaffolds for signaling. J. Exp. Med. 202:1031-1036.
    • (2005) J. Exp. Med , vol.202 , pp. 1031-1036
    • Campi, G.1    Varma, R.2    Dustin, M.3
  • 28
    • 33746011209 scopus 로고    scopus 로고
    • T cell receptor-proximal signals are sustained in peripheral microclusters and terminated in the central supramolecular activation cluster
    • Varma, R., G. Campi, T. Yokosuka, T. Saito, and M. Dustin. 2006. T cell receptor-proximal signals are sustained in peripheral microclusters and terminated in the central supramolecular activation cluster. Immunity. 25:117-127.
    • (2006) Immunity , vol.25 , pp. 117-127
    • Varma, R.1    Campi, G.2    Yokosuka, T.3    Saito, T.4    Dustin, M.5
  • 29
    • 37349077033 scopus 로고    scopus 로고
    • CD19 is essential for B cell activation by promoting B cell receptor-antigen microcluster formation in response to membrane bound ligand
    • Depoil, D., S. Fleire, B. Treanor, M. Weber, K. Marchbank, V. Tybulewicz, M. Reth, N. Harwood, and F. Batista. 2008. CD19 is essential for B cell activation by promoting B cell receptor-antigen microcluster formation in response to membrane bound ligand. Nat. Immunol. 9:63-72.
    • (2008) Nat. Immunol , vol.9 , pp. 63-72
    • Depoil, D.1    Fleire, S.2    Treanor, B.3    Weber, M.4    Marchbank, K.5    Tybulewicz, V.6    Reth, M.7    Harwood, N.8    Batista, F.9
  • 30
    • 0033010661 scopus 로고    scopus 로고
    • Genetic analysis of B cell antigen receptor signaling
    • Kurosaki, T. 1999. Genetic analysis of B cell antigen receptor signaling. Annu. Rev. Immunol. 17:555-592.
    • (1999) Annu. Rev. Immunol , vol.17 , pp. 555-592
    • Kurosaki, T.1
  • 31
    • 34547459959 scopus 로고    scopus 로고
    • Genetic analysis of B cell signaling
    • Shinohara, H., and T. Kurosaki. 2006. Genetic analysis of B cell signaling. Subcell. Biochem. 40:145-187.
    • (2006) Subcell. Biochem , vol.40 , pp. 145-187
    • Shinohara, H.1    Kurosaki, T.2
  • 32
    • 0034927336 scopus 로고    scopus 로고
    • Regulation of phosphoinositide-specific phospholipase C
    • Rhee, S.G. 2001. Regulation of phosphoinositide-specific phospholipase C. Annu. Rev. Biochem. 70:281-312.
    • (2001) Annu. Rev. Biochem , vol.70 , pp. 281-312
    • Rhee, S.G.1
  • 34
    • 0032127159 scopus 로고    scopus 로고
    • BLNK: A central linker protein in B cell activation
    • Fu, C., C. Turck, T. Kurosaki, and A. Chan. 1998. BLNK: a central linker protein in B cell activation. Immunity. 9:93-103.
    • (1998) Immunity , vol.9 , pp. 93-103
    • Fu, C.1    Turck, C.2    Kurosaki, T.3    Chan, A.4
  • 35
    • 0037011114 scopus 로고    scopus 로고
    • BLNK: Molecular scaffolding through 'cis'-mediated organization of signaling proteins
    • Chiu, C.W., M. Dalton, M. Ishiai, T. Kurosaki, and A.C. Chan. 2002. BLNK: molecular scaffolding through 'cis'-mediated organization of signaling proteins. EMBO J. 21:6461-6472.
    • (2002) EMBO J , vol.21 , pp. 6461-6472
    • Chiu, C.W.1    Dalton, M.2    Ishiai, M.3    Kurosaki, T.4    Chan, A.C.5
  • 37
    • 0033214220 scopus 로고    scopus 로고
    • Identification of the SH2 domain binding protein of Bruton' s tyrosine kinase as BLNK-functional significance of Btk-SH2 domain in B-cell antigen receptor-coupled calcium signaling
    • Hashimoto, S., A. Iwamatsu, M. Ishiai, K. Okawa, T. Yamadori, M. Matsushita, Y. Baba, T. Kishimoto, T. Kurosaki, and S. Tsukada. 1999. Identification of the SH2 domain binding protein of Bruton' s tyrosine kinase as BLNK-functional significance of Btk-SH2 domain in B-cell antigen receptor-coupled calcium signaling. Blood. 94:2357-2364.
    • (1999) Blood , vol.94 , pp. 2357-2364
    • Hashimoto, S.1    Iwamatsu, A.2    Ishiai, M.3    Okawa, K.4    Yamadori, T.5    Matsushita, M.6    Baba, Y.7    Kishimoto, T.8    Kurosaki, T.9    Tsukada, S.10
  • 38
    • 0032541388 scopus 로고    scopus 로고
    • SLP-65: A new signaling component in B lymphocytes which requires expression of the antigen receptor for phosphorylation
    • Wienands, J., J. Schweikert, B. Wollscheid, H. Jumaa, P. Nielsen, and M. Reth. 1998. SLP-65: a new signaling component in B lymphocytes which requires expression of the antigen receptor for phosphorylation. J. Exp. Med. 188:791-795.
    • (1998) J. Exp. Med , vol.188 , pp. 791-795
    • Wienands, J.1    Schweikert, J.2    Wollscheid, B.3    Jumaa, H.4    Nielsen, P.5    Reth, M.6
  • 40
    • 4444336336 scopus 로고    scopus 로고
    • Tec kinases mediate sustained calcium influx via site-specific tyrosine phosphorylation of the phospholipase Cgamma Src homology 2-Src homology 3 linker
    • Humphries, L.A., C. Dangelmaier, K. Sommer, K. Kipp, R.M. Kato, N. Griffith, I. Bakman, C.W. Turk, J.L. Daniel, and D.J. Rawlings. 2004. Tec kinases mediate sustained calcium influx via site-specific tyrosine phosphorylation of the phospholipase Cgamma Src homology 2-Src homology 3 linker. J. Biol. Chem. 279:37651-37661.
    • (2004) J. Biol. Chem , vol.279 , pp. 37651-37661
    • Humphries, L.A.1    Dangelmaier, C.2    Sommer, K.3    Kipp, K.4    Kato, R.M.5    Griffith, N.6    Bakman, I.7    Turk, C.W.8    Daniel, J.L.9    Rawlings, D.J.10
  • 41
    • 7644232049 scopus 로고    scopus 로고
    • Mechanism of B-cell receptor-induced phosphorylation and activation of phospholipase C-gamma2
    • Kim, Y.J., F. Sekiya, B. Poulin, Y.S. Bae, and S.G. Rhee. 2004. Mechanism of B-cell receptor-induced phosphorylation and activation of phospholipase C-gamma2. Mol. Cell. Biol. 24:9986-9999.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 9986-9999
    • Kim, Y.J.1    Sekiya, F.2    Poulin, B.3    Bae, Y.S.4    Rhee, S.G.5
  • 42
    • 0035914314 scopus 로고    scopus 로고
    • Four tyrosine residues in phospholipase C-gamma 2, identified as Btk-dependent phosphorylation sites, are required for B cell antigen receptor-coupled calcium signaling
    • Watanabe, D., S. Hashimoto, M. Ishiai, M. Matsushita, Y. Baba, T. Kishimoto, T. Kurosaki, and S. Tsukada. 2001. Four tyrosine residues in phospholipase C-gamma 2, identified as Btk-dependent phosphorylation sites, are required for B cell antigen receptor-coupled calcium signaling. J. Biol. Chem. 276:38595-38601.
    • (2001) J. Biol. Chem , vol.276 , pp. 38595-38601
    • Watanabe, D.1    Hashimoto, S.2    Ishiai, M.3    Matsushita, M.4    Baba, Y.5    Kishimoto, T.6    Kurosaki, T.7    Tsukada, S.8
  • 43
    • 0031007450 scopus 로고    scopus 로고
    • Genetic evidence for involvement of type 1, type 2 and type 3 inositol 1,4,5-trisphosphate receptors in signal transduction through the B-cell antigen receptor
    • Sugawara, H., M. Kurosaki, M. Takata, and T. Kurosaki. 1997. Genetic evidence for involvement of type 1, type 2 and type 3 inositol 1,4,5-trisphosphate receptors in signal transduction through the B-cell antigen receptor. EMBO J. 16:3078-3088.
    • (1997) EMBO J , vol.16 , pp. 3078-3088
    • Sugawara, H.1    Kurosaki, M.2    Takata, M.3    Kurosaki, T.4
  • 44
    • 0037148505 scopus 로고    scopus 로고
    • Vav3 modulates B cell receptor responses by regulating phosphoinositide 3-kinase activation
    • Inabe, K., M. Ishiai, A. Scharenberg, N. Freshney, J. Downward, and T. Kurosaki. 2002. Vav3 modulates B cell receptor responses by regulating phosphoinositide 3-kinase activation. J. Exp. Med. 195:189-200.
    • (2002) J. Exp. Med , vol.195 , pp. 189-200
    • Inabe, K.1    Ishiai, M.2    Scharenberg, A.3    Freshney, N.4    Downward, J.5    Kurosaki, T.6
  • 47
    • 27944479854 scopus 로고    scopus 로고
    • Rho GTPases: Biochemistry and biology
    • Jaffe, A.B., and A. Hall. 2005. Rho GTPases: biochemistry and biology. Annu. Rev. Cell Dev. Biol. 21:247-269.
    • (2005) Annu. Rev. Cell Dev. Biol , vol.21 , pp. 247-269
    • Jaffe, A.B.1    Hall, A.2
  • 48
    • 0028180858 scopus 로고
    • Tyrosine kinases Lyn and Syk regulate B cell receptor-coupled Ca2+ mobilization through distinct pathways
    • Takata, M., H. Sabe, A. Hata, T. Inazu, Y. Homma, T. Nukada, H. Yamamura, and T. Kurosaki. 1994. Tyrosine kinases Lyn and Syk regulate B cell receptor-coupled Ca2+ mobilization through distinct pathways. EMBO J. 13:1341-1349.
    • (1994) EMBO J , vol.13 , pp. 1341-1349
    • Takata, M.1    Sabe, H.2    Hata, A.3    Inazu, T.4    Homma, Y.5    Nukada, T.6    Yamamura, H.7    Kurosaki, T.8
  • 49
    • 0029786988 scopus 로고    scopus 로고
    • Knockouts of Src-family kinases: Stiffbones, wimpy T cells, and bad memories
    • Lowell, C.A., and P. Soriano. 1996. Knockouts of Src-family kinases: stiffbones, wimpy T cells, and bad memories. Genes Dev. 10:1845-1857.
    • (1996) Genes Dev , vol.10 , pp. 1845-1857
    • Lowell, C.A.1    Soriano, P.2
  • 50
    • 0028597993 scopus 로고
    • Signaling through CD19 activates Vav/mitogen-activated protein kinase pathway and induces formation of a CD19/Vav/phosphatidylinositol 3-kinase complex in human B cell precursors
    • Weng, W.K., L. Jarvis, and T.W. LeBien. 1994. Signaling through CD19 activates Vav/mitogen-activated protein kinase pathway and induces formation of a CD19/Vav/phosphatidylinositol 3-kinase complex in human B cell precursors. J. Biol. Chem. 269:32514-32521.
    • (1994) J. Biol. Chem , vol.269 , pp. 32514-32521
    • Weng, W.K.1    Jarvis, L.2    LeBien, T.W.3
  • 51
    • 12844271053 scopus 로고    scopus 로고
    • The adaptor protein 3BP2 associates with VAV guanine nucleotide exchange factors to regulate NFAT activation by the B-cell antigen receptor
    • Foucault, I., S. Le Bras, C. Charvet, C. Moon, A. Altman, and M. Deckert. 2005. The adaptor protein 3BP2 associates with VAV guanine nucleotide exchange factors to regulate NFAT activation by the B-cell antigen receptor. Blood. 105:1106-1113.
    • (2005) Blood , vol.105 , pp. 1106-1113
    • Foucault, I.1    Le Bras, S.2    Charvet, C.3    Moon, C.4    Altman, A.5    Deckert, M.6
  • 52
    • 33745825204 scopus 로고    scopus 로고
    • 3BP2 deficiency impairs the response of B cells, but not T cells, to antigen receptor ligation
    • de la Fuente, M.A., L. Kumar, B. Lu, and R.S. Geha. 2006. 3BP2 deficiency impairs the response of B cells, but not T cells, to antigen receptor ligation. Mol. Cell. Biol. 26:5214-5225.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 5214-5225
    • de la Fuente, M.A.1    Kumar, L.2    Lu, B.3    Geha, R.S.4
  • 54
    • 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., 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 (PtdIns-3,4,5-P3)/Tec kinase-dependent calcium signaling pathway: a target for SHIP-mediated inhibitory signals. EMBO J. 17:1961-1972.
    • (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    Gout, I.7    Cantley, L.C.8    Rawlings, D.J.9    Kinet, J.P.10
  • 55
    • 0032518666 scopus 로고    scopus 로고
    • Activation of phospholipase C gamma by PI 3-kinase-induced PH domain-mediated membrane targeting
    • Falasca, M., S. Logan, V. Lehto, G. Baccante, M. Lemmon, and J. Schlessinger. 1998. Activation of phospholipase C gamma by PI 3-kinase-induced PH domain-mediated membrane targeting. EMBO J. 17:414-422.
    • (1998) EMBO J , vol.17 , pp. 414-422
    • Falasca, M.1    Logan, S.2    Lehto, V.3    Baccante, G.4    Lemmon, M.5    Schlessinger, J.6
  • 56
    • 0032055485 scopus 로고    scopus 로고
    • SHIP modulates immune receptor responses by regulating membrane association of Btk
    • Bolland, S., R. Pearse, T. Kurosaki, and J. Ravetch. 1998. SHIP modulates immune receptor responses by regulating membrane association of Btk. Immunity. 8:509-516.
    • (1998) Immunity , vol.8 , pp. 509-516
    • Bolland, S.1    Pearse, R.2    Kurosaki, T.3    Ravetch, J.4
  • 57
    • 0035075507 scopus 로고    scopus 로고
    • Dynamic actin polymerization drives T cell receptor-induced spreading: A role for the signal transduction adaptor LAT
    • Bunnell, S.C., V. Kapoor, R.P. Trible, W. Zhang, and L.E. Samelson. 2001. Dynamic actin polymerization drives T cell receptor-induced spreading: a role for the signal transduction adaptor LAT. Immunity. 14:315-329.
    • (2001) Immunity , vol.14 , pp. 315-329
    • Bunnell, S.C.1    Kapoor, V.2    Trible, R.P.3    Zhang, W.4    Samelson, L.E.5
  • 58
    • 0347593996 scopus 로고    scopus 로고
    • Requirement for Ras guanine nucleotide releasing protein 3 in coupling phospholipase C-γ2 to Ras in B cell receptor signaling
    • Oh-hora, M., S. Johmura, A. Hashimoto, M. Hikida, and T. Kurosaki. 2003. Requirement for Ras guanine nucleotide releasing protein 3 in coupling phospholipase C-γ2 to Ras in B cell receptor signaling. J. Exp. Med. 198:1841-1851.
    • (2003) J. Exp. Med , vol.198 , pp. 1841-1851
    • Oh-hora, M.1    Johmura, S.2    Hashimoto, A.3    Hikida, M.4    Kurosaki, T.5
  • 59
    • 28244476478 scopus 로고    scopus 로고
    • RasGRP1 and RasGRP3 regulate B cell proliferation by facilitating B cell receptor-Ras signaling
    • Coughlin, J.J., S.L. Stang, N.A. Dower, and J.C. Stone. 2005. RasGRP1 and RasGRP3 regulate B cell proliferation by facilitating B cell receptor-Ras signaling. J. Immunol. 175:7179-7184.
    • (2005) J. Immunol , vol.175 , pp. 7179-7184
    • Coughlin, J.J.1    Stang, S.L.2    Dower, N.A.3    Stone, J.C.4
  • 60
    • 0026044059 scopus 로고
    • A short sequence responsible for both phosphoinositide binding and actin binding activities of cofilin
    • Yonezawa, N., Y. Homma, I. Yahara, H. Sakai, and E. Nishida. 1991. A short sequence responsible for both phosphoinositide binding and actin binding activities of cofilin. J. Biol. Chem. 266:17218-17221.
    • (1991) J. Biol. Chem , vol.266 , pp. 17218-17221
    • Yonezawa, N.1    Homma, Y.2    Yahara, I.3    Sakai, H.4    Nishida, E.5
  • 62
    • 0242384071 scopus 로고    scopus 로고
    • Vav proteins, masters of the world of cytoskeleton organization
    • Hornstein, I., A. Alcover, and S. Katzav. 2004. Vav proteins, masters of the world of cytoskeleton organization. Cell. Signal. 16:1-11.
    • (2004) Cell. Signal , vol.16 , pp. 1-11
    • Hornstein, I.1    Alcover, A.2    Katzav, S.3
  • 65
    • 0035652354 scopus 로고    scopus 로고
    • Exclusion of CD43 from the immunological synapse is mediated by phosphorylation-regulated relocation of the cytoskeletal adaptor moesin
    • Delon, J., K. Kaibuchi, and R. Germain. 2001. Exclusion of CD43 from the immunological synapse is mediated by phosphorylation-regulated relocation of the cytoskeletal adaptor moesin. Immunity. 15:691-701.
    • (2001) Immunity , vol.15 , pp. 691-701
    • Delon, J.1    Kaibuchi, K.2    Germain, R.3
  • 66
    • 33744494534 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of B cell lipid rafts reveals that ezrin regulates antigen receptor-mediated lipid raft dynamics
    • Gupta, N., B. Wollscheid, J. Watts, B. Scheer, R. Aebersold, and A. DeFranco. 2006. Quantitative proteomic analysis of B cell lipid rafts reveals that ezrin regulates antigen receptor-mediated lipid raft dynamics. Nat. Immunol. 7:625-633.
    • (2006) Nat. Immunol , vol.7 , pp. 625-633
    • Gupta, N.1    Wollscheid, B.2    Watts, J.3    Scheer, B.4    Aebersold, R.5    DeFranco, A.6
  • 68
    • 4043060068 scopus 로고    scopus 로고
    • Syk-mediated tyrosine phosphorylation is required for the association of hematopoietic lineage cell-specific protein 1 with lipid rafts and B cell antigen receptor signalosome complex
    • Hao, J.J., G.B. Carey, and X. Zhan. 2004. Syk-mediated tyrosine phosphorylation is required for the association of hematopoietic lineage cell-specific protein 1 with lipid rafts and B cell antigen receptor signalosome complex. J. Biol. Chem. 279:33413-33420.
    • (2004) J. Biol. Chem , vol.279 , pp. 33413-33420
    • Hao, J.J.1    Carey, G.B.2    Zhan, X.3
  • 70
    • 33644506455 scopus 로고    scopus 로고
    • Recruitment and activation of PLCgamma1 in T cells: A new insight into old domains
    • Braiman, A., M. Barda-Saad, C. Sommers, and L. Samelson. 2006. Recruitment and activation of PLCgamma1 in T cells: a new insight into old domains. EMBO J. 25:774-784.
    • (2006) EMBO J , vol.25 , pp. 774-784
    • Braiman, A.1    Barda-Saad, M.2    Sommers, C.3    Samelson, L.4
  • 72
    • 0037029653 scopus 로고    scopus 로고
    • Vav1 transduces T cell receptor signals to the activation of phospholipase C-γ1 via phosphoinositide 3-kinase-dependent and-independent pathways
    • Reynolds, L.F., L.A. Smyth, T. Norton, N. Freshney, J. Downward, D. Kioussis, and V.L. Tybulewicz. 2002. Vav1 transduces T cell receptor signals to the activation of phospholipase C-γ1 via phosphoinositide 3-kinase-dependent and-independent pathways. J. Exp. Med. 195:1103-1114.
    • (2002) J. Exp. Med , vol.195 , pp. 1103-1114
    • Reynolds, L.F.1    Smyth, L.A.2    Norton, T.3    Freshney, N.4    Downward, J.5    Kioussis, D.6    Tybulewicz, V.L.7
  • 73
    • 0034097043 scopus 로고    scopus 로고
    • Regulation of B lymphocyte responses to foreign and self-antigens by the CD19/CD21 complex
    • Fearon, D.T., and M.C. Carroll. 2000. Regulation of B lymphocyte responses to foreign and self-antigens by the CD19/CD21 complex. Annu. Rev. Immunol. 18:393-422.
    • (2000) Annu. Rev. Immunol , vol.18 , pp. 393-422
    • Fearon, D.T.1    Carroll, M.C.2
  • 74
    • 0032076954 scopus 로고    scopus 로고
    • CD19 as a membrane-anchored adaptor protein of B lymphocytes: Costimulation of lipid and protein kinases by recruitment of Vav
    • O'Rourke, L.M., R. Tooze, M. Turner, D.M. Sandoval, R.H. Carter, V.L. Tybulewicz, and D.T. Fearon. 1998. CD19 as a membrane-anchored adaptor protein of B lymphocytes: costimulation of lipid and protein kinases by recruitment of Vav. Immunity. 8:635-645.
    • (1998) Immunity , vol.8 , pp. 635-645
    • O'Rourke, L.M.1    Tooze, R.2    Turner, M.3    Sandoval, D.M.4    Carter, R.H.5    Tybulewicz, V.L.6    Fearon, D.T.7
  • 75
    • 2942627439 scopus 로고    scopus 로고
    • Binding of cytoplasmic proteins to the CD19 intracellular domain is high affinity, competitive, and multimeric
    • Brooks, S.R., P.M. Kirkham, L. Freeberg, and R.H. Carter. 2004. Binding of cytoplasmic proteins to the CD19 intracellular domain is high affinity, competitive, and multimeric. J. Immunol. 172:7556-7564.
    • (2004) J. Immunol , vol.172 , pp. 7556-7564
    • Brooks, S.R.1    Kirkham, P.M.2    Freeberg, L.3    Carter, R.H.4
  • 76
    • 0033997322 scopus 로고    scopus 로고
    • The role of membrane-associated adaptors in T cell receptor signalling
    • Zhang, W., and L. Samelson. 2000. The role of membrane-associated adaptors in T cell receptor signalling. Semin. Immunol. 12:35-41.
    • (2000) Semin. Immunol , vol.12 , pp. 35-41
    • Zhang, W.1    Samelson, L.2
  • 78
    • 0030818183 scopus 로고    scopus 로고
    • B lymphocyte-specific, Cre-mediated mutagenesis in mice
    • Rickert, R.C., J. Roes, and K. Rajewsky. 1997. B lymphocyte-specific, Cre-mediated mutagenesis in mice. Nucleic Acids Res. 25:1317-1318.
    • (1997) Nucleic Acids Res , vol.25 , pp. 1317-1318
    • Rickert, R.C.1    Roes, J.2    Rajewsky, K.3
  • 79
    • 2442467885 scopus 로고    scopus 로고
    • LFA-1/ICAM-1 interaction lowers the threshold of B cell activation by facilitating B cell adhesion and synapse formation
    • Carrasco, Y.R., S.J. Fleire, T. Cameron, M.L. Dustin, and F.D. Batista. 2004. LFA-1/ICAM-1 interaction lowers the threshold of B cell activation by facilitating B cell adhesion and synapse formation. Immunity. 20:589-599.
    • (2004) Immunity , vol.20 , pp. 589-599
    • Carrasco, Y.R.1    Fleire, S.J.2    Cameron, T.3    Dustin, M.L.4    Batista, F.D.5
  • 80
    • 0031577470 scopus 로고    scopus 로고
    • A transgenic mouse line that retains Cre recombinase activity in mature oocytes irrespective of the cre transgene transmission
    • Sakai, K., and J. Miyazaki. 1997. A transgenic mouse line that retains Cre recombinase activity in mature oocytes irrespective of the cre transgene transmission. Biochem. Biophys. Res. Commun. 237:318-324.
    • (1997) Biochem. Biophys. Res. Commun , vol.237 , pp. 318-324
    • Sakai, K.1    Miyazaki, J.2
  • 81
    • 0030972162 scopus 로고    scopus 로고
    • Immunogenicity of a contiguous T-B synthetic epitope of the A/PR/8/34 influenza virus
    • Brumeanu, T.D., S. Casares, A. Bot, S. Bot, and C.A. Bona. 1997. Immunogenicity of a contiguous T-B synthetic epitope of the A/PR/8/34 influenza virus. J. Virol. 71:5473-5480.
    • (1997) J. Virol , vol.71 , pp. 5473-5480
    • Brumeanu, T.D.1    Casares, S.2    Bot, A.3    Bot, S.4    Bona, C.A.5
  • 82
    • 0020379096 scopus 로고
    • Evidence for an IgD homologue on chicken lymphocytes
    • Chen, C.L., J.E. Lehmeyer, and M.D. Cooper. 1982. Evidence for an IgD homologue on chicken lymphocytes. J. Immunol. 129:2580-2585.
    • (1982) J. Immunol , vol.129 , pp. 2580-2585
    • Chen, C.L.1    Lehmeyer, J.E.2    Cooper, M.D.3


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