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Volumn 184, Issue 7, 2010, Pages 3665-3676

Swiprosin-1/EFhd2 controls B cell receptor signaling through the assembly of the B cell receptor, Syk, and phospholipase C γ2 in membrane rafts

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; B LYMPHOCYTE RECEPTOR; CELL PROTEIN; MEMBRANE PROTEIN; PHOSPHOLIPASE C GAMMA2; PROTEIN KINASE LYN; PROTEIN KINASE SYK; PROTEIN TYROSINE KINASE; SCAFFOLD PROTEIN; SWIPROSIN 1; UNCLASSIFIED DRUG; LYMPHOCYTE ANTIGEN RECEPTOR; PHOSPHOLIPASE C GAMMA; SIGNAL PEPTIDE; SIGNAL TRANSDUCING ADAPTOR PROTEIN; SWIPROSIN 1 PROTEIN, MOUSE; SWIPROSIN-1 PROTEIN, MOUSE;

EID: 77951648119     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.0903642     Document Type: Article
Times cited : (50)

References (78)
  • 1
    • 0036639318 scopus 로고    scopus 로고
    • To make antibodies or not: Signaling by the B-cell antigen receptor
    • Gold, M. R. 2002. To make antibodies or not: signaling by the B-cell antigen receptor. Trends Pharmacol. Sci. 23: 316-324.
    • (2002) Trends Pharmacol. Sci. , vol.23 , pp. 316-324
    • Gold, M.R.1
  • 2
    • 0036866477 scopus 로고    scopus 로고
    • Amplification of B cell antigen receptor signaling by a Syk/ITAM positive feedback loop
    • DOI 10.1016/S1097-2765(02)00739-6
    • Rolli, V., M. Gallwitz, T. Wossning, A. Flemming, W. W. Schamel, C. Zürn, and M. Reth. 2002. Amplification of B cell antigen receptor signaling by a Syk/ ITAM positive feedback loop. Mol. Cell 10: 1057-1069. (Pubitemid 36001972)
    • (2002) Molecular Cell , vol.10 , Issue.5 , pp. 1057-1069
    • Rolli, V.1    Gallwitz, M.2    Wossning, T.3    Flemming, A.4    Schamel, W.W.A.5    Zurn, C.6    Reth, M.7
  • 3
    • 0032127159 scopus 로고    scopus 로고
    • BLNK: A central linker protein in B cell activation
    • DOI 10.1016/S1074-7613(00)80591-9
    • Fu, C., C. W. Turck, T. Kurosaki, and A. C. Chan. 1998. BLNK: a central linker protein in B cell activation. Immunity 9: 93-103. (Pubitemid 28361298)
    • (1998) Immunity , vol.9 , Issue.1 , pp. 93-103
    • Fu, C.1    Turck, C.W.2    Kurosaki, T.3    Chan, A.C.4
  • 4
    • 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. J. 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.J.5    Reth, M.6
  • 7
  • 8
    • 27144515996 scopus 로고    scopus 로고
    • STIM1 is a Ca2+ sensor that activates CRAC channels and migrates from the Ca2+ store to the plasma membrane
    • Zhang, S. L., Y. Yu, J. Roos, J. A. Kozak, T. J. Deerinck, M. H. Ellisman, K. A. Stauderman, and M. D. Cahalan. 2005. STIM1 is a Ca2+ sensor that activates CRAC channels and migrates from the Ca2+ store to the plasma membrane. Nature 437: 902-905.
    • (2005) Nature , vol.437 , pp. 902-905
    • Zhang, S.L.1    Yu, Y.2    Roos, J.3    Kozak, J.A.4    Deerinck, T.J.5    Ellisman, M.H.6    Stauderman, K.A.7    Cahalan, M.D.8
  • 9
    • 57849148942 scopus 로고    scopus 로고
    • Calcium signaling in immune cells
    • Vig, M., and J. P. Kinet. 2009. Calcium signaling in immune cells. Nat. Immunol. 10: 21-27.
    • (2009) Nat. Immunol. , vol.10 , pp. 21-27
    • Vig, M.1    Kinet, J.P.2
  • 11
    • 0030888186 scopus 로고    scopus 로고
    • Differential activation of transcription factors induced by Ca2+ response amplitude and duration
    • Dolmetsch, R. E., R. S. Lewis, C. C. Goodnow, and J. I. Healy. 1997. Differential activation of transcription factors induced by Ca2+ response amplitude and duration. Nature 386: 855-858.
    • (1997) Nature , vol.386 , pp. 855-858
    • Dolmetsch, R.E.1    Lewis, R.S.2    Goodnow, C.C.3    Healy, J.I.4
  • 14
    • 43249129993 scopus 로고    scopus 로고
    • The kinase Syk as an adaptor controlling sustained calcium signalling and B-cell development
    • DOI 10.1038/emboj.2008.62, PII EMBOJ200862
    • Kulathu, Y., E. Hobeika, G. Turchinovich, and M. Reth. 2008. The kinase Syk as an adaptor controlling sustained calcium signalling and B-cell development. EMBO J. 27: 1333-1344. (Pubitemid 351655176)
    • (2008) EMBO Journal , vol.27 , Issue.9 , pp. 1333-1344
    • Kulathu, Y.1    Hobeika, E.2    Turchinovich, G.3    Reth, M.4
  • 15
    • 33847240085 scopus 로고    scopus 로고
    • 2+ signaling in B cells
    • DOI 10.1038/sj.emboj.7601557, PII 7601557
    • Stork, B., K. Neumann, I. Goldbeck, S. Alers, T. Kähne, M. Naumann, M. Engelke, and J. Wienands. 2007. Subcellular localization of Grb2 by the adaptor protein Dok-3 restricts the intensity of Ca2+ signaling in B cells. EMBO J. 26: 1140-1149. (Pubitemid 46303581)
    • (2007) EMBO Journal , vol.26 , Issue.4 , pp. 1140-1149
    • Stork, B.1    Neumann, K.2    Goldbeck, I.3    Alers, S.4    Kahne, T.5    Naumann, M.6    Engelke, M.7    Wienands, J.8
  • 16
    • 2542439968 scopus 로고    scopus 로고
    • Activation of the Syk tyrosine kinase is insufficient for downstream signal transduction in B lymphocytes
    • Hsueh, R. C., A. M. Hammill, J. A. Lee, J. W. Uhr, and R. H. Scheuermann. 2002. Activation of the Syk tyrosine kinase is insufficient for downstream signal transduction in B lymphocytes. BMC Immunol. 3: 16.
    • (2002) BMC Immunol. , vol.3 , pp. 16
    • Hsueh, R.C.1    Hammill, A.M.2    Lee, J.A.3    Uhr, J.W.4    Scheuermann, R.H.5
  • 17
    • 61849141064 scopus 로고    scopus 로고
    • Tyrosine kinases and their substrates in B lymphocytes
    • Kurosaki, T., and M. Hikida. 2009. Tyrosine kinases and their substrates in B lymphocytes. Immunol. Rev. 228: 132-148.
    • (2009) Immunol. Rev. , vol.228 , pp. 132-148
    • Kurosaki, T.1    Hikida, M.2
  • 18
    • 1842432039 scopus 로고    scopus 로고
    • Membrane domains in lymphocytes - From lipid rafts to protein scaffolds
    • DOI 10.1111/j.1600-0854.2003.00163.x
    • Harder, T., and K. R. Engelhardt. 2004. Membrane domains in lymphocytes - from lipid rafts to protein scaffolds. Traffic 5: 265-275. (Pubitemid 38455750)
    • (2004) Traffic , vol.5 , Issue.4 , pp. 265-275
    • Harder, T.1    Engelhardt, K.R.2
  • 19
    • 33744476136 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer in living cells reveals dynamic membrane changes in the initiation of B cell signaling
    • Sohn, H. W., P. Tolar, T. Jin, and S. K. Pierce. 2006. Fluorescence resonance energy transfer in living cells reveals dynamic membrane changes in the initiation of B cell signaling. Proc. Natl. Acad. Sci. U.S.A. 103: 8143-8148.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 8143-8148
    • Sohn, H.W.1    Tolar, P.2    Jin, T.3    Pierce, S.K.4
  • 20
    • 0001751245 scopus 로고    scopus 로고
    • A requirement for lipid rafts in B cell receptor induced Ca(2+) flux
    • Aman, M. J., and K. S. Ravichandran. 2000. A requirement for lipid rafts in B cell receptor induced Ca(2+) flux. Curr. Biol. 10: 393-396.
    • (2000) Curr. Biol. , vol.10 , pp. 393-396
    • Aman, M.J.1    Ravichandran, K.S.2
  • 21
    • 14844362909 scopus 로고    scopus 로고
    • Lipid rafts associate with intracellular B cell receptors and exhibit a B cell stage-specific protein composition
    • Mielenz, D., C. Vettermann, M. Hampel, C. Lang, A. Avramidou, M. Karas, and H. M. Jäck. 2005. Lipid rafts associate with intracellular B cell receptors and exhibit a B cell stage-specific protein composition. J. Immunol. 174: 3508-3517. (Pubitemid 40354059)
    • (2005) Journal of Immunology , vol.174 , Issue.6 , pp. 3508-3517
    • Mielenz, D.1    Vettermann, C.2    Hampel, M.3    Lang, C.4    Avramidou, A.5    Karas, M.6    Jack, H.-M.7
  • 22
    • 35548953798 scopus 로고    scopus 로고
    • The novel adaptor protein Swiprosin-1 enhances BCR signals and contributes to BCR-induced apoptosis
    • DOI 10.1038/sj.cdd.4402206, PII 4402206
    • Avramidou, A., C. Kroczek, C. Lang, W. Schuh, H. M. Jäck, and D. Mielenz. 2007. The novel adaptor protein Swiprosin-1 enhances BCR signals and contributes to BCR-induced apoptosis. Cell Death Differ. 14: 1936-1947. (Pubitemid 350011669)
    • (2007) Cell Death and Differentiation , vol.14 , Issue.11 , pp. 1936-1947
    • Avramidou, A.1    Kroczek, C.2    Lang, C.3    Schuh, W.4    Ja5    ck, H.-M.6    Mielenz, D.7
  • 23
    • 40349092941 scopus 로고    scopus 로고
    • Covalent capture of kinase-specific phosphopeptides reveals Cdk1-cyclin B substrates
    • Blethrow, J. D., J. S. Glavy, D. O. Morgan, and K. M. Shokat. 2008. Covalent capture of kinase-specific phosphopeptides reveals Cdk1-cyclin B substrates. Proc. Natl. Acad. Sci. U.S.A. 105: 1442-1447.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 1442-1447
    • Blethrow, J.D.1    Glavy, J.S.2    Morgan, D.O.3    Shokat, K.M.4
  • 26
    • 38649139336 scopus 로고    scopus 로고
    • Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain
    • Ballif, B. A., G. R. Carey, S. R. Sunyaev, and S. P. Gygi. 2008. Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain. J. Proteome Res. 7: 311-318.
    • (2008) J. Proteome Res. , vol.7 , pp. 311-318
    • Ballif, B.A.1    Carey, G.R.2    Sunyaev, S.R.3    Gygi, S.P.4
  • 28
    • 0022620212 scopus 로고
    • Abortive activation of B lymphocytes by monoclonal anti-immunoglobulin antibodies
    • Cambier, J. C., C. H. Heusser, and M. H. Julius. 1986. Abortive activation of B lymphocytes by monoclonal anti-immunoglobulin antibodies. J. Immunol. 136: 3140-3146. (Pubitemid 16113890)
    • (1986) Journal of Immunology , vol.136 , Issue.9 , pp. 3140-3146
    • Cambier, J.C.1    Heusser, C.H.2    Julius, M.H.3
  • 29
    • 0022340978 scopus 로고
    • Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product
    • Evan, G. I., G. K. Lewis, G. Ramsay, and J. M. Bishop. 1985. Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product. Mol. Cell. Biol. 5: 3610-3616.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 3610-3616
    • Evan, G.I.1    Lewis, G.K.2    Ramsay, G.3    Bishop, J.M.4
  • 30
    • 0019451918 scopus 로고
    • The regulation of growth and differentiation of a murine B cell lymphoma. II. The inhibition of WEHI 231 by anti-immunoglobulin antibodies
    • Boyd, A. W., and J. W. Schrader. 1981. The regulation of growth and differentiation of a murine B cell lymphoma. II. The inhibition of WEHI 231 by anti-immunoglobulin antibodies. J. Immunol. 126: 2466-2469.
    • (1981) J. Immunol. , vol.126 , pp. 2466-2469
    • Boyd, A.W.1    Schrader, J.W.2
  • 31
    • 0022496821 scopus 로고
    • Membrane IgM, IgD, and IgG act as signal transmission molecules in a series of B lymphomas
    • Mizuguchi, J., W. Tsang, S. L. Morrison, M. A. Beaven, and W. E. Paul. 1986. Membrane IgM, IgD, and IgG act as signal transmission molecules in a series of B lymphomas. J. Immunol. 137: 2162-2167. (Pubitemid 16020706)
    • (1986) Journal of Immunology , vol.137 , Issue.7 , pp. 2162-2167
    • Mizuguchi, J.1    Tsang, W.2    Morrison, L.3
  • 32
    • 0022911057 scopus 로고
    • Use of the CH lymphomas as models of murine B cell differentiation
    • Bishop, G. A., and G. Haughton. 1986. Use of the CH lymphomas as models of murine B cell differentiation. Immunol. Res. 5: 263-270.
    • (1986) Immunol. Res. , vol.5 , pp. 263-270
    • Bishop, G.A.1    Haughton, G.2
  • 33
    • 7244227849 scopus 로고    scopus 로고
    • IL-7 does not prevent pro-B/ pre-B cell maturation to the immature/sIgM(+) stage
    • Milne, C. D., H. E. Fleming, and C. J. Paige. 2004. IL-7 does not prevent pro-B/ pre-B cell maturation to the immature/sIgM(+) stage. Eur. J. Immunol. 34: 2647-2655.
    • (2004) Eur. J. Immunol. , vol.34 , pp. 2647-2655
    • Milne, C.D.1    Fleming, H.E.2    Paige, C.J.3
  • 34
    • 0032532563 scopus 로고    scopus 로고
    • The germinal center kinase (GCK)-related protein kinases HPK1 and KHS are candidates for highly selective signal transducers of Crk family adapter proteins
    • Oehrl, W., C. Kardinal, S. Ruf, K. Adermann, J. Groffen, G. S. Feng, J. Blenis, T. H. Tan, and S. M. Feller. 1998. The germinal center kinase (GCK)-related protein kinases HPK1 and KHS are candidates for highly selective signal transducers of Crk family adapter proteins. Oncogene 17: 1893-1901. (Pubitemid 28488457)
    • (1998) Oncogene , vol.17 , Issue.15 , pp. 1893-1901
    • Oehrl, W.1    Kardinal, C.2    Ruf, S.3    Adermann, K.4    Groffen, J.5    Feng, G.-S.6    Blenis, J.7    Tan, T.-H.8    Feller, S.M.9
  • 35
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 36
    • 0028060150 scopus 로고
    • Temporal differences in the activation of three classes of non-transmembrane protein tyrosine kinases following B-cell antigen receptor surface engagement
    • Saouaf, S. J., S. Mahajan, R. B. Rowley, S. A. Kut, J. Fargnoli, A. L. Burkhardt, S. Tsukada, O. N. Witte, and J. B. Bolen. 1994. Temporal differences in the activation of three classes of non-transmembrane protein tyrosine kinases following B-cell antigen receptor surface engagement. Proc. Natl. Acad. Sci. U.S.A. 91: 9524-9528.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 9524-9528
    • Saouaf, S.J.1    Mahajan, S.2    Rowley, R.B.3    Kut, S.A.4    Fargnoli, J.5    Burkhardt, A.L.6    Tsukada, S.7    Witte, O.N.8    Bolen, J.B.9
  • 37
    • 67649494454 scopus 로고    scopus 로고
    • The novel Syk inhibitor R406 reveals mechanistic differences in the initiation of GPVI and CLEC-2 signaling in platelets
    • Spalton, J. C., J. Mori, A. Y. Pollitt, C. E. Hughes, J. A. Eble, and S. P. Watson. 2009. The novel Syk inhibitor R406 reveals mechanistic differences in the initiation of GPVI and CLEC-2 signaling in platelets. J. Thromb. Haemost. 7: 1192-1199.
    • (2009) J. Thromb. Haemost. , vol.7 , pp. 1192-1199
    • Spalton, J.C.1    Mori, J.2    Pollitt, A.Y.3    Hughes, C.E.4    Eble, J.A.5    Watson, S.P.6
  • 38
    • 0042834298 scopus 로고    scopus 로고
    • Immunoglobulin μ heavy chains do not mediate tyrosine phosphorylation of Igα from the ER-cis-Golgi
    • Mielenz, D., A. Ruschel, C. Vettermann, and H. M. Jäck. 2003. Immunoglobulin mu heavy chains do not mediate tyrosine phosphorylation of Ig alpha from the ER-cis-Golgi. J. Immunol. 171: 3091-3101. (Pubitemid 37093532)
    • (2003) Journal of Immunology , vol.171 , Issue.6 , pp. 3091-3101
    • Mielenz, D.1    Ruschel, A.2    Vettermann, C.3    Jack, H.-M.4
  • 39
    • 56249131085 scopus 로고    scopus 로고
    • Kinetic assay for characterization of spleen tyrosine kinase activity and inhibition with recombinant kinase and crude cell lysates
    • Li, M., P. Luraghi, A. Amour, X. D. Qian, P. S. Carter, C. J. Clark, A. Deakin, J. Denyer, C. I. Hobbs, M. Surby, et al. 2009. Kinetic assay for characterization of spleen tyrosine kinase activity and inhibition with recombinant kinase and crude cell lysates. Anal. Biochem. 384: 56-67.
    • (2009) Anal. Biochem. , vol.384 , pp. 56-67
    • Li, M.1    Luraghi, P.2    Amour, A.3    Qian, X.D.4    Carter, P.S.5    Clark, C.J.6    Deakin, A.7    Denyer, J.8    Hobbs, C.I.9    Surby, M.10
  • 40
    • 18844424394 scopus 로고    scopus 로고
    • The role of CD22 and other inhibitory co-receptors in B-cell activation
    • Nitschke, L. 2005. The role of CD22 and other inhibitory co-receptors in B-cell activation. Curr. Opin. Immunol. 17: 290-297.
    • (2005) Curr. Opin. Immunol. , vol.17 , pp. 290-297
    • Nitschke, L.1
  • 41
    • 0037013743 scopus 로고    scopus 로고
    • Interaction sites on human IgG-Fc for FcgammaR: Current models
    • Jefferis, R., and J. Lund. 2002. Interaction sites on human IgG-Fc for FcgammaR: current models. Immunol. Lett. 82: 57-65.
    • (2002) Immunol. Lett. , vol.82 , pp. 57-65
    • Jefferis, R.1    Lund, J.2
  • 42
    • 0025666553 scopus 로고
    • Molecular definition of interaction sites on human IgG for Fc receptors (huFc gamma R)
    • Jefferis, R., J. Lund, and J. Pound. 1990. Molecular definition of interaction sites on human IgG for Fc receptors (huFc gamma R). Mol. Immunol. 27: 1237-1240.
    • (1990) Mol. Immunol. , vol.27 , pp. 1237-1240
    • Jefferis, R.1    Lund, J.2    Pound, J.3
  • 43
    • 0025975844 scopus 로고
    • The role of tyrosine phosphorylation in signal transduction through surface Ig in human B cells. Inhibition of tyrosine phosphorylation prevents intracellular calcium release
    • Lane, P. J., J. A. Ledbetter, F. M. McConnell, K. Draves, J. Deans, G. L. Schieven, and E. A. Clark. 1991. The role of tyrosine phosphorylation in signal transduction through surface Ig in human B cells. Inhibition of tyrosine phosphorylation prevents intracellular calcium release. J. Immunol. 146: 715-722.
    • (1991) J. Immunol. , vol.146 , pp. 715-722
    • Lane, P.J.1    Ledbetter, J.A.2    McConnell, F.M.3    Draves, K.4    Deans, J.5    Schieven, G.L.6    Clark, E.A.7
  • 44
    • 0028180858 scopus 로고
    • Tyrosine kinase 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. (Pubitemid 2046442)
    • (1994) EMBO Journal , vol.13 , Issue.6 , 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
  • 46
    • 0024238959 scopus 로고
    • Generation of an active protein-tyrosine kinase from lymphocytes by proteolysis
    • Zioncheck, T. F., M. L. Harrison, C. C. Isaacson, and R. L. Geahlen. 1988. Generation of an active protein-tyrosine kinase from lymphocytes by proteolysis. J. Biol. Chem. 263: 19195-19202.
    • (1988) J. Biol. Chem. , vol.263 , pp. 19195-19202
    • Zioncheck, T.F.1    Harrison, M.L.2    Isaacson, C.C.3    Geahlen, R.L.4
  • 48
    • 8844222731 scopus 로고    scopus 로고
    • A novel Syk kinase-selective inhibitor blocks antigen presentation of immune complexes in dendritic cells
    • Nakashima, K., T. Kokubo, M. Shichijo, Y. F. Li, T. Yura, and N. Yamamoto. 2004. A novel Syk kinase-selective inhibitor blocks antigen presentation of immune complexes in dendritic cells. Eur. J. Pharmacol. 505: 223-228.
    • (2004) Eur. J. Pharmacol. , vol.505 , pp. 223-228
    • Nakashima, K.1    Kokubo, T.2    Shichijo, M.3    Li, Y.F.4    Yura, T.5    Yamamoto, N.6
  • 49
    • 0033033321 scopus 로고    scopus 로고
    • Clusters of glycolipid and glycosylphosphatidylinositol- anchored proteins in lymphoid cells: Accumulation of actin regulated by local tyrosine phosphorylation
    • Harder, T., and K. Simons. 1999. Clusters of glycolipid and glycosylphosphatidylinositol- anchored proteins in lymphoid cells: accumulation of actin regulated by local tyrosine phosphorylation. Eur. J. Immunol. 29: 556-562.
    • (1999) Eur. J. Immunol. , vol.29 , pp. 556-562
    • Harder, T.1    Simons, K.2
  • 51
    • 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. D. Watts, B. Scheer, R. Aebersold, and A. L. 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.D.3    Scheer, B.4    Aebersold, R.5    DeFranco, A.L.6
  • 52
    • 63649139510 scopus 로고    scopus 로고
    • Comparative proteomics analysis of caspase-9-protein complexes in untreated and cytochrome c/dATP stimulated lysates of NSCLC cells
    • Checińska, A., G. Giaccone, J. A. Rodriguez, F. A. Kruyt, and C. R. Jimenez. 2009. Comparative proteomics analysis of caspase-9-protein complexes in untreated and cytochrome c/dATP stimulated lysates of NSCLC cells. J. Proteomics 72: 575-585.
    • (2009) J. Proteomics , vol.72 , pp. 575-585
    • Checińska, A.1    Giaccone, G.2    Rodriguez, J.A.3    Kruyt, F.A.4    Jimenez, C.R.5
  • 53
    • 29144495943 scopus 로고    scopus 로고
    • Compositional characterization of the cytoskeleton of NK-like cells
    • DOI 10.1021/pr0502121
    • Meng, X., and J. A. Wilkins. 2005. Compositional characterization of the cytoskeleton of NK-like cells. J. Proteome Res. 4: 2081-2087. (Pubitemid 41814274)
    • (2005) Journal of Proteome Research , vol.4 , Issue.6 , pp. 2081-2087
    • Meng, X.1    Wilkins, J.A.2
  • 54
    • 67651229135 scopus 로고    scopus 로고
    • Large-scale proteomic analysis of tyrosine-phosphorylation induced by T-cell receptor or B-cell receptor activation reveals new signaling pathways
    • Matsumoto, M., K. Oyamada, H. Takahashi, T. Sato, S. Hatakeyama, and K. I. Nakayama. 2009. Large-scale proteomic analysis of tyrosine-phosphorylation induced by T-cell receptor or B-cell receptor activation reveals new signaling pathways. Proteomics 9: 3549-3563.
    • (2009) Proteomics , vol.9 , pp. 3549-3563
    • Matsumoto, M.1    Oyamada, K.2    Takahashi, H.3    Sato, T.4    Hatakeyama, S.5    Nakayama, K.I.6
  • 55
    • 0033852012 scopus 로고    scopus 로고
    • Syk-dependent phosphorylation of microtubules in activated B-lymphocytes
    • Faruki, S., R. L. Geahlen, and D. J. Asai. 2000. Syk-dependent phosphorylation of microtubules in activated B-lymphocytes. J. Cell Sci. 113: 2557-2565. (Pubitemid 30601377)
    • (2000) Journal of Cell Science , vol.113 , Issue.14 , pp. 2557-2565
    • Faruki, S.1    Geahlen, R.L.2    Asai, D.J.3
  • 56
    • 33744913799 scopus 로고    scopus 로고
    • Regulation of microtubule formation in activated mast cells by complexes of γ-tubulin with Fyn and Syk kinases
    • Sulimenko, V., E. Dráberová, T. Sulimenko, L. Macurek, V. Richterová, P. Dráber, and P. Dráber. 2006. Regulation of microtubule formation in activated mast cells by complexes of gamma-tubulin with Fyn and Syk kinases. J. Immunol. 176: 7243-7253. (Pubitemid 43849024)
    • (2006) Journal of Immunology , vol.176 , Issue.12 , pp. 7243-7253
    • Sulimenko, V.1    Draberova, E.2    Sulimenko, T.3    Macurek, L.4    Richterova, V.5    Draber, P.6    Draber, P.7
  • 57
    • 0037054546 scopus 로고    scopus 로고
    • Phospholipids undergo hop diffusion in compartmentalized cell membrane
    • DOI 10.1083/jcb.200202050
    • Fujiwara, T., K. Ritchie, H. Murakoshi, K. Jacobson, and A. Kusumi. 2002. Phospholipids undergo hop diffusion in compartmentalized cell membrane. J. Cell Biol. 157: 1071-1081. (Pubitemid 34839781)
    • (2002) Journal of Cell Biology , vol.157 , Issue.6 , pp. 1071-1081
    • Fujiwara, T.1    Ritchie, K.2    Murakoshi, H.3    Jacobson, K.4    Kusumi, A.5
  • 58
    • 18244397166 scopus 로고    scopus 로고
    • Actin depolymerization transduces the strength of B-cell receptor stimulation
    • Hao, S., and A. August. 2005. Actin depolymerization transduces the strength of B-cell receptor stimulation. Mol. Biol. Cell 16: 2275-2284.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2275-2284
    • Hao, S.1    August, A.2
  • 59
    • 42249090333 scopus 로고    scopus 로고
    • Phospholipase C-gamma2 and Vav cooperate within signaling microclusters to propagate B cell spreading in response to membrane-bound antigen
    • Weber, M., B. Treanor, D. Depoil, H. Shinohara, N. E. Harwood, M. Hikida, T. Kurosaki, and F. D. Batista. 2008. Phospholipase C-gamma2 and Vav cooperate within signaling microclusters to propagate B cell spreading in response to membrane-bound antigen. J. Exp. Med. 205: 853-868.
    • (2008) J. Exp. Med. , vol.205 , pp. 853-868
    • Weber, M.1    Treanor, B.2    Depoil, D.3    Shinohara, H.4    Harwood, N.E.5    Hikida, M.6    Kurosaki, T.7    Batista, F.D.8
  • 60
    • 44649160533 scopus 로고    scopus 로고
    • Have we become overly reliant on lipid rafts? Talking Point on the involvement of lipid rafts in T-cell activation
    • DOI 10.1038/embor.2008.92, PII EMBOR200892
    • Kenworthy, A. K. 2008. Have we become overly reliant on lipid rafts? Talking Point on the involvement of lipid rafts in T-cell activation. EMBO Rep. 9: 531-535. (Pubitemid 351772915)
    • (2008) EMBO Reports , vol.9 , Issue.6 , pp. 531-535
    • Kenworthy, A.K.1
  • 61
    • 0028151351 scopus 로고
    • Interactions between saturated acyl chains confer detergent resistance on lipids and glycosylphosphatidylinositol (GPI)-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behavior
    • Schroeder, R., E. London, and D. Brown. 1994. Interactions between saturated acyl chains confer detergent resistance on lipids and glycosylphosphatidylinositol (GPI)-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behavior. Proc. Natl. Acad. Sci. U.S.A. 91: 12130-12134.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 12130-12134
    • Schroeder, R.1    London, E.2    Brown, D.3
  • 62
    • 0036238473 scopus 로고    scopus 로고
    • SH3-dependent stimulation of Src-family kinase autophosphorylation without tail release from the SH2 domain in vivo
    • Lerner, E. C., and T. E. Smithgall. 2002. SH3-dependent stimulation of Src-family kinase autophosphorylation without tail release from the SH2 domain in vivo. Nat. Struct. Biol. 9: 365-369.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 365-369
    • Lerner, E.C.1    Smithgall, T.E.2
  • 63
    • 24044540256 scopus 로고    scopus 로고
    • Specificity and versatility of SH3 and other proline-recognition domains: Structural basis and implications for cellular signal transduction
    • Li, S. S. 2005. Specificity and versatility of SH3 and other proline-recognition domains: structural basis and implications for cellular signal transduction. Biochem. J. 390: 641-653.
    • (2005) Biochem. J. , vol.390 , pp. 641-653
    • Li, S.S.1
  • 64
    • 0035887778 scopus 로고    scopus 로고
    • Unique signaling properties of B cell antigen receptor in mature and immature B cells: Implications for tolerance and activation
    • Benschop, R. J., E. Brandl, A. C. Chan, and J. C. Cambier. 2001. Unique signaling properties of B cell antigen receptor in mature and immature B cells: implications for tolerance and activation. J. Immunol. 167: 4172-4179.
    • (2001) J. Immunol. , vol.167 , pp. 4172-4179
    • Benschop, R.J.1    Brandl, E.2    Chan, A.C.3    Cambier, J.C.4
  • 66
    • 0028896269 scopus 로고
    • Immature B lymphocytes are deficient in expression of the src-family kinases p59fyn and p55fgr1
    • Wechsler, R. J., and J. G. Monroe. 1995. Immature B lymphocytes are deficient in expression of the src-family kinases p59fyn and p55fgr1. J. Immunol. 154: 1919-1929.
    • (1995) J. Immunol. , vol.154 , pp. 1919-1929
    • Wechsler, R.J.1    Monroe, J.G.2
  • 67
    • 0028954463 scopus 로고
    • The proto-oncogene c-fgr is expressed in normal mantle zone B lymphocytes and is developmentally regulated during myelomonocytic differentiation in vivo
    • Link, D. C., and M. Zutter. 1995. The proto-oncogene c-fgr is expressed in normal mantle zone B lymphocytes and is developmentally regulated during myelomonocytic differentiation in vivo. Blood 85: 472-479.
    • (1995) Blood , vol.85 , pp. 472-479
    • Link, D.C.1    Zutter, M.2
  • 68
    • 0036952736 scopus 로고    scopus 로고
    • Cyclin-dependent kinase-1: Linking apoptosis to cell cycle and mitotic catastrophe
    • DOI 10.1038/sj.cdd.4401130
    • Castedo, M., J. L. Perfettini, T. Roumier, and G. Kroemer. 2002. Cyclin-dependent kinase-1: linking apoptosis to cell cycle and mitotic catastrophe. Cell Death Differ. 9: 1287-1293. (Pubitemid 36097698)
    • (2002) Cell Death and Differentiation , vol.9 , Issue.12 , pp. 1287-1293
    • Castedo, M.1    Perfettini, J.-L.2    Roumier, T.3    Kroemer, G.4
  • 69
    • 0033876133 scopus 로고    scopus 로고
    • Expression of cdc2 and cyclin B1 in Helicobacter pylori-associated gastric MALT and MALT lymphoma: Relationship to cell death, proliferation, and transformation
    • Banerjee, S. K., A. P. Weston, M. N. Zoubine, D. R. Campbell, and R. Cherian. 2000. Expression of cdc2 and cyclin B1 in Helicobacter pylori-associated gastric MALT and MALT lymphoma : relationship to cell death, proliferation, and transformation. Am. J. Pathol. 156: 217-225.
    • (2000) Am. J. Pathol. , vol.156 , pp. 217-225
    • Banerjee, S.K.1    Weston, A.P.2    Zoubine, M.N.3    Campbell, D.R.4    Cherian, R.5
  • 70
    • 8944262826 scopus 로고    scopus 로고
    • Activation mediated by RP105 but not CD40 makes normal B cells susceptible to anti-IgM-induced apoptosis: A role for Fc receptor coligation
    • Yamashita, Y., K. Miyake, Y. Miura, Y. Kaneko, H. Yagita, T. Suda, S. Nagata, J. Nomura, N. Sakaguchi, and M. Kimoto. 1996. Activation mediated by RP105 but not CD40 makes normal B cells susceptible to anti-IgM-induced apoptosis: a role for Fc receptor coligation. J. Exp. Med. 184: 113-120.
    • (1996) J. Exp. Med. , vol.184 , pp. 113-120
    • Yamashita, Y.1    Miyake, K.2    Miura, Y.3    Kaneko, Y.4    Yagita, H.5    Suda, T.6    Nagata, S.7    Nomura, J.8    Sakaguchi, N.9    Kimoto, M.10
  • 71
    • 33845422163 scopus 로고    scopus 로고
    • Control of B Lymphocyte Apoptosis by the Transcription Factor NF-κB
    • DOI 10.1016/j.immuni.2006.12.003, PII S1074761306005279
    • Sen, R. 2006. Control of B lymphocyte apoptosis by the transcription factor NF-kappaB. Immunity 25: 871-883. (Pubitemid 44894957)
    • (2006) Immunity , vol.25 , Issue.6 , pp. 871-883
    • Sen, R.1
  • 72
    • 0342711256 scopus 로고    scopus 로고
    • In vivo ablation of surface immunoglobulin on mature B cells by inducible gene targeting results in rapid cell death
    • Lam, K. P., R. Kühn, and K. Rajewsky. 1997. In vivo ablation of surface immunoglobulin on mature B cells by inducible gene targeting results in rapid cell death. Cell 90: 1073-1083.
    • (1997) Cell , vol.90 , pp. 1073-1083
    • Lam, K.P.1    Kühn, R.2    Rajewsky, K.3
  • 73
    • 34247103287 scopus 로고    scopus 로고
    • Drosophila hemopoiesis and cellular immunity
    • Williams, M. J. 2007. Drosophila hemopoiesis and cellular immunity. J. Immunol. 178: 4711-4716.
    • (2007) J. Immunol. , vol.178 , pp. 4711-4716
    • Williams, M.J.1
  • 74
    • 61849170193 scopus 로고    scopus 로고
    • Genome-wide profiling of salt fractions maps physical properties of chromatin
    • Henikoff, S., J. G. Henikoff, A. Sakai, G. B. Loeb, and K. Ahmad. 2009. Genome-wide profiling of salt fractions maps physical properties of chromatin. Genome Res. 19: 460-469.
    • (2009) Genome Res. , vol.19 , pp. 460-469
    • Henikoff, S.1    Henikoff, J.G.2    Sakai, A.3    Loeb, G.B.4    Ahmad, K.5


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