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Volumn 171, Issue 3, 2005, Pages 527-536

Temporally resolved interactions between antigen-stimulated IgE receptors and Lyn kinase on living cells

Author keywords

[No Author keywords available]

Indexed keywords

CHIMERIC PROTEIN; EPIDERMAL GROWTH FACTOR; FCEPSILONRI RECEPTOR; IMMUNOGLOBULIN E RECEPTOR; PROTEIN KINASE LYN; PROTEIN TYROSINE KINASE; UNCLASSIFIED DRUG;

EID: 27744432013     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.200503110     Document Type: Article
Times cited : (108)

References (52)
  • 1
    • 1842414894 scopus 로고    scopus 로고
    • Src family-selective tyrosine kinase inhibitor, PPI, inhibits both FcεRI- and Thy-1-mediated activation of rat basophilic leukemia cells
    • Amoui, M., P. Draber, and L. Draberova. 1997. Src family-selective tyrosine kinase inhibitor, PPI, inhibits both FcεRI- and Thy-1-mediated activation of rat basophilic leukemia cells. Eur. J. Immunol. 27:1881-1886.
    • (1997) Eur. J. Immunol. , vol.27 , pp. 1881-1886
    • Amoui, M.1    Draber, P.2    Draberova, L.3
  • 2
    • 0019460298 scopus 로고
    • IgE-induced histamine release from rat basophilic leukemia cell lines: Isolation of releasing and nonreleasing clones
    • Barsumian, E.L., C. Isersky, M.G. Petrin, and R. Siraganian. 1981. IgE-induced histamine release from rat basophilic leukemia cell lines: isolation of releasing and nonreleasing clones. Eur. J. Immunol. 11:317-323.
    • (1981) Eur. J. Immunol. , vol.11 , pp. 317-323
    • Barsumian, E.L.1    Isersky, C.2    Petrin, M.G.3    Siraganian, R.4
  • 3
    • 0242331729 scopus 로고    scopus 로고
    • Imaging coexisting fluid domains in biomembrane models coupling curvature and line tension
    • Baumgart, T., S.T. Hess, and W.W. Webb. 2003. Imaging coexisting fluid domains in biomembrane models coupling curvature and line tension. Nature. 425:821-824.
    • (2003) Nature , vol.425 , pp. 821-824
    • Baumgart, T.1    Hess, S.T.2    Webb, W.W.3
  • 4
    • 23244446181 scopus 로고    scopus 로고
    • Membrane elasticity in giant vesicles with fluid phase coexistence
    • Baumgart, T., S. Das, W.W. Webb, and J.T. Jenkins. 2005. Membrane elasticity in giant vesicles with fluid phase coexistence. Biophys. J. 89:1067-1080.
    • (2005) Biophys. J. , vol.89 , pp. 1067-1080
    • Baumgart, T.1    Das, S.2    Webb, W.W.3    Jenkins, J.T.4
  • 5
    • 0024491621 scopus 로고
    • Complete structure and expression in transfected cells of high affinity IgE receptor
    • Blank, U., C. Ra, L. Miller, K. White, H. Metzger, and J.P. Kinet. 1989. Complete structure and expression in transfected cells of high affinity IgE receptor. Nature. 337:187-189.
    • (1989) Nature , vol.337 , pp. 187-189
    • Blank, U.1    Ra, C.2    Miller, L.3    White, K.4    Metzger, H.5    Kinet, J.P.6
  • 6
    • 0025342635 scopus 로고
    • Two-photon laser scanning fluorescence microscopy
    • Denk, W., J.H. Strickler, and W.W. Webb. 1990. Two-photon laser scanning fluorescence microscopy. Science. 248:73-76.
    • (1990) Science , vol.248 , pp. 73-76
    • Denk, W.1    Strickler, J.H.2    Webb, W.W.3
  • 7
    • 0033582440 scopus 로고    scopus 로고
    • The Lck SH3 domain is required for activation of the mitogen-activated protein kinase pathway but not the initiation of T-cell antigen receptor signaling
    • Denny, M.F., H.C. Kaufman, A.C. Chan, and D.B. Straus. 1999. The Lck SH3 domain is required for activation of the mitogen-activated protein kinase pathway but not the initiation of T-cell antigen receptor signaling. J. Biol. Chem. 274:5146-5152.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5146-5152
    • Denny, M.F.1    Kaufman, H.C.2    Chan, A.C.3    Straus, D.B.4
  • 8
    • 0029946890 scopus 로고    scopus 로고
    • Constrained diffusion or immobile fraction on cell surfaces: A new interpretation
    • Feder, T.J., I. Brust-Mascher, J.P. Slattery, B. Baird, and W.W. Webb. 1996. Constrained diffusion or immobile fraction on cell surfaces: a new interpretation. Biophys. J. 70:2767-2773.
    • (1996) Biophys. J. , vol.70 , pp. 2767-2773
    • Feder, T.J.1    Brust-Mascher, I.2    Slattery, J.P.3    Baird, B.4    Webb, W.W.5
  • 9
    • 0031041581 scopus 로고    scopus 로고
    • Compartmentalized activation of the high affinity immunoglobulin E receptor within membrane domains
    • Field, K.A., D. Holowka, and B. Baird. 1997. Compartmentalized activation of the high affinity immunoglobulin E receptor within membrane domains. J. Biol. Chem. 272:4276-4280.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4276-4280
    • Field, K.A.1    Holowka, D.2    Baird, B.3
  • 10
    • 23444461435 scopus 로고    scopus 로고
    • Transmembrane sequences are determinants of immunoreceptor signaling
    • Gosse, J.A., A. Wagendnecht-Wiesner, D. Holowka, and B. Baird. 2005. Transmembrane sequences are determinants of immunoreceptor signaling. J. Immunol. 175:2123-2131
    • (2005) J. Immunol. , vol.175 , pp. 2123-2131
    • Gosse, J.A.1    Wagendnecht-Wiesner, A.2    Holowka, D.3    Baird, B.4
  • 11
    • 0034641711 scopus 로고    scopus 로고
    • Simultaneous two-photon excitation of distinct labels for dual-color fluorescence crosscorrelation analysis
    • Heinze, K.G., A. Koltermann, and P. Schwille. 2000. Simultaneous two-photon excitation of distinct labels for dual-color fluorescence crosscorrelation analysis. Proc. Natl. Acad. Sci. USA. 97:10377-10382.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10377-10382
    • Heinze, K.G.1    Koltermann, A.2    Schwille, P.3
  • 13
    • 0141754061 scopus 로고    scopus 로고
    • Quantitative analysis of the fluorescence properties of intrinsically fluorescent proteins in living cells
    • Hess, S.T., E.D. Sheets, A. Wagenknecht-Wiesner, and A.A. Heikal. 2003. Quantitative analysis of the fluorescence properties of intrinsically fluorescent proteins in living cells. Biophys. J. 85:2566-2580.
    • (2003) Biophys. J. , vol.85 , pp. 2566-2580
    • Hess, S.T.1    Sheets, E.D.2    Wagenknecht-Wiesner, A.3    Heikal, A.A.4
  • 14
    • 0029977729 scopus 로고    scopus 로고
    • Antigen-mediated IgE receptor aggregation and signaling: A window on cell surface structure and dynamics
    • Holowka, D., and B. Baird. 1996. Antigen-mediated IgE receptor aggregation and signaling: a window on cell surface structure and dynamics. Annu. Rev. Biophys. Biomol. Struct. 25:79-112.
    • (1996) Annu. Rev. Biophys. Biomol. Struct. , vol.25 , pp. 79-112
    • Holowka, D.1    Baird, B.2
  • 15
    • 0034069892 scopus 로고    scopus 로고
    • Interactions between Fc(epsilon) RI and lipid raft components are regulated by the actin cytoskeleton
    • Holowka, D., E.D. Sheets, and B. Baird. 2000. Interactions between Fc(epsilon) RI and lipid raft components are regulated by the actin cytoskeleton. J. Cell Sci. 113:1009-1019.
    • (2000) J. Cell Sci. , vol.113 , pp. 1009-1019
    • Holowka, D.1    Sheets, E.D.2    Baird, B.3
  • 17
    • 0033981831 scopus 로고    scopus 로고
    • Sequential requirements of the N-terminal palmitoylation site and SH2 domain of Src family kinases in the initiation and progression of Fcvarepsilon RI signaling
    • Honda, Z.-i., T. Suzuki, H. Kono, M. Okada, T. Yamamoto, C. Ra, Y. Morita, and K. Yamamoto. 2000. Sequential requirements of the N-terminal palmitoylation site and SH2 domain of Src family kinases in the initiation and progression of Fcvarepsilon RI signaling. Mol. Cell. Biol. 20:1759-1771.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1759-1771
    • Honda, Z.-I.1    Suzuki, T.2    Kono, H.3    Okada, M.4    Yamamoto, T.5    Ra, C.6    Morita, Y.7    Yamamoto, K.8
  • 18
    • 0038788003 scopus 로고    scopus 로고
    • Mechanism of Lck recruitment to the T-cell receptor cluster as studied by single-molecule-fluorescence video imaging
    • Ike, H., A. Kosugi, A. Kato, R. Iino, H. Hirano, T. Fujiwara, K. Ritchie, and A. Kusumi. 2003. Mechanism of Lck recruitment to the T-cell receptor cluster as studied by single-molecule-fluorescence video imaging. ChemPhysChem. 4:620-626.
    • (2003) ChemPhysChem. , vol.4 , pp. 620-626
    • Ike, H.1    Kosugi, A.2    Kato, A.3    Iino, R.4    Hirano, H.5    Fujiwara, T.6    Ritchie, K.7    Kusumi, A.8
  • 19
    • 0027998631 scopus 로고
    • Src homology 2 domains of Syk and Lyn bind to tyrosine-phosphorylated subunits of the high affinity IgE receptor
    • Kihara, H., and R. Siraganian. 1994. Src homology 2 domains of Syk and Lyn bind to tyrosine-phosphorylated subunits of the high affinity IgE receptor. J. Biol. Chem. 269:22427-22432.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22427-22432
    • Kihara, H.1    Siraganian, R.2
  • 20
    • 0032970154 scopus 로고    scopus 로고
    • The high-affinity IgE receptor (Fc epsilon RI): From physiology to pathology
    • Kinet, J.-P. 1999. The high-affinity IgE receptor (Fc epsilon RI): from physiology to pathology. Annu. Rev. Immunol. 17:931-972.
    • (1999) Annu. Rev. Immunol. , vol.17 , pp. 931-972
    • Kinet, J.-P.1
  • 21
    • 0035197895 scopus 로고    scopus 로고
    • Structure-function analysis of Lyn kinase association with lipid rafts and initiation of early signaling events after Fcvarepsilon receptor I aggregation
    • Kovarova, M., P. Tolar, R. Arudchandran, L. Draberova, J. Rivera, and P. Draber. 2001. Structure-function analysis of Lyn kinase association with lipid rafts and initiation of early signaling events after Fcvarepsilon receptor I aggregation. Mol. Cell. Biol. 21:8318-8328.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 8318-8328
    • Kovarova, M.1    Tolar, P.2    Arudchandran, R.3    Draberova, L.4    Rivera, J.5    Draber, P.6
  • 23
    • 0016285205 scopus 로고
    • The interaction of IgE with rat basophilic leukemia cells. II. Quantitative aspects of the binding reaction
    • Kulczycki, A., and H. Metzger. 1974. The interaction of IgE with rat basophilic leukemia cells. II. Quantitative aspects of the binding reaction. J. Exp. Med. 140:1676-1695.
    • (1974) J. Exp. Med. , vol.140 , pp. 1676-1695
    • Kulczycki, A.1    Metzger, H.2
  • 25
    • 0141530039 scopus 로고    scopus 로고
    • Direct measurement of Gag-Gag interaction during retrovirus assembly with FRET and fluorescence correlation spectroscopy
    • Larson, D.R., Y.M. Ma, V.M. Vogt, and W.W. Webb. 2003. Direct measurement of Gag-Gag interaction during retrovirus assembly with FRET and fluorescence correlation spectroscopy. J. Cell Biol. 162:1233-1244.
    • (2003) J. Cell Biol. , vol.162 , pp. 1233-1244
    • Larson, D.R.1    Ma, Y.M.2    Vogt, V.M.3    Webb, W.W.4
  • 27
    • 35949038838 scopus 로고
    • Thermodynamic fluctuations in a reacting system. Measurement by fluorescence correlation spectroscopy
    • Magde, D., E. Elson, and W.W. Webb. 1972. Thermodynamic fluctuations in a reacting system. Measurement by fluorescence correlation spectroscopy. Phys. Rev. Lett. 29:705-708.
    • (1972) Phys. Rev. Lett. , vol.29 , pp. 705-708
    • Magde, D.1    Elson, E.2    Webb, W.W.3
  • 28
    • 0028911068 scopus 로고
    • Chemical cross-linking of IgEreceptor complexes in RBL-2H3 cells
    • Mao, S.Y., T. Yamashita, and H. Metzger. 1995. Chemical cross-linking of IgEreceptor complexes in RBL-2H3 cells. Biochemistry. 34:11968-11977.
    • (1995) Biochemistry , vol.34 , pp. 11968-11977
    • Mao, S.Y.1    Yamashita, T.2    Metzger, H.3
  • 29
    • 0022590784 scopus 로고
    • Cross-linking of receptor-bound Ige to aggregates larger than dimers leads to rapid immobilization
    • Menon, A.K., D. Holowka, W.W. Webb, and B. Baird. 1986. Cross-linking of receptor-bound Ige to aggregates larger than dimers leads to rapid immobilization. J. Cell Biol. 102:541-550.
    • (1986) J. Cell Biol. , vol.102 , pp. 541-550
    • Menon, A.K.1    Holowka, D.2    Webb, W.W.3    Baird, B.4
  • 31
    • 0024332066 scopus 로고
    • Immunoglobulin e receptor cross-linking induces oscillations in intracellular free ionized calcium in individual tumor mast cells
    • Millard, P.J., T.A. Ryan, W.W. Webb, and C. Fewtrell. 1989. Immunoglobulin E receptor cross-linking induces oscillations in intracellular free ionized calcium in individual tumor mast cells. J. Biol. Chem. 264:19730-19739.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19730-19739
    • Millard, P.J.1    Ryan, T.A.2    Webb, W.W.3    Fewtrell, C.4
  • 32
    • 7444243760 scopus 로고    scopus 로고
    • In situ measurement of degranulation as a biosensor based on RBL-2H3 mast cells
    • Naal, R.M.Z.G., J. Tabb, D. Holowka, and B. Baird. 2004. In situ measurement of degranulation as a biosensor based on RBL-2H3 mast cells. Biosens. Bioelectron. 20:791-796.
    • (2004) Biosens. Bioelectron. , vol.20 , pp. 791-796
    • Naal, R.M.Z.G.1    Tabb, J.2    Holowka, D.3    Baird, B.4
  • 34
    • 0036498594 scopus 로고    scopus 로고
    • Cutting edge: Transmembrane phosphoprotein Csk-binding protein/phosphoprotein associated with glycosphingolipid-enriched microdomains as a negative feedback regulator of mast cell signaling through the FcepsilonRI
    • Ohtake, H., N. Ichikawa, M. Okada, and T. Yamashita. 2002. Cutting edge: transmembrane phosphoprotein Csk-binding protein/phosphoprotein associated with glycosphingolipid-enriched microdomains as a negative feedback regulator of mast cell signaling through the FcepsilonRI. J. Immunol. 168:2087-2090.
    • (2002) J. Immunol. , vol.168 , pp. 2087-2090
    • Ohtake, H.1    Ichikawa, N.2    Okada, M.3    Yamashita, T.4
  • 36
    • 0026633167 scopus 로고
    • Aggregation of IgE-receptor complexes on rat basophilic leukemia cells does not change the intrinsic affinity but can alter the kinetics of the ligand-IgE interaction
    • Posner, R.G., B. Lee, D.H. Conrad, D. Holowka, B. Baird, and B. Goldstein. 1992. Aggregation of IgE-receptor complexes on rat basophilic leukemia cells does not change the intrinsic affinity but can alter the kinetics of the ligand-IgE interaction. Biochemistry. 31:5350-5356.
    • (1992) Biochemistry , vol.31 , pp. 5350-5356
    • Posner, R.G.1    Lee, B.2    Conrad, D.H.3    Holowka, D.4    Baird, B.5    Goldstein, B.6
  • 37
    • 0028035310 scopus 로고
    • Transphosphorylation as the mechanism by which the high-affinity receptor for IgE is phosphorylated upon aggregation
    • Pribluda, V.S., C. Pribluda, and H. Metzger. 1994. Transphosphorylation as the mechanism by which the high-affinity receptor for IgE is phosphorylated upon aggregation. Proc. Natl. Acad. Sci. USA. 91:11246-11250.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11246-11250
    • Pribluda, V.S.1    Pribluda, C.2    Metzger, H.3
  • 38
    • 0035041672 scopus 로고    scopus 로고
    • Cross-correlation analysis of innerleaflet-anchored green fluorescent protein co-redistributed with IgE receptors and outer leaflet lipid raft components
    • Pyenta, P.S., D. Holowka, and B. Baird. 2001. Cross-correlation analysis of innerleaflet-anchored green fluorescent protein co-redistributed with IgE receptors and outer leaflet lipid raft components. Biophys. J. 80:2120-2132.
    • (2001) Biophys. J. , vol.80 , pp. 2120-2132
    • Pyenta, P.S.1    Holowka, D.2    Baird, B.3
  • 39
    • 0242334251 scopus 로고    scopus 로고
    • Lateral diffusion of membrane lipid-anchored probes before and after aggregation of cell surface IgE-receptors
    • Pyenta, P.S., P. Schwille, W.W. Webb, D. Holowka, and B.A. Baird. 2003. Lateral diffusion of membrane lipid-anchored probes before and after aggregation of cell surface IgE-receptors. J. Phys. Chem. A. 107:8310-8318.
    • (2003) J. Phys. Chem. A , vol.107 , pp. 8310-8318
    • Pyenta, P.S.1    Schwille, P.2    Webb, W.W.3    Holowka, D.4    Baird, B.A.5
  • 43
    • 0032828419 scopus 로고    scopus 로고
    • Molecular dynamics in living cells observed by fluorescence correlation spectroscopy with one- and two-photon excitation
    • Schwille, P., U. Haupts, S. Maiti, and W.W. Webb. 1999. Molecular dynamics in living cells observed by fluorescence correlation spectroscopy with one- and two-photon excitation. Biophys. J. 77:2251-2265.
    • (1999) Biophys. J. , vol.77 , pp. 2251-2265
    • Schwille, P.1    Haupts, U.2    Maiti, S.3    Webb, W.W.4
  • 44
    • 0242659390 scopus 로고    scopus 로고
    • Mast cell signal transduction from the high-affinity IgE receptor
    • Siraganian, R.P. 2003. Mast cell signal transduction from the high-affinity IgE receptor. Curr. Opin. Immunol. 15:639-646.
    • (2003) Curr. Opin. Immunol. , vol.15 , pp. 639-646
    • Siraganian, R.P.1
  • 45
    • 0030796010 scopus 로고    scopus 로고
    • Inhibition of Lyn function in mast cell activation by SH3 domain binding peptides
    • Stauffer, T.P., C.H. Martenson, J.E. Rider, B.K. Kay, and T. Meyer. 1997. Inhibition of Lyn function in mast cell activation by SH3 domain binding peptides. Biochemistry. 36:9388-9394.
    • (1997) Biochemistry , vol.36 , pp. 9388-9394
    • Stauffer, T.P.1    Martenson, C.H.2    Rider, J.E.3    Kay, B.K.4    Meyer, T.5
  • 46
    • 0028352175 scopus 로고
    • Large-scale coaggregation of fluorescent lipid probes with cell-surface proteins
    • Thomas, J.L., D. Holowka, B. Baird, and W.W. Webb. 1994. Large-scale coaggregation of fluorescent lipid probes with cell-surface proteins. J. Cell Biol. 125:795-802.
    • (1994) J. Cell Biol. , vol.125 , pp. 795-802
    • Thomas, J.L.1    Holowka, D.2    Baird, B.3    Webb, W.W.4
  • 47
    • 0000247668 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy: Inception, biophysical experimentations and prospectus
    • Webb, W.W. 2001. Fluorescence correlation spectroscopy: inception, biophysical experimentations and prospectus. Appl. Opt. 40:3969-3983.
    • (2001) Appl. Opt. , vol.40 , pp. 3969-3983
    • Webb, W.W.1
  • 48
    • 0034728966 scopus 로고    scopus 로고
    • Observing FcεRI signaling from the inside of the mast cell membrane
    • Wilson, B.S., J.R. Pfeiffer, and J.M. Oliver. 2000. Observing FcεRI signaling from the inside of the mast cell membrane. J. Cell Biol. 149:1131-1142.
    • (2000) J. Cell Biol. , vol.149 , pp. 1131-1142
    • Wilson, B.S.1    Pfeiffer, J.R.2    Oliver, J.M.3
  • 49
    • 4644364556 scopus 로고    scopus 로고
    • Visualization of plasma membrane compartmentalization with patterned lipid bilayers
    • Wu, M., D. Holowka, H.G. Craighead, and B. Baird. 2004. Visualization of plasma membrane compartmentalization with patterned lipid bilayers. Proc. Natl. Acad. Sci. USA. 101:13798-13803.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 13798-13803
    • Wu, M.1    Holowka, D.2    Craighead, H.G.3    Baird, B.4
  • 51
    • 0028100051 scopus 로고
    • Aggregation of the high-affinity IgE receptor and enhanced activity of p53/ 56lyn protein-tyrosine kinase
    • Yamashita, T., S. Mao, and H. Metzger. 1994. Aggregation of the high-affinity IgE receptor and enhanced activity of p53/ 56lyn protein-tyrosine kinase. Proc. Natl. Acad. Sci. USA. 91:11251-11255.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11251-11255
    • Yamashita, T.1    Mao, S.2    Metzger, H.3
  • 52
    • 12544257509 scopus 로고    scopus 로고
    • Reconstitution of regulated phosphorylation of Fc epsilon RI by a lipid raft-excluded protein-tyrosine phosphatase
    • Young, R.M., X.M. Zheng, D. Holowka, and B. Baird. 2005. Reconstitution of regulated phosphorylation of Fc epsilon RI by a lipid raft-excluded protein-tyrosine phosphatase. J. Biol. Chem. 280:1230-1235.
    • (2005) J. Biol. Chem. , vol.280 , pp. 1230-1235
    • Young, R.M.1    Zheng, X.M.2    Holowka, D.3    Baird, B.4


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