메뉴 건너뛰기




Volumn 82, Issue 2-3, 1999, Pages 109-119

How does the plasma membrane participate in cellular signaling by receptors for immunoglobulin E?

Author keywords

IgE receptor; Lipid rafts; Lipid lipid interactions; Lipid protein interactions; Membrane domains; Signal transduction

Indexed keywords

CHOLESTEROL; IMMUNOGLOBULIN E; IMMUNOGLOBULIN E RECEPTOR; MEMBRANE LIPID; MEMBRANE PROTEIN; PHOSPHOLIPID;

EID: 0033552651     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(99)00110-6     Document Type: Conference Paper
Times cited : (79)

References (50)
  • 1
    • 0032983905 scopus 로고    scopus 로고
    • Membrane organization in immunoglobulin E receptor signaling
    • Sheets E.D., Holowka D., Baird B. Membrane organization in immunoglobulin E receptor signaling. Curr. Opin. Chem. Biol. 3:1999;95-99.
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 95-99
    • Sheets, E.D.1    Holowka, D.2    Baird, B.3
  • 2
    • 0029977729 scopus 로고    scopus 로고
    • Antigen-mediated IgE receptor aggregation and signaling: A window on cell surface structure and dynamics
    • Holowka D., Baird B. Antigen-mediated IgE receptor aggregation and signaling: a window on cell surface structure and dynamics. Annu. Rev. Biophys. Biomol. Struct. 25:1996;79-112.
    • (1996) Annu. Rev. Biophys. Biomol. Struct. , vol.25 , pp. 79-112
    • Holowka, D.1    Baird, B.2
  • 3
    • 0032970154 scopus 로고    scopus 로고
    • The high affinity IgE receptor (FcεRI): From physiology to pathology
    • Kinet J.-P. The high affinity IgE receptor (FcεRI): from physiology to pathology. Annu. Rev. Immunol. 17:1999;931-972.
    • (1999) Annu. Rev. Immunol. , vol.17 , pp. 931-972
    • Kinet, J.-P.1
  • 4
    • 0028014460 scopus 로고
    • Signal transduction by lymphocyte antigen receptors
    • Weiss A., Littman D.R. Signal transduction by lymphocyte antigen receptors. Cell. 76:1994;263-274.
    • (1994) Cell , vol.76 , pp. 263-274
    • Weiss, A.1    Littman, D.R.2
  • 5
    • 0030929805 scopus 로고    scopus 로고
    • Fc receptor biology
    • Daëron M. Fc receptor biology. Annu. Rev. Immunol. 15:1997;203-234.
    • (1997) Annu. Rev. Immunol. , vol.15 , pp. 203-234
    • Daëron, M.1
  • 6
    • 0029000726 scopus 로고
    • Early events in mast cell signal transduction
    • Scharenberg A.M., Kinet J.P. Early events in mast cell signal transduction. Chem. Immunol. 61:1995;72-87.
    • (1995) Chem. Immunol. , vol.61 , pp. 72-87
    • Scharenberg, A.M.1    Kinet, J.P.2
  • 7
    • 0029082078 scopus 로고
    • Antigen and Fc receptor signaling. The awesome power of the immunoreceptor tyrosine-based activation motif (ITAM)
    • Cambier J.C. Antigen and Fc receptor signaling. The awesome power of the immunoreceptor tyrosine-based activation motif (ITAM). J. Immunol. 155:1995;3281-3285.
    • (1995) J. Immunol. , vol.155 , pp. 3281-3285
    • Cambier, J.C.1
  • 8
    • 0030457522 scopus 로고    scopus 로고
    • Downstream signals initiated in mast cells by FcεRI and other receptors
    • Beaven M.A., Baumgartner R.A. Downstream signals initiated in mast cells by FcεRI and other receptors. Curr. Opin. Immunol. 8:1996;766-772.
    • (1996) Curr. Opin. Immunol. , vol.8 , pp. 766-772
    • Beaven, M.A.1    Baumgartner, R.A.2
  • 9
    • 0026611231 scopus 로고
    • The receptor with high affinity for IgE
    • Metzger H. The receptor with high affinity for IgE. Immunol. Rev. 125:1992;37-48.
    • (1992) Immunol. Rev. , vol.125 , pp. 37-48
    • Metzger, H.1
  • 10
    • 0021364151 scopus 로고
    • Small oligomers of immunoglobulin E (IgE) cause large-scale clustering of IgE receptors on the surface of rat basophilic leukemia cells
    • Menon A.K., Holowka D., Baird B. Small oligomers of immunoglobulin E (IgE) cause large-scale clustering of IgE receptors on the surface of rat basophilic leukemia cells. J. Cell. Biol. 98:1984;577-583.
    • (1984) J. Cell. Biol. , vol.98 , pp. 577-583
    • Menon, A.K.1    Holowka, D.2    Baird, B.3
  • 11
    • 0022590784 scopus 로고
    • Cross-linking of receptor-bound IgE to aggregates larger than dimers leads to rapid immobilization
    • Menon A.K., Holowka D., Webb W.W., Baird B. Cross-linking of receptor-bound IgE to aggregates larger than dimers leads to rapid immobilization. J. Cell. Biol. 102:1986;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
  • 12
    • 0026530567 scopus 로고
    • Rotational motion of monomeric and dimeric immunoglobulin E-receptor complexes
    • Myers J.N., Holowka D., Baird B. Rotational motion of monomeric and dimeric immunoglobulin E-receptor complexes. Biochemistry. 31:1992;567-575.
    • (1992) Biochemistry , vol.31 , pp. 567-575
    • Myers, J.N.1    Holowka, D.2    Baird, B.3
  • 13
    • 0028352175 scopus 로고
    • Large-scale co-aggregation of fluorescent lipid probes with cell surface proteins
    • Thomas J.L., Holowka D., Baird B., Webb W.W. Large-scale co-aggregation of fluorescent lipid probes with cell surface proteins. J. Cell. Biol. 125:1994;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
  • 14
    • 0029665631 scopus 로고    scopus 로고
    • FcεRI-mediated association of 6-μm beads with RBL-2H3 mast cells results in exclusion of signaling proteins from the forming phagosome and abrogation of normal downstream signaling
    • Pierini L., Holowka D., Baird B. FcεRI-mediated association of 6-μm beads with RBL-2H3 mast cells results in exclusion of signaling proteins from the forming phagosome and abrogation of normal downstream signaling. J. Cell. Biol. 134:1996;1427-1439.
    • (1996) J. Cell. Biol. , vol.134 , pp. 1427-1439
    • Pierini, L.1    Holowka, D.2    Baird, B.3
  • 15
    • 0033577805 scopus 로고    scopus 로고
    • Critical role for cholesterol in Lyn-mediated tyrosine phosphorylation of FcεRI and their association with detergent-resistant membrane
    • E.D. Sheets, D. Holowka, B. Baird, Critical role for cholesterol in Lyn-mediated tyrosine phosphorylation of FcεRI and their association with detergent-resistant membrane, J. Cell. Biol. (1999) 877-887.
    • (1999) J. Cell. Biol. , pp. 877-887
    • Sheets, E.D.1    Holowka, D.2    Baird, B.3
  • 16
    • 0026017135 scopus 로고
    • Membrane-binding domain of the small G protein G25K contains an S-(all trans-geranylgeranyl)cysteine methyl ester as its carboxyl terminus
    • Yamane H.K., Farnsworth C.C., Xie H.Y., Evans T., Howald W.N., Gelb M.H. et al. Membrane-binding domain of the small G protein G25K contains an S-(all trans-geranylgeranyl)cysteine methyl ester as its carboxyl terminus. Proc. Natl. Acad. Sci. U.S.A. 88:1991;286-290.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 286-290
    • Yamane, H.K.1    Farnsworth, C.C.2    Xie, H.Y.3    Evans, T.4    Howald, W.N.5    Gelb, M.H.6
  • 17
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown D.A., Rose J.K. Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell. 68:1992;533-544.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 18
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown D.A., London E. Functions of lipid rafts in biological membranes. Annu. Rev. Cell. Dev. Biol. 14:1998;111-136.
    • (1998) Annu. Rev. Cell. Dev. Biol. , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 19
    • 0030949124 scopus 로고    scopus 로고
    • Functions rafts in cell membranes
    • Simons K., Ikonen E. Functions rafts in cell membranes. Nature. 387:1997;569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 20
    • 0031692336 scopus 로고    scopus 로고
    • The caveolae membrane system
    • Anderson R.G.W. The caveolae membrane system. Annu. Rev. Biochem. 67:1998;199-225.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 199-225
    • Anderson, R.G.W.1
  • 21
    • 0032527642 scopus 로고    scopus 로고
    • Structure and origin of ordered lipid domains in biological membranes
    • Brown D.A., London E. Structure and origin of ordered lipid domains in biological membranes. J. Membr. Biol. 164:1998;103-114.
    • (1998) J. Membr. Biol. , vol.164 , pp. 103-114
    • Brown, D.A.1    London, E.2
  • 23
    • 0027269661 scopus 로고
    • The tyrosine kinase connection: How GPI-anchored proteins activate T cells
    • Brown D.A. The tyrosine kinase connection: how GPI-anchored proteins activate T cells. Curr. Opin. Immunol. 5:1993;349-354.
    • (1993) Curr. Opin. Immunol. , vol.5 , pp. 349-354
    • Brown, D.A.1
  • 24
    • 0027275642 scopus 로고
    • Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins from a caveolin-rich insoluble complex in MDCK cells
    • Sargiacomo M., Sudol M., Tang Z., Lisanti M.P. Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins from a caveolin-rich insoluble complex in MDCK cells. J. Cell. Biol. 122:1993;789-807.
    • (1993) J. Cell. Biol. , vol.122 , pp. 789-807
    • Sargiacomo, M.1    Sudol, M.2    Tang, Z.3    Lisanti, M.P.4
  • 25
    • 0028981284 scopus 로고
    • lyn to detergent-resistant membrane domains accompanies cellular signaling
    • lyn to detergent-resistant membrane domains accompanies cellular signaling. Proc. Natl. Acad. Sci. U.S.A. 92:1995;9201-9205.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 9201-9205
    • Field, K.A.1    Holowka, D.2    Baird, B.3
  • 26
    • 0031041581 scopus 로고    scopus 로고
    • Compartmentalized activation of the high affinity immunoglobulin E receptor within membrane domains
    • Field K.A., Holowka D., Baird B. Compartmentalized activation of the high affinity immunoglobulin E receptor within membrane domains. J. Biol. Chem. 272:1997;4276-4280.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4276-4280
    • Field, K.A.1    Holowka, D.2    Baird, B.3
  • 27
    • 0028035310 scopus 로고
    • Transphosphorylation as the mechanism by which the high-affinity receptor for IgE is phosphorylated upon aggregation
    • Pribluda V.S., Pribluda C., Metzger H. Transphosphorylation as the mechanism by which the high-affinity receptor for IgE is phosphorylated upon aggregation. Proc. Natl. Acad. Sci. U.S.A. 91:1994;11246-11250.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 11246-11250
    • Pribluda, V.S.1    Pribluda, C.2    Metzger, H.3
  • 28
    • 0033556044 scopus 로고    scopus 로고
    • Structural aspects of the association of FcεRI with detergent-resistant membranes
    • Field K.A., Holowka D., Baird B. Structural aspects of the association of FcεRI with detergent-resistant membranes. J. Biol. Chem. 274:1999;1753-1758.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1753-1758
    • Field, K.A.1    Holowka, D.2    Baird, B.3
  • 29
    • 0033594934 scopus 로고    scopus 로고
    • Quantitative analysis of phospholipids in functionally important membrane domains from RBL-2H3 mast cells using tandem high-resolution mass spectrometry
    • Fridriksson E.K., Shipkova P.A., Sheets E.D., Holowka D., Baird B., McLafferty F.W. Quantitative analysis of phospholipids in functionally important membrane domains from RBL-2H3 mast cells using tandem high-resolution mass spectrometry. Biochemistry. 38:1999;8056-8063.
    • (1999) Biochemistry , vol.38 , pp. 8056-8063
    • Fridriksson, E.K.1    Shipkova, P.A.2    Sheets, E.D.3    Holowka, D.4    Baird, B.5    McLafferty, F.W.6
  • 30
    • 0032774243 scopus 로고    scopus 로고
    • Electron spin resonance characterization of liquid ordered phase of detergent resistant membranes from RBL-2H3 cells
    • Ge M., Field K.A., Aneja R., Holowka D., Baird B., Freed J. Electron spin resonance characterization of liquid ordered phase of detergent resistant membranes from RBL-2H3 cells. Biophys. J. 77:1999;925-933.
    • (1999) Biophys. J. , vol.77 , pp. 925-933
    • Ge, M.1    Field, K.A.2    Aneja, R.3    Holowka, D.4    Baird, B.5    Freed, J.6
  • 32
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • Varma R., Mayor S. GPI-anchored proteins are organized in submicron domains at the cell surface. Nature. 394:1998;798-801.
    • (1998) Nature , vol.394 , pp. 798-801
    • Varma, R.1    Mayor, S.2
  • 33
    • 0032514258 scopus 로고    scopus 로고
    • Distribution of a glycosylphosphatidylinostitol-anchored protein at the apical surface of MDCK cells examined at a resolution of <100 Å using imaging fluorescence resonance energy transfer
    • Kenworthy A.K., Edidin M. Distribution of a glycosylphosphatidylinostitol-anchored protein at the apical surface of MDCK cells examined at a resolution of <100 Å using imaging fluorescence resonance energy transfer. J. Cell. Biol. 142:1998;69-84.
    • (1998) J. Cell. Biol. , vol.142 , pp. 69-84
    • Kenworthy, A.K.1    Edidin, M.2
  • 34
    • 0029946890 scopus 로고    scopus 로고
    • Constrained diffusion of immobile fraction on cell surfaces: A new interpretation
    • Feder T.J., Brust-Mascher I., Slattery J.P., Baird B., Webb W.W. Constrained diffusion of immobile fraction on cell surfaces: a new interpretation. Biophys. J. 70:1996;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
  • 35
    • 0032828419 scopus 로고    scopus 로고
    • Molecular dynamics in living cells observed by fluorescence correlation spectroscopy with one- and two-photon excitation
    • Schwille P., Haupts K., Maiti S., Webb W.W. Molecular dynamics in living cells observed by fluorescence correlation spectroscopy with one- and two-photon excitation. Biophys. J. 77:1999;2257-2265.
    • (1999) Biophys. J. , vol.77 , pp. 2257-2265
    • Schwille, P.1    Haupts, K.2    Maiti, S.3    Webb, W.W.4
  • 36
    • 0033027026 scopus 로고    scopus 로고
    • Image correlation spectroscopy. II. Optimization for ultrasensitive detection of preexisting platelet-derived growth factor-β receptor oligomers on intact cells
    • Wiseman P.W., Petersen N.O. Image correlation spectroscopy. II. Optimization for ultrasensitive detection of preexisting platelet-derived growth factor-β receptor oligomers on intact cells. Biophys. J. 76:1999;963-977.
    • (1999) Biophys. J. , vol.76 , pp. 963-977
    • Wiseman, P.W.1    Petersen, N.O.2
  • 37
    • 0031452944 scopus 로고    scopus 로고
    • Compartmentalized IgE receptor-mediated signal transduction in living cells
    • Stauffer T.P., Meyer T. Compartmentalized IgE receptor-mediated signal transduction in living cells. J. Cell. Biol. 139:1997;1447-1454.
    • (1997) J. Cell. Biol. , vol.139 , pp. 1447-1454
    • Stauffer, T.P.1    Meyer, T.2
  • 38
    • 4243886550 scopus 로고    scopus 로고
    • Interactions between FcεRI and detergent resistant membrane components are regulated by the actin cytoskeleton
    • Holowka D., Sheets E.D., Baird B. Interactions between FcεRI and detergent resistant membrane components are regulated by the actin cytoskeleton. Mol. Biol. Cell. 9:1998;91a.
    • (1998) Mol. Biol. Cell. , vol.9
    • Holowka, D.1    Sheets, E.D.2    Baird, B.3
  • 39
    • 0033005974 scopus 로고    scopus 로고
    • Regulation of cortical structure by the ezrin-radixin-moesin protein family
    • Bretscher A. Regulation of cortical structure by the ezrin-radixin-moesin protein family. Curr. Opin. Cell Biol. 11:1999;109-116.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 109-116
    • Bretscher, A.1
  • 40
    • 0028922840 scopus 로고
    • Transmembrane domain of CD44 is required for its detergent insolubility in fibroblasts
    • Perschl A., Lesley J., English N., Hyman R., Trowbridge I.S. Transmembrane domain of CD44 is required for its detergent insolubility in fibroblasts. J. Cell Sci. 108:1995;1033-1041.
    • (1995) J. Cell Sci. , vol.108 , pp. 1033-1041
    • Perschl, A.1    Lesley, J.2    English, N.3    Hyman, R.4    Trowbridge, I.S.5
  • 41
    • 0032530369 scopus 로고    scopus 로고
    • Engagement of T cell receptor triggers its recruitment to low-density detergent-insoluble membrane domains
    • Montixi C., Langlet C., Bernard A.M., Thimonier J., Dubois C., Wurbel M.A. et al. Engagement of T cell receptor triggers its recruitment to low-density detergent-insoluble membrane domains. EMBO J. 17:1998;5334-5348.
    • (1998) EMBO J. , vol.17 , pp. 5334-5348
    • Montixi, C.1    Langlet, C.2    Bernard, A.M.3    Thimonier, J.4    Dubois, C.5    Wurbel, M.A.6
  • 42
    • 0032101348 scopus 로고    scopus 로고
    • Membrane compartmentation is required for efficient T cell activation
    • Xavier R., Brennan T., Li Q., McCormack C., Seed B. Membrane compartmentation is required for efficient T cell activation. Immunity. 8:1998;723-732.
    • (1998) Immunity , vol.8 , pp. 723-732
    • Xavier, R.1    Brennan, T.2    Li, Q.3    McCormack, C.4    Seed, B.5
  • 43
    • 0032142953 scopus 로고    scopus 로고
    • LAT palmitoylation: Its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation
    • Zhang W., Trible R.P., Samelson L.E. LAT palmitoylation: its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation. Immunity. 9:1998;239-246.
    • (1998) Immunity , vol.9 , pp. 239-246
    • Zhang, W.1    Trible, R.P.2    Samelson, L.E.3
  • 44
    • 0029906007 scopus 로고    scopus 로고
    • Cholesterol at different bilayer concentrations can promote or antagonize lateral segregation of phospholipids of differing acyl chain length
    • Silvius J.R., del Giudice D., Lafleur M. Cholesterol at different bilayer concentrations can promote or antagonize lateral segregation of phospholipids of differing acyl chain length. Biochemistry. 35:1996;15198-15208.
    • (1996) Biochemistry , vol.35 , pp. 15198-15208
    • Silvius, J.R.1    Del Giudice, D.2    Lafleur, M.3
  • 45
    • 0033617281 scopus 로고    scopus 로고
    • It's spring, and thoughts turn to...allergies
    • Metzger H. It's spring, and thoughts turn to...allergies. Cell. 97:1999;287-290.
    • (1999) Cell , vol.97 , pp. 287-290
    • Metzger, H.1
  • 46
    • 0032986606 scopus 로고    scopus 로고
    • The regulation of antigen receptor signaling to protein tyrosine phosphatases: A hole in the story
    • Thomas M. The regulation of antigen receptor signaling to protein tyrosine phosphatases: a hole in the story. Curr. Opin. Immunol. 11:1999;270-276.
    • (1999) Curr. Opin. Immunol. , vol.11 , pp. 270-276
    • Thomas, M.1
  • 47
    • 0033558012 scopus 로고    scopus 로고
    • The role of actin microfilaments in the down-regulation of the degranulation response in RBL-2H3 mast cells
    • Frigeri L., Agpar J.R. The role of actin microfilaments in the down-regulation of the degranulation response in RBL-2H3 mast cells. J. Immunol. 162:1999;2243-2250.
    • (1999) J. Immunol. , vol.162 , pp. 2243-2250
    • Frigeri, L.1    Agpar, J.R.2
  • 48
    • 0030849446 scopus 로고    scopus 로고
    • The unique domain as the site on Lyn kinase for its constitutive association with the high affinity receptor for IgE
    • Vonakis B.M., Chen H., Haleem-Smith H., Metzger H. The unique domain as the site on Lyn kinase for its constitutive association with the high affinity receptor for IgE. J. Biol. Chem. 272:1997;24072-24080.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24072-24080
    • Vonakis, B.M.1    Chen, H.2    Haleem-Smith, H.3    Metzger, H.4
  • 49
    • 0025791981 scopus 로고
    • Structure-function relationships in the mast cell high affinity receptor for IgE. Role of the cytoplasmic domains and of the beta subunit
    • Alber G., Miller L., Jelsema C.L., Varin-Blank N., Metzger H. Structure-function relationships in the mast cell high affinity receptor for IgE. Role of the cytoplasmic domains and of the beta subunit. J. Biol. Chem. 266:1991;22613-22620.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22613-22620
    • Alber, G.1    Miller, L.2    Jelsema, C.L.3    Varin-Blank, N.4    Metzger, H.5
  • 50
    • 0028104202 scopus 로고
    • Regulation of signal transduction and signal diversity by receptor oligomerization
    • Lemmon M.A., Schlessinger J. Regulation of signal transduction and signal diversity by receptor oligomerization. Trends Biochem. Sci. 19:1994;459-463.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 459-463
    • Lemmon, M.A.1    Schlessinger, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.