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Volumn 14, Issue 6, 2002, Pages 688-693

Molecular adapters in FcεRI signaling and the allergic response

Author keywords

[No Author keywords available]

Indexed keywords

2 MORPHOLINO 8 PHENYLCHROMONE; ADHESION AND DEGRANULATION PROMOTING ADAPTER PROTEIN; CBL PROTEIN; CRK LIKE PROTEIN; FC RECEPTOR; GRB2 ASSOCIATED BINDER LIKE PROTEIN 2; GRB2 LIKE ADAPTER DOWNSTREAM OF SHC PROTEIN; GROWTH FACTOR RECEPTOR BOUND PROTEIN 2; IMMUNOGLOBULIN E; LINKER FOR ACTIVATION OF T CELL PROTEIN; PROTEIN; PROTEIN 3BP2; PROTEIN 62 DOK; PROTEIN CLNK; PROTEIN MIST; PROTEIN NCK; PROTEIN SHC; PROTEIN VAV1; SH2 CONTAINING LEUKOCYTE SPECIFIC PROTEIN 76; UNCLASSIFIED DRUG; CARRIER PROTEIN; GAB2 PROTEIN, HUMAN; IMMUNOGLOBULIN E RECEPTOR; LAT PROTEIN, HUMAN; MEMBRANE PROTEIN; PHOSPHOPROTEIN; SIGNAL TRANSDUCING ADAPTOR PROTEIN; SLP 76 SIGNAL TRANSDUCING ADAPTOR PROTEINS; SLP-76 SIGNAL TRANSDUCING ADAPTOR PROTEINS;

EID: 0036888683     PISSN: 09527915     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0952-7915(02)00396-5     Document Type: Review
Times cited : (159)

References (51)
  • 1
    • 0033753014 scopus 로고    scopus 로고
    • Signal transduction by the high-affinity immunoglobulin E receptor Fc epsilon RI: Coupling form to function
    • Nadler M.J., Matthews S.A., Turner H., Kinet J.-P. Signal transduction by the high-affinity immunoglobulin E receptor Fc epsilon RI: coupling form to function. Adv Immunol. 76:2000;325-355. A review with focus on structure and function relationship of the high affinity receptor for IgE. This is an excellent and relatively current source of IgE receptor signaling in mast cell activation.
    • (2000) Adv Immunol , vol.76 , pp. 325-355
    • Nadler, M.J.1    Matthews, S.A.2    Turner, H.3    Kinet, J.-P.4
  • 2
    • 0034502164 scopus 로고    scopus 로고
    • Activating and inhibitory signaling in mast cells: New opportunities for therapeutic intervention?
    • Ott V.L., Cambier J.C. Activating and inhibitory signaling in mast cells: new opportunities for therapeutic intervention? J Allergy Clin Immunol. 106:2000;429-440. This review summarizes how inhibitory and activating receptors govern mast cell activation and the therapeutic implications in understanding how these receptors work.
    • (2000) J Allergy Clin Immunol , vol.106 , pp. 429-440
    • Ott, V.L.1    Cambier, J.C.2
  • 3
    • 0033729622 scopus 로고    scopus 로고
    • Role of mast cells and basophils in innate and acquired immunity
    • Wedemeyer J., Tsai M., Galli S.J. Role of mast cells and basophils in innate and acquired immunity. Curr Opin Immunol. 12:2000;624-631. See annotation to [4•].
    • (2000) Curr Opin Immunol , vol.12 , pp. 624-631
    • Wedemeyer, J.1    Tsai, M.2    Galli, S.J.3
  • 4
    • 0035796556 scopus 로고    scopus 로고
    • The diverse roles of mast cells
    • Gurish M.F., Austen K.F. The diverse roles of mast cells. J Exp Med. 194:2001;F1-F6. The above reviews [3•,4•] provide an excellent summary of the role of mast cells in health and disease and present a compelling argument for the physiological importance of mast cells in innate and acquired immunity.
    • (2001) J Exp Med , vol.194
    • Gurish, M.F.1    Austen, K.F.2
  • 5
    • 0026601947 scopus 로고
    • Engagement of the high-affinity IgE receptor activates src protein-related tyrosine kinases
    • Eiseman E., Bolen J.B. Engagement of the high-affinity IgE receptor activates src protein-related tyrosine kinases. Nature. 355:1992;78-80.
    • (1992) Nature , vol.355 , pp. 78-80
    • Eiseman, E.1    Bolen, J.B.2
  • 6
    • 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.X., 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.X.2    Haleem-Smith, H.3    Metzger, H.4
  • 7
    • 0031092657 scopus 로고    scopus 로고
    • 2+ mobilization, but not degranulation, in Lyn-deficient bone marrow-derived mast cells
    • 2+ mobilization, but not degranulation, in Lyn-deficient bone marrow-derived mast cells. J Immunol. 158:1997;2350-2355.
    • (1997) J Immunol , vol.158 , pp. 2350-2355
    • Nishizumi, H.1    Yamamoto, T.2
  • 8
    • 0034254791 scopus 로고    scopus 로고
    • Redundant and opposing functions of two tyrosine kinases, Btk and Lyn, in mast cell activation
    • Kawakami Y., Kitaura J., Satterthwaite A.B., Kato R.M., Asai K., Hartman S.E., Maeda-Yamamoto M., Lowell C.A., Rawlings D.J., Witte O.N., et al. Redundant and opposing functions of two tyrosine kinases, Btk and Lyn, in mast cell activation. J Immunol. 165:2000;1210-1219. Using Btk and Lyn-null mast cells the authors demonstrate a functional role for Btk in mast cell degranulation, whereas they find that Lyn is dispensable.
    • (2000) J Immunol , vol.165 , pp. 1210-1219
    • Kawakami, Y.1    Kitaura, J.2    Satterthwaite, A.B.3    Kato, R.M.4    Asai, K.5    Hartman, S.E.6    Maeda-Yamamoto, M.7    Lowell, C.A.8    Rawlings, D.J.9    Witte, O.N.10
  • 9
    • 0036347746 scopus 로고    scopus 로고
    • Fyn kinase initiates complementary signals required for IgE-dependent mast cell degranulation
    • Parravicini V., Gadina M., Kovarova M., Odom S., Gonzalez-Espinosa C., Furumoto Y., Saitoh S., Samelson L.E., O'Shea J.J., Rivera J. Fyn kinase initiates complementary signals required for IgE-dependent mast cell degranulation. Nature Immunol. 3:2002;744-748. This paper reports that Fyn and not Lyn is required for mast cell degranulation. It also shows that Fyn regulates the Gab2-PI3K complex in mast cells and demonstrates the importance of this complex in support of PKC but not calcium signals.
    • (2002) Nature Immunol , vol.3 , pp. 744-748
    • Parravicini, V.1    Gadina, M.2    Kovarova, M.3    Odom, S.4    Gonzalez-Espinosa, C.5    Furumoto, Y.6    Saitoh, S.7    Samelson, L.E.8    O'Shea, J.J.9    Rivera, J.10
  • 10
    • 0036604986 scopus 로고    scopus 로고
    • Scaffolds, adaptors and linkers of TCR signaling: Theory and practice
    • Burack W.R., Cheng A.M., Shaw A.S. Scaffolds, adaptors and linkers of TCR signaling: theory and practice. Curr Opin Immunol. 14:2002;312-316.
    • (2002) Curr Opin Immunol , vol.14 , pp. 312-316
    • Burack, W.R.1    Cheng, A.M.2    Shaw, A.S.3
  • 11
    • 0032498231 scopus 로고    scopus 로고
    • LAT: The ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation
    • Zhang W., Sloan-Lancaster J., Kitchen J., Trible R.P., Samelson L.E. LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation. Cell. 92:1998;83-92.
    • (1998) Cell , vol.92 , pp. 83-92
    • Zhang, W.1    Sloan-Lancaster, J.2    Kitchen, J.3    Trible, R.P.4    Samelson, L.E.5
  • 12
    • 0033678973 scopus 로고    scopus 로고
    • LAT is essential for Fc(epsilon)RI-mediated mast cell activation
    • Saitoh S., Arudchandran R., Manetz T.S., Zhang W., Sommers C.L., Love P.E., Rivera J., Samelson L.E. LAT is essential for Fc(epsilon)RI-mediated mast cell activation. Immunity. 12:2000;525-535. The first report of a functional role for LAT in FcεRI-mediated mast cell degranulation. This study demonstrates the broad role of LAT in FcεRI-mediated mast cell activation.
    • (2000) Immunity , vol.12 , pp. 525-535
    • Saitoh, S.1    Arudchandran, R.2    Manetz, T.S.3    Zhang, W.4    Sommers, C.L.5    Love, P.E.6    Rivera, J.7    Samelson, L.E.8
  • 13
    • 0034051162 scopus 로고    scopus 로고
    • Membrane rafts and signaling by the multichain immune recognition receptors
    • Langlet C., Bernard A.-M., Drevot P., He H.-T. Membrane rafts and signaling by the multichain immune recognition receptors. Curr Opin Immunol. 12:2000;250-255.
    • (2000) Curr Opin Immunol , vol.12 , pp. 250-255
    • Langlet, C.1    Bernard, A.-M.2    Drevot, P.3    He, H.-T.4
  • 14
    • 0034598312 scopus 로고    scopus 로고
    • The Src homology 2 domain of Vav is required for its compartmentation to the plasma membrane and activation of c-jun NH(2)-terminal kinase 1
    • Arudchandran R., Brown M.J., Peirce M.J., Song J.S., Zhang J., Siraganian R.P., Blank U., Rivera J. The Src homology 2 domain of Vav is required for its compartmentation to the plasma membrane and activation of c-jun NH(2)-terminal kinase 1. J Exp Med. 191:2000;47-60.
    • (2000) J Exp Med , vol.191 , pp. 47-60
    • Arudchandran, R.1    Brown, M.J.2    Peirce, M.J.3    Song, J.S.4    Zhang, J.5    Siraganian, R.P.6    Blank, U.7    Rivera, J.8
  • 15
    • 0034725625 scopus 로고    scopus 로고
    • Association of Grb2, Gads, and phospholipase C-γ1 with phosphorylated LAT tyrosine residues
    • Zhang W., Trible R.P., Zhu M., Liu S.K., McGlade J., Samelson L.E. Association of Grb2, Gads, and phospholipase C-γ1 with phosphorylated LAT tyrosine residues. J Biol Chem. 275:2000;23355-23361.
    • (2000) J Biol Chem , vol.275 , pp. 23355-23361
    • Zhang, W.1    Trible, R.P.2    Zhu, M.3    Liu, S.K.4    McGlade, J.5    Samelson, L.E.6
  • 16
    • 0035817631 scopus 로고    scopus 로고
    • High resolution mapping of mast cell membranes reveals primary and secondary domains of FcεRI and LAT
    • Wilson B.S., Pfeiffer J.R., Surviladze Z., Gaudet E.A., Oliver J.M. High resolution mapping of mast cell membranes reveals primary and secondary domains of FcεRI and LAT. J Cell Biol. 154:2001;645-658. An elegant electron microscopic analysis of membrane-localized signaling proteins used by FcεRI. This study reveals that there are two distinct signaling domains formed by FcεRI aggregation and demonstrates that LAT and Gab2 are differentially partitioned in these domains.
    • (2001) J Cell Biol , vol.154 , pp. 645-658
    • Wilson, B.S.1    Pfeiffer, J.R.2    Surviladze, Z.3    Gaudet, E.A.4    Oliver, J.M.5
  • 18
    • 0034695633 scopus 로고    scopus 로고
    • Biochemical interactions integrating Itk with the T cell receptor-initiated signaling cascade
    • Bunnell S.C., Diehn M., Yaffe M.B., Findell P.R., Cantley L.C., Berg L.J. Biochemical interactions integrating Itk with the T cell receptor-initiated signaling cascade. J Biol Chem. 275:2000;2219-2230.
    • (2000) J Biol Chem , vol.275 , pp. 2219-2230
    • Bunnell, S.C.1    Diehn, M.2    Yaffe, M.B.3    Findell, P.R.4    Cantley, L.C.5    Berg, L.J.6
  • 19
    • 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., El-Hillal O., Fruman D.A., Beitz L.O., Li Z., Lin S., Gout I., Cantley L.C., Rawlings D.J., Kinet J.-P. 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. 17:1998;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
  • 20
    • 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., Smyth L.A., Norton T., Freshney N., Downward J., Kioussis D., Tybulewicz V.L.J. Vav1 transduces T cell receptor signals to the activation of phospholipase C-γ1 via phosphoinositide 3-kinase-dependent and -independent pathways. J Exp Med. 195:2002;1103-1114. See annotation to [36•].
    • (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.J.7
  • 22
    • 0034596827 scopus 로고    scopus 로고
    • Recruitment of SLP-76 to the membrane and glycolipid-enriched membrane microdomains replaces the requirement for linker for activation of T cells in T cell receptor signaling
    • Boerth N.J., Sadler J.J., Bauer D.E., Clements J.L., Gheith S.M., Koretzky G.A. Recruitment of SLP-76 to the membrane and glycolipid-enriched membrane microdomains replaces the requirement for linker for activation of T cells in T cell receptor signaling. J Exp Med. 192:2000;1047-1058. Using a chimeric SLP-76-LAT (transmembrane domain) construct expressed in LAT-deficient T cells the authors demonstrate that constitutive targeting of SLP-76 to the membrane reconstitutes many of the functions of LAT. This study shows that SLP-76 is critical to LAT-complex function.
    • (2000) J Exp Med , vol.192 , pp. 1047-1058
    • Boerth, N.J.1    Sadler, J.J.2    Bauer, D.E.3    Clements, J.L.4    Gheith, S.M.5    Koretzky, G.A.6
  • 25
    • 0035949507 scopus 로고    scopus 로고
    • Adaptor Fyb (Fyn-binding protein) regulates integrin mediated adhesion and mediator release: Differential involvement of the Fyb SH3 domain
    • Geng L., Pfister S., Kraeft S.K., Rudd C.E. Adaptor Fyb (Fyn-binding protein) regulates integrin mediated adhesion and mediator release: Differential involvement of the Fyb SH3 domain. Proc Natl Acad Sci USA. 98:2001;11527-11532. Papers [23••,24••] demonstrate that T cell activation, TCR-induced integrin clustering and integrin-mediated adhesion are defective in ADAP-deficient T cells. This paper [25••] demonstrates that ADAP overexpression can effectively modulate mast cell degranulation and adhesion and that the SH3 domain of ADAP is critical for the effect on degranulation.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 11527-11532
    • Geng, L.1    Pfister, S.2    Kraeft, S.K.3    Rudd, C.E.4
  • 26
    • 0033597929 scopus 로고    scopus 로고
    • FYN-T-FYB-SLP-76 interactions define a T-cell receptor zeta/CD3-mediated tyrosine phosphorylation pathway that up-regulates interleukin 2 transcription in T-cells
    • Raab M., Kang H., Da Silva A., Zhu X.C., Rudd C.E. FYN-T-FYB-SLP-76 interactions define a T-cell receptor zeta/CD3-mediated tyrosine phosphorylation pathway that up-regulates interleukin 2 transcription in T-cells. J Biol Chem. 274:1999;21170-21179.
    • (1999) J Biol Chem , vol.274 , pp. 21170-21179
    • Raab, M.1    Kang, H.2    Da Silva, A.3    Zhu, X.C.4    Rudd, C.E.5
  • 27
    • 0028034990 scopus 로고
    • Fibronectin receptor integrins are involved in mast cell activation
    • Ra C., Yasuda M., Yagita H., Okumura K. Fibronectin receptor integrins are involved in mast cell activation. J Allergy Clin Immunol. 94:1994;625-628.
    • (1994) J Allergy Clin Immunol , vol.94 , pp. 625-628
    • Ra, C.1    Yasuda, M.2    Yagita, H.3    Okumura, K.4
  • 28
    • 0035723473 scopus 로고    scopus 로고
    • Integrin VLA-5: Modulator and activator of mast cells
    • Houtman R., Koster A.S., Nijkamp F.P. Integrin VLA-5: modulator and activator of mast cells. Clin Exp Allergy. 31:2001;817-822.
    • (2001) Clin Exp Allergy , vol.31 , pp. 817-822
    • Houtman, R.1    Koster, A.S.2    Nijkamp, F.P.3
  • 29
    • 0030872840 scopus 로고    scopus 로고
    • Molecular analysis of the fyn-complex: Cloning of SKAP55 and SLAP-130, two novel adaptor proteins which associate with fyn and may participate in the regulation of T cell receptor-mediated signaling
    • Schraven B., Marie-Cardine A., Koretzky G. Molecular analysis of the fyn-complex: cloning of SKAP55 and SLAP-130, two novel adaptor proteins which associate with fyn and may participate in the regulation of T cell receptor-mediated signaling. Immunol Lett. 57:1997;165-169.
    • (1997) Immunol Lett , vol.57 , pp. 165-169
    • Schraven, B.1    Marie-Cardine, A.2    Koretzky, G.3
  • 31
    • 0035849822 scopus 로고    scopus 로고
    • Essential role for Gab2 in the allergic response
    • Gu H., Saito K., Klaman L.D., Shen J., Fleming T., Wang Y., Pratt J.C., Lin G., Lim B., Kinet J.-P., et al. Essential role for Gab2 in the allergic response. Nature. 412:2001;186-190. This paper is the first report a phenotype for Gab2-deficiency and demonstrates the essential nature of Gab2 for PI3K activity and mast cell degranulation.
    • (2001) Nature , vol.412 , pp. 186-190
    • Gu, H.1    Saito, K.2    Klaman, L.D.3    Shen, J.4    Fleming, T.5    Wang, Y.6    Pratt, J.C.7    Lin, G.8    Lim, B.9    Kinet, J.-P.10
  • 32
    • 0036569710 scopus 로고    scopus 로고
    • The adapter molecule Gab2 regulates FcεRI-mediated signal transduction in mast cells
    • Xie Z.-H., Ambudkar I., Siraganian R.P. The adapter molecule Gab2 regulates FcεRI-mediated signal transduction in mast cells. J Immunol. 168:2002;4682-4691.
    • (2002) J Immunol , vol.168 , pp. 4682-4691
    • Xie, Z.-H.1    Ambudkar, I.2    Siraganian, R.P.3
  • 34
    • 0033974061 scopus 로고    scopus 로고
    • Regulatory and signaling properties of the Vav family
    • Bustelo X.R. Regulatory and signaling properties of the Vav family. Mol Cell Biol. 20:2000;1461-1477.
    • (2000) Mol Cell Biol , vol.20 , pp. 1461-1477
    • Bustelo, X.R.1
  • 35
    • 0036631548 scopus 로고    scopus 로고
    • Vav proteins as signal integrators for multi-subunit immune-recognition receptors
    • Turner M., Billadeau D.D. Vav proteins as signal integrators for multi-subunit immune-recognition receptors. Nat Rev Immunol. 2:2002;476-486.
    • (2002) Nat Rev Immunol , vol.2 , pp. 476-486
    • Turner, M.1    Billadeau, D.D.2
  • 36
    • 0001764561 scopus 로고    scopus 로고
    • Vav1 regulates phospholipase Cγ activation and calcium responses in mast cells
    • Manetz T.S., Gonzalez-Espinosa G., Arudchandran R., Xirasagar S., Tybulewicz V., Rivera J. Vav1 regulates phospholipase Cγ activation and calcium responses in mast cells. Mol Cell Biol. 21:2001;3763-3774. This paper demonstrates the requirement of Vav1 for PLCγ1 and PLCγ2 tyrosine phosphorylation and for IP3 and PIP3 production. Together with [20•] these studies provide compelling evidence for the role of Vav1 in the regulation of PLCγ activity via multiple mechanisms in which Vav1 participates.
    • (2001) Mol Cell Biol , vol.21 , pp. 3763-3774
    • Manetz, T.S.1    Gonzalez-Espinosa, G.2    Arudchandran, R.3    Xirasagar, S.4    Tybulewicz, V.5    Rivera, J.6
  • 38
    • 0032566691 scopus 로고    scopus 로고
    • Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1
    • Le Good J.A., Ziegler W.H., Parekh D.B., Alessi D.R., Cohen P., Parker P.J. Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1. Science. 281:1998;2042-2045.
    • (1998) Science , vol.281 , pp. 2042-2045
    • Le Good, J.A.1    Ziegler, W.H.2    Parekh, D.B.3    Alessi, D.R.4    Cohen, P.5    Parker, P.J.6
  • 39
    • 0032562995 scopus 로고    scopus 로고
    • An unusual mechanism for ligand antagonism
    • Torigoe C., Inman J.K., Metzger H. An unusual mechanism for ligand antagonism. Science. 281:1998;568-572.
    • (1998) Science , vol.281 , pp. 568-572
    • Torigoe, C.1    Inman, J.K.2    Metzger, H.3
  • 40
    • 0035912716 scopus 로고    scopus 로고
    • Unexpected signals in a system subject to kinetic proofreading
    • Liu Z.-J., Haleem-Smith H., Chen H., Metzger H. Unexpected signals in a system subject to kinetic proofreading. Proc Natl Acad Sci USA. 98:2001;7289-7294. Using ligands (antigen) of low and high affinities the authors show that MCP-1 production, a late event in FcεRI-activated mast cells, escapes kinetic proofreading constraints. This study demonstrates that some signals can become independent and productive even when the presence of clustered and activated receptors is transient.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 7289-7294
    • Liu, Z.-J.1    Haleem-Smith, H.2    Chen, H.3    Metzger, H.4
  • 41
    • 0035423433 scopus 로고    scopus 로고
    • Elevated levels of cyclooxygenase-2 in antigen-stimulated mast cells is associated with minimal activation of p38 mitogen-activated protein kinase
    • Hundley T.R., Prasad A.R., Beaven M.A. Elevated levels of cyclooxygenase-2 in antigen-stimulated mast cells is associated with minimal activation of p38 mitogen-activated protein kinase. J Immunol. 167:2001;1629-1636.
    • (2001) J Immunol , vol.167 , pp. 1629-1636
    • Hundley, T.R.1    Prasad, A.R.2    Beaven, M.A.3
  • 42
    • 0037105464 scopus 로고    scopus 로고
    • Regulation of FcεRI-mediated degranulation by an adaptor protein 3BP2 in the rat basophilic leukemia RBL-2H3 cells
    • Sada K., Shahjahan Miah S.M., Maeno K., Kyo S., Qu X., Yamamura H. Regulation of FcεRI-mediated degranulation by an adaptor protein 3BP2 in the rat basophilic leukemia RBL-2H3 cells. Blood. 100:2002;2138-2144.
    • (2002) Blood , vol.100 , pp. 2138-2144
    • Sada, K.1    Shahjahan Miah, S.M.2    Maeno, K.3    Kyo, S.4    Qu, X.5    Yamamura, H.6
  • 43
    • 0029852837 scopus 로고    scopus 로고
    • Characterization of Cbl tyrosine phosphorylation and a Cbl-Syk complex in RBL-2H3 cells
    • Ota Y., Beitz L.O., Scharenberg A.M., Donovan J.A., Kinet J.-P., Samelson L.E. Characterization of Cbl tyrosine phosphorylation and a Cbl-Syk complex in RBL-2H3 cells. J Exp Med. 184:1996;1713-1723.
    • (1996) J Exp Med , vol.184 , pp. 1713-1723
    • Ota, Y.1    Beitz, L.O.2    Scharenberg, A.M.3    Donovan, J.A.4    Kinet, J.-P.5    Samelson, L.E.6
  • 44
    • 0001000138 scopus 로고    scopus 로고
    • Clnk, a novel SLP-76-related adaptor molecule expressed in cytokine-stimulated hemopoietic cells
    • Cao M.Y., Davidson D., Yu J., Latour S., Veillette A. Clnk, a novel SLP-76-related adaptor molecule expressed in cytokine-stimulated hemopoietic cells. J Exp Med. 190:1999;1527-1534.
    • (1999) J Exp Med , vol.190 , pp. 1527-1534
    • Cao, M.Y.1    Davidson, D.2    Yu, J.3    Latour, S.4    Veillette, A.5
  • 46
    • 0032533490 scopus 로고    scopus 로고
    • Differential interaction of Crkl with Cbl or C3G, Hef-1, and gamma subunit immunoreceptor tyrosine-based activation motif in signaling of myeloid high affinity Fc receptor for IgG (Fc gamma RI)
    • Kyono W.T., de Jong R., Park R.K., Liu Y., Heisterkamp N., Groffen J., Durden D.L. Differential interaction of Crkl with Cbl or C3G, Hef-1, and gamma subunit immunoreceptor tyrosine-based activation motif in signaling of myeloid high affinity Fc receptor for IgG (Fc gamma RI). J Immunol. 161:1998;5555-5563.
    • (1998) J Immunol , vol.161 , pp. 5555-5563
    • Kyono, W.T.1    De Jong, R.2    Park, R.K.3    Liu, Y.4    Heisterkamp, N.5    Groffen, J.6    Durden, D.L.7
  • 48
    • 0032542350 scopus 로고    scopus 로고
    • Gads is a novel SH2 and SH3 domain-containing adaptor protein that binds to tyrosine-phosphorylated Shc
    • Liu S.K., McGlade C.J. Gads is a novel SH2 and SH3 domain-containing adaptor protein that binds to tyrosine-phosphorylated Shc. Oncogene. 17:1998;3073-3082.
    • (1998) Oncogene , vol.17 , pp. 3073-3082
    • Liu, S.K.1    McGlade, C.J.2
  • 49
    • 0028897659 scopus 로고
    • Regulation of the adapter molecule Grb2 by the FcεR1 in the mast cell line RBL2H3
    • Turner H., Reif K., Rivera J., Cantrell D.A. Regulation of the adapter molecule Grb2 by the FcεR1 in the mast cell line RBL2H3. J Biol Chem. 270:1995;9500-9506.
    • (1995) J Biol Chem , vol.270 , pp. 9500-9506
    • Turner, H.1    Reif, K.2    Rivera, J.3    Cantrell, D.A.4
  • 50
    • 0031021586 scopus 로고    scopus 로고
    • SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells
    • Hendricks-Taylor L.R., Motto D.G., Zhang J., Siraganian R.P., Koretzky G.A. SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells. J Biol Chem. 272:1997;1363-1367.
    • (1997) J Biol Chem , vol.272 , pp. 1363-1367
    • Hendricks-Taylor, L.R.1    Motto, D.G.2    Zhang, J.3    Siraganian, R.P.4    Koretzky, G.A.5
  • 51
    • 0037029646 scopus 로고    scopus 로고
    • Vav1 is a component of transcriptionally active complexes
    • Houlard M., Arudchandran R., Regnier-Ricard F., Germani A., Gisselbrecht S., Blank U., Rivera J., Varin-Blank N. Vav1 is a component of transcriptionally active complexes. J Exp Med. 195:2002;1115-1127. This paper demonstrates that with prolonged FcεRI stimulation, Vav1 enters the nucleus of mast cells and is found complexed with transcriptionally active NFAT and NFκB.
    • (2002) J Exp Med , vol.195 , pp. 1115-1127
    • Houlard, M.1    Arudchandran, R.2    Regnier-Ricard, F.3    Germani, A.4    Gisselbrecht, S.5    Blank, U.6    Rivera, J.7    Varin-Blank, N.8


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