메뉴 건너뛰기




Volumn 191, Issue 1, 2000, Pages 47-59

The Src homology 2 domain of Vav is required for its compartmentation to the plasma membrane and activation of c-Jun NH2-terminal kinase 1

Author keywords

Fc receptor I; Glycosphingolipid enriched microdomains; Mast cell; Plasma membrane; Vav

Indexed keywords

ADAPTOR PROTEIN; FC RECEPTOR; GLYCOSPHINGOLIPID; GUANINE NUCLEOTIDE EXCHANGE FACTOR; RAC PROTEIN; STRESS ACTIVATED PROTEIN KINASE;

EID: 0034598312     PISSN: 00221007     EISSN: None     Source Type: Journal    
DOI: 10.1084/jem.191.1.47     Document Type: Article
Times cited : (74)

References (65)
  • 1
    • 0033534533 scopus 로고    scopus 로고
    • Adaptors and molecular scaffolds in immune cell signaling
    • Rudd, C.E. 1999. Adaptors and molecular scaffolds in immune cell signaling. Cell. 96:5-8.
    • (1999) Cell , vol.96 , pp. 5-8
    • Rudd, C.E.1
  • 2
    • 0032080391 scopus 로고    scopus 로고
    • The real LAT steps forward
    • Cantrell, D. 1998. The real LAT steps forward. Trends Cell Biol. 8:180-182.
    • (1998) Trends Cell Biol. , vol.8 , pp. 180-182
    • Cantrell, D.1
  • 4
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K., and E. Ikonen. 1997. Functional rafts in cell membranes. Nature. 387:569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 6
    • 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
  • 8
    • 0032101348 scopus 로고    scopus 로고
    • Membrane compartmentation is required for efficient T cell activation
    • Xavier, R., T. Brennan, Q. Li, C. McCormack, and B. Seed. 1998. Membrane compartmentation is required for efficient T cell activation. Immunity. 8:723-732.
    • (1998) Immunity , vol.8 , pp. 723-732
    • Xavier, R.1    Brennan, T.2    Li, Q.3    McCormack, C.4    Seed, B.5
  • 9
    • 0032142953 scopus 로고    scopus 로고
    • LAT palmitoylation: Its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation
    • Zhang, W., R.P. Trible, and L.E. Samelson. 1998. LAT palmitoylation: its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation. Immunity. 9:239-246.
    • (1998) Immunity , vol.9 , pp. 239-246
    • Zhang, W.1    Trible, R.P.2    Samelson, L.E.3
  • 10
    • 0029911401 scopus 로고    scopus 로고
    • Association of a p95 Vav-containing signaling complex with the Fc∈RI gamma chain in the RBL-2H3 mast cell line. Evidence for a constitutive in vivo association of Vav with Grb2, Raf-1, and ERK2 in an active complex
    • Song, J.S., J. Gomez, L.F. Stancato, and J. Rivera. 1996. Association of a p95 Vav-containing signaling complex with the Fc∈RI gamma chain in the RBL-2H3 mast cell line. Evidence for a constitutive in vivo association of Vav with Grb2, Raf-1, and ERK2 in an active complex. J. Biol. Chem. 271: 26962-26970.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26962-26970
    • Song, J.S.1    Gomez, J.2    Stancato, L.F.3    Rivera, J.4
  • 11
    • 0031033292 scopus 로고    scopus 로고
    • Phosphotyrosine-dependent activation of Rac-1 GDP/GTP exchange by the vav proto-oncogene product
    • Crespo, P., K.E. Schuebel, A.A. Ostrom, J.S. Gutkind, and X.R. Bustelo. 1997. Phosphotyrosine-dependent activation of Rac-1 GDP/GTP exchange by the vav proto-oncogene product. Nature. 385:169-172.
    • (1997) Nature , vol.385 , pp. 169-172
    • Crespo, P.1    Schuebel, K.E.2    Ostrom, A.A.3    Gutkind, J.S.4    Bustelo, X.R.5
  • 12
    • 0028961293 scopus 로고
    • Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes, C.D., and A. Hall. 1995. Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell. 81:53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 14
    • 15144353776 scopus 로고    scopus 로고
    • Role of substrates and products of PI 3-kinase in regulating activation of Rac-related guanosine triphosphatases by Vav
    • Han, J., K. Luby-Phelps, B. Das, X. Shu, Y. Xia, R.D. Mosteller, U.M. Krishna, J.R. Falck, M.A. White, and D. Broek. 1998. Role of substrates and products of PI 3-kinase in regulating activation of Rac-related guanosine triphosphatases by Vav. Science. 279:558-560.
    • (1998) Science , vol.279 , pp. 558-560
    • Han, J.1    Luby-Phelps, K.2    Das, B.3    Shu, X.4    Xia, Y.5    Mosteller, R.D.6    Krishna, U.M.7    Falck, J.R.8    White, M.A.9    Broek, D.10
  • 16
    • 0028232808 scopus 로고
    • Vav hinds to several SH2/SH3 containing proteins in activated lymphocytes
    • Ramos-Morales, F., B.J. Druker, and S. Fischer. 1994. Vav hinds to several SH2/SH3 containing proteins in activated lymphocytes. Oncogene. 9:1917-1923.
    • (1994) Oncogene , vol.9 , pp. 1917-1923
    • Ramos-Morales, F.1    Druker, B.J.2    Fischer, S.3
  • 17
    • 0030499383 scopus 로고    scopus 로고
    • Functional and physical interactions of Syk family kinases with the Vav proto-oncogene product
    • Deckert, M., S. Tartare-Deckert, C. Couture, T. Mustelin, and A. Altman. 1996. Functional and physical interactions of Syk family kinases with the Vav proto-oncogene product. Immunity. 5:591-604.
    • (1996) Immunity , vol.5 , pp. 591-604
    • Deckert, M.1    Tartare-Deckert, S.2    Couture, C.3    Mustelin, T.4    Altman, A.5
  • 18
    • 0030914118 scopus 로고    scopus 로고
    • The Vav binding site (Y315) in ZAP-70 is critical for antigen receptor-mediated signal transduction
    • Wu, J., Q. Zhao, T. Kurosaki, and A. Weiss. 1997. The Vav binding site (Y315) in ZAP-70 is critical for antigen receptor-mediated signal transduction. J. Exp. Med. 185:1877-1882.
    • (1997) J. Exp. Med. , vol.185 , pp. 1877-1882
    • Wu, J.1    Zhao, Q.2    Kurosaki, T.3    Weiss, A.4
  • 19
    • 0001584956 scopus 로고    scopus 로고
    • Vav and SLP-76 interact and functionally cooperate in IL-2 gene activation
    • Wu, J., D.G. Motto, G.A. Koretzky, and A. Weiss. 1996. Vav and SLP-76 interact and functionally cooperate in IL-2 gene activation. Immunity. 4:593-602.
    • (1996) Immunity , vol.4 , pp. 593-602
    • Wu, J.1    Motto, D.G.2    Koretzky, G.A.3    Weiss, A.4
  • 21
    • 0028577724 scopus 로고
    • Binding of Vav to Grb2 through dimerization of Src homology 3 domains
    • Ye, Z.S., and D. Baltimore. 1994. Binding of Vav to Grb2 through dimerization of Src homology 3 domains. Proc. Natl. Acad. Sci. USA. 91:12629-12633.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12629-12633
    • Ye, Z.S.1    Baltimore, D.2
  • 23
    • 0028114049 scopus 로고
    • Novel signaling pathway suggested by SH3 domain-mediated p95vav/heterogeneous ribonucleoprotein K interaction
    • Robert, O., B. Jallal, J. Schlessinger, and A. Ullrich. 1994. Novel signaling pathway suggested by SH3 domain-mediated p95vav/heterogeneous ribonucleoprotein K interaction. J. Biol. Chem. 269:20225-20228.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20225-20228
    • Robert, O.1    Jallal, B.2    Schlessinger, J.3    Ullrich, A.4
  • 24
    • 0032489365 scopus 로고    scopus 로고
    • Vav binding to heterogeneous nuclear ribonucleoprotein (hnRNP) C. Evidence for Vav-hnRNP interactions in an RNA-dependent manner
    • Romero, F., A. Germani, E. Puvion, J. Camonis, N. Varin-Blank, S. Gisselbrecht, and S. Fischer. 1998. Vav binding to heterogeneous nuclear ribonucleoprotein (hnRNP) C. Evidence for Vav-hnRNP interactions in an RNA-dependent manner. J. Biol. Chem. 273:5923-5931.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5923-5931
    • Romero, F.1    Germani, A.2    Puvion, E.3    Camonis, J.4    Varin-Blank, N.5    Gisselbrecht, S.6    Fischer, S.7
  • 26
    • 0029985426 scopus 로고    scopus 로고
    • SH3 domain-dependent interaction of the proto-oncogene product Vav with the focal contact protein zyxin
    • Hobert, O., J.W. Schilling, M.C. Beckerle, A. Ullrich, and B. Jallal. 1996. SH3 domain-dependent interaction of the proto-oncogene product Vav with the focal contact protein zyxin. Oncogene. 12:1577-1581.
    • (1996) Oncogene , vol.12 , pp. 1577-1581
    • Hobert, O.1    Schilling, J.W.2    Beckerle, M.C.3    Ullrich, A.4    Jallal, B.5
  • 27
    • 0024980981 scopus 로고
    • Antigen receptor tail clue
    • Reth, M. 1989. Antigen receptor tail clue. Nature. 338: 383-384.
    • (1989) Nature , vol.338 , pp. 383-384
    • Reth, M.1
  • 28
    • 0027433055 scopus 로고
    • Protein-tyrosine kinase p72syk in high affinity IgE receptor signaling. Identification as a component of pp72 and association with the receptor gamma chain after receptor aggregation
    • Benhamou, M., N.J. Ryba, H. Kihara, H. Nishikata, and R.P. Siraganian. 1993. Protein-tyrosine kinase p72syk in high affinity IgE receptor signaling. Identification as a component of pp72 and association with the receptor gamma chain after receptor aggregation. J. Biol. Chem. 268:23318-23324.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23318-23324
    • Benhamou, M.1    Ryba, N.J.2    Kihara, H.3    Nishikata, H.4    Siraganian, R.P.5
  • 29
    • 0030472724 scopus 로고    scopus 로고
    • Critical role for the tyrosine kinase Syk in signalling through the high affinity IgE receptor of mast cells
    • Costello, P.S., M. Turner, A.E. Walters, C.N. Cunningham, P.H. Bauer, J. Downward, and V.L. Tybulewicz. 1996. Critical role for the tyrosine kinase Syk in signalling through the high affinity IgE receptor of mast cells. Oncogene. 13:2595-2605.
    • (1996) Oncogene , vol.13 , pp. 2595-2605
    • Costello, P.S.1    Turner, M.2    Walters, A.E.3    Cunningham, C.N.4    Bauer, P.H.5    Downward, J.6    Tybulewicz, V.L.7
  • 30
    • 0030018183 scopus 로고    scopus 로고
    • Transfection of Syk protein tyrosine kinase reconstitutes high affinity IgE receptor-mediated degranulation in a Syk-negative variant of rat basophilic leukemia RBL-2H3 cells
    • Zhang, J., E.H. Berenstein, R.L. Evans, and R.P. Siraganian. 1996. Transfection of Syk protein tyrosine kinase reconstitutes high affinity IgE receptor-mediated degranulation in a Syk-negative variant of rat basophilic leukemia RBL-2H3 cells. J. Exp. Med. 184:71-79.
    • (1996) J. Exp. Med. , vol.184 , pp. 71-79
    • Zhang, J.1    Berenstein, E.H.2    Evans, R.L.3    Siraganian, R.P.4
  • 31
    • 0030888167 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the vav proto-oncogene product links Fc∈RI to the Rac1-JNK pathway
    • Teramoto, H., P. Salem, K.C. Robbins, X.R. Bustelo, and J.S. Gutkind. 1997. Tyrosine phosphorylation of the vav proto-oncogene product links Fc∈RI to the Rac1-JNK pathway. J. Biol. Chem. 272:10751-10755.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10751-10755
    • Teramoto, H.1    Salem, P.2    Robbins, K.C.3    Bustelo, X.R.4    Gutkind, J.S.5
  • 32
    • 0023930021 scopus 로고
    • Studies with a monoclonal antibody to the β subunit of the receptor with high affinity for immunoglobulin E
    • Rivera, J., J.P. Kinet, J. Kim, C. Pucillo, and H. Metzger. 1988. Studies with a monoclonal antibody to the β subunit of the receptor with high affinity for immunoglobulin E. Mol. Immunol. 25:647-661.
    • (1988) Mol. Immunol. , vol.25 , pp. 647-661
    • Rivera, J.1    Kinet, J.P.2    Kim, J.3    Pucillo, C.4    Metzger, H.5
  • 33
    • 0020025675 scopus 로고
    • Further characterization of the β-component of the receptor for immunoglobulin E
    • Holowka, D., and H. Metzger. 1982. Further characterization of the β-component of the receptor for immunoglobulin E. Mol. Immunol. 19:219-227.
    • (1982) Mol. Immunol. , vol.19 , pp. 219-227
    • Holowka, D.1    Metzger, H.2
  • 34
    • 0032898076 scopus 로고    scopus 로고
    • Polyethylene glycolmediated infection of non-permissive mammalian cells with semliki forest virus: Application to signal transduction studies
    • Arudchandran, R., M.J. Brown, J.S. Song, S.A. Wank, H. Haleem-Smith, and J. Rivera. 1999. Polyethylene glycolmediated infection of non-permissive mammalian cells with semliki forest virus: application to signal transduction studies. J. Immunol. Methods. 222:197-208.
    • (1999) J. Immunol. Methods. , vol.222 , pp. 197-208
    • Arudchandran, R.1    Brown, M.J.2    Song, J.S.3    Wank, S.A.4    Haleem-Smith, H.5    Rivera, J.6
  • 35
    • 0030453582 scopus 로고    scopus 로고
    • Exclusion of CD45 inhibits activity of p56lck associated with glycolipid-enriched membrane domains
    • Rodgers, W., and J.K. Rose. 1996. Exclusion of CD45 inhibits activity of p56lck associated with glycolipid-enriched membrane domains. J. Cell Biol. 135:1515-1523.
    • (1996) J. Cell Biol. , vol.135 , pp. 1515-1523
    • Rodgers, W.1    Rose, J.K.2
  • 36
    • 0029763450 scopus 로고    scopus 로고
    • Human HPK1, a novel human hematopoietic progenitor kinase that activates the JNK/SAPK kinase cascade
    • Hu, M.C., W.R. Qiu, X. Wang, C.F. Meyer, and T.H. Tan. 1996. Human HPK1, a novel human hematopoietic progenitor kinase that activates the JNK/SAPK kinase cascade. Genes Dev. 10:2251-2264.
    • (1996) Genes Dev. , vol.10 , pp. 2251-2264
    • Hu, M.C.1    Qiu, W.R.2    Wang, X.3    Meyer, C.F.4    Tan, T.H.5
  • 37
    • 0021917273 scopus 로고
    • The fate of IgE bound to rat basophilic leukemia cells. IV. Functional association between the receptors for IgE
    • Furuichi, K., J. Rivera, T. Triche, and C. Isersky. 1985. The fate of IgE bound to rat basophilic leukemia cells. IV. Functional association between the receptors for IgE. J. Immunol. 134:1760-1773.
    • (1985) J. Immunol. , vol.134 , pp. 1760-1773
    • Furuichi, K.1    Rivera, J.2    Triche, T.3    Isersky, C.4
  • 38
    • 0023341187 scopus 로고
    • DNP-phycobiliproteins, fluorescent antigens to study dynamic properties of antigen-IgE-receptor complexes on RBL-2H3 rat mast cells
    • Seagrave, J.C., G.G. Deanin, J.C. Martin, B.H. Davis, and J.M. Oliver. 1987. DNP-phycobiliproteins, fluorescent antigens to study dynamic properties of antigen-IgE-receptor complexes on RBL-2H3 rat mast cells. Cytometry. 8:287-295.
    • (1987) Cytometry , vol.8 , pp. 287-295
    • Seagrave, J.C.1    Deanin, G.G.2    Martin, J.C.3    Davis, B.H.4    Oliver, J.M.5
  • 39
    • 0031452944 scopus 로고    scopus 로고
    • Compartmentalized IgE receptor-mediated signal transduction in living cells
    • Stauffer, T.P., and T. Meyer. 1997. Compartmentalized IgE receptor-mediated signal transduction in living cells. J. Cell Biol. 139:1447-1454.
    • (1997) J. Cell Biol. , vol.139 , pp. 1447-1454
    • Stauffer, T.P.1    Meyer, T.2
  • 40
    • 0028595695 scopus 로고
    • The protein tyrosine kinase ZAP-70 can associate with the SH2 domain of proto-Vav
    • Katzav, S., M. Sutherland, G. Packham, T. Yi, and A. Weiss. 1994. The protein tyrosine kinase ZAP-70 can associate with the SH2 domain of proto-Vav J. Biol. Chem. 269:32579-32585.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32579-32585
    • Katzav, S.1    Sutherland, M.2    Packham, G.3    Yi, T.4    Weiss, A.5
  • 41
    • 0028072499 scopus 로고
    • Inhibition of mast cell Fc∈R1-mediated signaling and effector function by the Syk-selective inhibitor, piceatannol
    • Oliver, J.M., D.L. Burg, B.S. Wilson, J.L. McLaughlin, and R.L. Geahlen. 1994. Inhibition of mast cell Fc∈R1-mediated signaling and effector function by the Syk-selective inhibitor, piceatannol J. Biol. Chem. 269:29697-29703.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29697-29703
    • Oliver, J.M.1    Burg, D.L.2    Wilson, B.S.3    McLaughlin, J.L.4    Geahlen, R.L.5
  • 42
    • 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., H. Chen, H. Haleem-Smith, and H. Metzger. 1997. The unique domain as the site on Lyn kinase for its constitutive association with the high affinity receptor for IgE. J. biol. Chem. 272:24072-24080.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24072-24080
    • Vonakis, B.M.1    Chen, H.2    Haleem-Smith, H.3    Metzger, H.4
  • 44
    • 0029658306 scopus 로고    scopus 로고
    • p95vav associates with tyrosine-phosphorylated SLP-76 in antigen-stimulated T cells
    • Tuosto, L., F. Michel, and O. Acuto. 1996. p95vav associates with tyrosine-phosphorylated SLP-76 in antigen-stimulated T cells. J. Exp. Med. 184:1161-1166.
    • (1996) J. Exp. Med. , vol.184 , pp. 1161-1166
    • Tuosto, L.1    Michel, F.2    Acuto, O.3
  • 45
    • 0032212728 scopus 로고    scopus 로고
    • LAT is required for TCR-mediated activation of PLCγ1 and the Ras pathway
    • Finco, T.S., T. Kadlecek, W. Zhang, L.E. Samelson, and A. Weiss. 1998. LAT is required for TCR-mediated activation of PLCγ1 and the Ras pathway. Immunity. 9:617-626.
    • (1998) Immunity , vol.9 , pp. 617-626
    • Finco, T.S.1    Kadlecek, T.2    Zhang, W.3    Samelson, L.E.4    Weiss, A.5
  • 46
    • 0032498231 scopus 로고    scopus 로고
    • LAT: The ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation
    • Zhang, W., J. Sloan-Lancaster, J. Kitchen, R.P. Trible, and L.E. Samelson. 1998. LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation. Cell. 92: 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
  • 47
    • 0016285205 scopus 로고
    • The interaction of ige with rat basophilic leukemia cells. II. Quantitative aspects of the binding reaction
    • Kulczycki, A., Jr., 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., Jr.1    Metzger, H.2
  • 48
    • 0028820041 scopus 로고
    • A detergent-free method for purifying caveolae membrane from tissue culture cells
    • Smart, E.J., Y.-S. Ying, C. Mineo, and R.G.W. Andenon. 1995. A detergent-free method for purifying caveolae membrane from tissue culture cells. Proc. Natl. Acad. Sci. USA. 92: 10104-10108.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10104-10108
    • Smart, E.J.1    Ying, Y.-S.2    Mineo, C.3    Andenon, R.G.W.4
  • 49
    • 0033597894 scopus 로고    scopus 로고
    • Polarized distribution of endogenous Rac1 and RhoA at the cell surface
    • Michaely, P.A., C. Mineo, Y.-S. Ying, and R.G.W. Anderson. 1999. Polarized distribution of endogenous Rac1 and RhoA at the cell surface. J. Biol. Chem. 274:21430-21436.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21430-21436
    • Michaely, P.A.1    Mineo, C.2    Ying, Y.-S.3    Anderson, R.G.W.4
  • 51
    • 0029783037 scopus 로고    scopus 로고
    • The pleckstrin homology domain mediates transformation by oncogenic Dbl through specific intracellular targeting
    • Zheng, Y., D. Zangrill, R.A. Cerione, and A. Eva. 1996. The pleckstrin homology domain mediates transformation by oncogenic Dbl through specific intracellular targeting. J. Biol. Chem. 271:19017-19020.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19017-19020
    • Zheng, Y.1    Zangrill, D.2    Cerione, R.A.3    Eva, A.4
  • 52
    • 0033556044 scopus 로고    scopus 로고
    • Structural aspects of the association of Fc∈RI with detergent-resistant membranes
    • Field, K.A., D. Holowka, and B. Baird. 1999. Structural aspects of the association of Fc∈RI with detergent-resistant membranes. J. Biol. Chem. 274:1753-1758.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1753-1758
    • Field, K.A.1    Holowka, D.2    Baird, B.3
  • 53
    • 0027570504 scopus 로고
    • Vav: A potential link between tyrosine kinases and ras-like GTPases in hematopoietic cell signaling
    • Hu, P., B. Margolis, and J. Schlessinger. 1993. Vav: a potential link between tyrosine kinases and ras-like GTPases in hematopoietic cell signaling. Bioessays. 15:179-183.
    • (1993) Bioessays , vol.15 , pp. 179-183
    • Hu, P.1    Margolis, B.2    Schlessinger, J.3
  • 54
    • 0032147184 scopus 로고    scopus 로고
    • Vav links antigen-receptor signaling to the actin cytoskeleton
    • Fischer, K.D., K. Tedford, and J.M. Penninger. 1998. Vav links antigen-receptor signaling to the actin cytoskeleton. Semin. Immunol. 10:317-327.
    • (1998) Semin. Immunol. , vol.10 , pp. 317-327
    • Fischer, K.D.1    Tedford, K.2    Penninger, J.M.3
  • 56
    • 0028100051 scopus 로고
    • Aggregation of the high-affinity IgE receptor and enhanced activity of p53/56lyn protein-tyrosine kinase
    • Yamashita, T., S.Y. 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.Y.2    Metzger, H.3
  • 57
    • 0033613826 scopus 로고    scopus 로고
    • T lymphocyte costimulation mediated by reorganization of membrane microdomains
    • Viola, A., S. Schroeder, Y. Sakakibara, and A. Lanzavecchia. 1999. T lymphocyte costimulation mediated by reorganization of membrane microdomains. Science. 283:680-682.
    • (1999) Science , vol.283 , pp. 680-682
    • Viola, A.1    Schroeder, S.2    Sakakibara, Y.3    Lanzavecchia, A.4
  • 58
    • 0028897659 scopus 로고
    • Regulation of the adapter molecule Grb2 by the Fc∈R1 in the mast cell line RBL2H3
    • Turner, H., K. Reif, J. Rivera, and D.A. Cantrell. 1995. Regulation of the adapter molecule Grb2 by the Fc∈R1 in the mast cell line RBL2H3. J. Biol. Chem. 270:9500-9506.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9500-9506
    • Turner, H.1    Reif, K.2    Rivera, J.3    Cantrell, D.A.4
  • 62
    • 0032529221 scopus 로고    scopus 로고
    • Multiple signaling pathways for the activation of JNK in mast cells: Involvement of Bruton's tyrosine kinase, protein kinase C, and JNK kinases, SEK1 and MKK7
    • Kawakami, Y., S.E. Hartman, P.M. Holland, J.A. Cooper, and T. Kawakami. 1998. Multiple signaling pathways for the activation of JNK in mast cells: involvement of Bruton's tyrosine kinase, protein kinase C, and JNK kinases, SEK1 and MKK7 J. Immunol. 161:1795-1802.
    • (1998) J. Immunol. , vol.161 , pp. 1795-1802
    • Kawakami, Y.1    Hartman, S.E.2    Holland, P.M.3    Cooper, J.A.4    Kawakami, T.5
  • 63
    • 0032541062 scopus 로고    scopus 로고
    • Uncoupling of nonreceptor tyrosine kinases from PLC-γ1 in an SLP-76-deficient T cell
    • Yablonski, D., M.R. Kuhne, T. Kadlecek, and A. Weiss. 1998. Uncoupling of nonreceptor tyrosine kinases from PLC-γ1 in an SLP-76-deficient T cell. Science. 281:413-416.
    • (1998) Science , vol.281 , pp. 413-416
    • Yablonski, D.1    Kuhne, M.R.2    Kadlecek, T.3    Weiss, A.4
  • 64
    • 0030719389 scopus 로고    scopus 로고
    • A requirement for the Rho-family GTP exchange factor Vav in positive and negative selection of thymocytes
    • Turner, M., P.J. Mee, A.E. Walters, M.E. Quinn, A.L. Mellor, R. Zamoyska, and V.L. Tybulewicz. 1997. A requirement for the Rho-family GTP exchange factor Vav in positive and negative selection of thymocytes. Immunity. 7:451-460.
    • (1997) Immunity , vol.7 , pp. 451-460
    • Turner, M.1    Mee, P.J.2    Walters, A.E.3    Quinn, M.E.4    Mellor, A.L.5    Zamoyska, R.6    Tybulewicz, V.L.7
  • 65
    • 0028981284 scopus 로고
    • Fc∈R1-mediated recruitment of p53/56lyn to detergent-resistant membrane domains accompanies cellular signaling
    • Field, K.A., D. Holowka, and B. Baird. 1995. Fc∈R1-mediated recruitment of p53/56lyn to detergent-resistant membrane domains accompanies cellular signaling. Proc. Natl. Acad. Sci. USA. 92:9201-9205.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9201-9205
    • Field, K.A.1    Holowka, D.2    Baird, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.