메뉴 건너뛰기




Volumn 10, Issue 4, 1998, Pages 317-327

Vav links antigen-receptor signaling to the actin cytoskeleton

Author keywords

Actin cytoskeleton; Antigen receptor capping; Guanine nucleotide exchange factor (GEF); Rho GTPases; T and B cells; Vav

Indexed keywords

ACTIN; INTERLEUKIN 2; LYMPHOCYTE ANTIGEN RECEPTOR; PHOSPHOLIPID;

EID: 0032147184     PISSN: 10445323     EISSN: None     Source Type: Journal    
DOI: 10.1006/smim.1998.0124     Document Type: Article
Times cited : (73)

References (76)
  • 1
    • 0028014460 scopus 로고
    • Signal transduction by lymphocyte antigen receptors
    • 1. Weiss A, Littman DR (1994) Signal transduction by lymphocyte antigen receptors. Cell 76:263-274
    • (1994) Cell , vol.76 , pp. 263-274
    • Weiss, A.1    Littman, D.R.2
  • 2
    • 0024433697 scopus 로고
    • Vav, a novel human oncogene derived from a locus ubiquitously expressed in hematopoietic cells
    • 2. Katzav S, Martin-Zanca D, Barbacid M (1989) vav, a novel human oncogene derived from a locus ubiquitously expressed in hematopoietic cells. EMBO J 8:2283-2290
    • (1989) EMBO J , vol.8 , pp. 2283-2290
    • Katzav, S.1    Martin-Zanca, D.2    Barbacid, M.3
  • 3
    • 0026591451 scopus 로고
    • The hematopoietically expressed vav proto-oncogene shares homology with the dbl GDP-GTP exchange factor, the bcr gene and a yeast gene (CDC24) involved in cytoskeletal organization
    • 3. Adams JM, Houston H, Allen J, Lints T, Harvey R (1992) The hematopoietically expressed vav proto-oncogene shares homology with the dbl GDP-GTP exchange factor, the bcr gene and a yeast gene (CDC24) involved in cytoskeletal organization. Oncogene 7:611-618
    • (1992) Oncogene , vol.7 , pp. 611-618
    • Adams, J.M.1    Houston, H.2    Allen, J.3    Lints, T.4    Harvey, R.5
  • 4
    • 0028785252 scopus 로고
    • Does Vav bind to F-actin through a CH domain?
    • 4. Castresana J, Saraste M (1995) Does Vav bind to F-actin through a CH domain? FEES Lett 374:149-151
    • (1995) FEES Lett , vol.374 , pp. 149-151
    • Castresana, J.1    Saraste, M.2
  • 5
    • 0030429765 scopus 로고    scopus 로고
    • The VAV family of signal transduction molecules
    • 5. Bustelo XR (1996) The VAV family of signal transduction molecules. Crit Rev Oncog 7:65-88
    • (1996) Crit Rev Oncog , vol.7 , pp. 65-88
    • Bustelo, X.R.1
  • 7
    • 0031033292 scopus 로고    scopus 로고
    • Phosphotyrosine-dependent activation of Rac-1 GDP/GTP exchange by the vav proto-oncogene product
    • 7. Crespo P, Schuebel KE, Ostrom AA, Gutkind JS, Bustelo XR (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
  • 11
    • 0028915948 scopus 로고
    • Defective signalling through the T- and B-cell antigen receptors in lymphoid cells lacking the vav proto-oncogene
    • 11. Zhang R, Alt FW, Davidson L, Orkin SH, Swat W (1995) Defective signalling through the T- and B-cell antigen receptors in lymphoid cells lacking the vav proto-oncogene. Nature 374:470-473
    • (1995) Nature , vol.374 , pp. 470-473
    • Zhang, R.1    Alt, F.W.2    Davidson, L.3    Orkin, S.H.4    Swat, W.5
  • 12
    • 0028904413 scopus 로고
    • Defective T-cell receptor signalling and positive selection of Vav-deficient CD4 + CD8 + thymocytes
    • 12. Fischer KD, Zmuldzinas A Gardner S, Barbacid M, Bernstein A, Guidos C (1995) Defective T-cell receptor signalling and positive selection of Vav-deficient CD4 + CD8 + thymocytes. Nature 374:474-477
    • (1995) Nature , vol.374 , pp. 474-477
    • Fischer, K.D.1    Zmuldzinas, A.2    Gardner, S.3    Barbacid, M.4    Bernstein, A.5    Guidos, C.6
  • 13
    • 0030719389 scopus 로고    scopus 로고
    • A requirement for the Rho-family GTP exchange factor Vav in positive and negative selection of thymocytes
    • 13. Turner M, Mee PJ, Walters AE, Quinn ME, Mellor AL, Zamoyska R, Tybulewicz VL (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
  • 15
    • 0030968580 scopus 로고    scopus 로고
    • Rho GTPases and signaling networks
    • 15. Van Aelst L, D'Souza-Schorey C (1997) Rho GTPases and signaling networks. Genes Dev 11:2295-2322
    • (1997) Genes Dev , vol.11 , pp. 2295-2322
    • Van Aelst, L.1    D'Souza-Schorey, C.2
  • 16
    • 0030806477 scopus 로고    scopus 로고
    • Different functions of the GTPase Rho in prothymocytes and late pre-T cells
    • 16. Galandrini R, Henning SW, Cantrell DA (1997) Different functions of the GTPase Rho in prothymocytes and late pre-T cells. Immunity 7:163-174
    • (1997) Immunity , vol.7 , pp. 163-174
    • Galandrini, R.1    Henning, S.W.2    Cantrell, D.A.3
  • 17
    • 0030772153 scopus 로고    scopus 로고
    • Enhanced apoptosis in the thymus of transgenic mice expressing constitutively activated forms of human Rac2GTPase
    • 17. Lores P, Morin L, Luna R, Gacon G (1997) Enhanced apoptosis in the thymus of transgenic mice expressing constitutively activated forms of human Rac2GTPase. Oncogene 15:601-605
    • (1997) Oncogene , vol.15 , pp. 601-605
    • Lores, P.1    Morin, L.2    Luna, R.3    Gacon, G.4
  • 18
    • 0030798405 scopus 로고    scopus 로고
    • The small GTPase Cdc42 initiates an apoptotic signaling pathway in Jurkat T lymphocytes
    • 18. Chuang TH, Hahn KM, Lee JD, Danley DE, Bokoch GM (1997) The small GTPase Cdc42 initiates an apoptotic signaling pathway in Jurkat T lymphocytes. Mol Biol Cell 8:1687-1698
    • (1997) Mol Biol Cell , vol.8 , pp. 1687-1698
    • Chuang, T.H.1    Hahn, K.M.2    Lee, J.D.3    Danley, D.E.4    Bokoch, G.M.5
  • 19
    • 0029008280 scopus 로고
    • Regulation of the polarization of T cells toward antigen-presenting cells by Ras-related GTPase CDC42
    • 19. Stowers L, Yelon D, Berg LJ, Chant J (1995) Regulation of the polarization of T cells toward antigen-presenting cells by Ras-related GTPase CDC42. Proc Natl Acad Sci USA 92:5027-5031
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5027-5031
    • Stowers, L.1    Yelon, D.2    Berg, L.J.3    Chant, J.4
  • 20
    • 0030156269 scopus 로고    scopus 로고
    • Disease mechanism: Unravelling Wiskott-Aldrich syndrome
    • 20. Kirchhausen T, Rosen FS (1996) Disease mechanism: unravelling Wiskott-Aldrich syndrome. Curr Biol 6:676-678
    • (1996) Curr Biol , vol.6 , pp. 676-678
    • Kirchhausen, T.1    Rosen, F.S.2
  • 21
    • 0027207287 scopus 로고
    • Tyrosine kinase-stimulated guanine nucleotide exchange activity of Vav in T cell activation
    • 21. Gulbins E, Coggeshall KM, Baier G, Katzav S, Burn P, Altman A (1993) Tyrosine kinase-stimulated guanine nucleotide exchange activity of Vav in T cell activation. Science 260:822-825
    • (1993) Science , vol.260 , pp. 822-825
    • Gulbins, E.1    Coggeshall, K.M.2    Baier, G.3    Katzav, S.4    Burn, P.5    Altman, A.6
  • 22
    • 0028075246 scopus 로고
    • Dbl and Vav mediate transformation via mitogen-activated protein kinase pathways that are distinct from those activated by oncogenic Ras
    • 22. Khosravi-Far R, Chrzanowska-Wodnicka M, Solski PA, Eva A, Burridge K, Der CJ (1994) Dbl and Vav mediate transformation via mitogen-activated protein kinase pathways that are distinct from those activated by oncogenic Ras. Mol Cell Biol 14:6848-6857
    • (1994) Mol Cell Biol , vol.14 , pp. 6848-6857
    • Khosravi-Far, R.1    Chrzanowska-Wodnicka, M.2    Solski, P.A.3    Eva, A.4    Burridge, K.5    Der, C.J.6
  • 23
    • 15144353776 scopus 로고    scopus 로고
    • Role of substrates and products of PI 3-kinase in regulating activation of Rac-related guanosine triphosphatasesby Vav
    • 23. Man J et al (1998) Role of substrates and products of PI 3-kinase in regulating activation of Rac-related guanosine triphosphatasesby Vav. Science 279:558-560
    • (1998) Science , vol.279 , pp. 558-560
    • Man, J.1
  • 24
    • 0031006326 scopus 로고    scopus 로고
    • Regulatory recruitment of signalling molecules to the cell membrane by pleckstrin-homology domains
    • 24. Lemmon MA, Falasca M, Ferguson KM, Schlessinger J (1997) Regulatory recruitment of signalling molecules to the cell membrane by pleckstrin-homology domains. Trends Cell Biol 7:237-242
    • (1997) Trends Cell Biol , vol.7 , pp. 237-242
    • Lemmon, M.A.1    Falasca, M.2    Ferguson, K.M.3    Schlessinger, J.4
  • 25
    • 0030992837 scopus 로고    scopus 로고
    • Signalling through the lipid products of phosphoinositide-3-OH kinase
    • 25. Toker A, Cantley LC (1997) Signalling through the lipid products of phosphoinositide-3-OH kinase. Nature 387:673-676
    • (1997) Nature , vol.387 , pp. 673-676
    • Toker, A.1    Cantley, L.C.2
  • 27
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • 27. Pawson T (1995) Protein modules and signalling networks. Nature 373:573-580
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 28
    • 0030022278 scopus 로고    scopus 로고
    • The tyrosine phosphatase PTPlC associates with Vav, Grb2, and mSos1 in hematopoietic cells
    • 28. Kon-Kozlowski M, Pani G, Pawson T, Siminovitch KA (1996) The tyrosine phosphatase PTPlC associates with Vav, Grb2, and mSos1 in hematopoietic cells. J Biol Chem 271:3856-3862
    • (1996) J Biol Chem , vol.271 , pp. 3856-3862
    • Kon-Kozlowski, M.1    Pani, G.2    Pawson, T.3    Siminovitch, K.A.4
  • 29
    • 0029787216 scopus 로고    scopus 로고
    • Signaling capacity of the T cell antigen receptor is negatively regulated by the PTP1C tyrosine phosphatase
    • 29. Pani G, Fischer KD, Mlinaric-Rascan I, Siminovitch KA (1996) Signaling capacity of the T cell antigen receptor is negatively regulated by the PTP1C tyrosine phosphatase. J Exp Med 184:839-852
    • (1996) J Exp Med , vol.184 , pp. 839-852
    • Pani, G.1    Fischer, K.D.2    Mlinaric-Rascan, I.3    Siminovitch, K.A.4
  • 32
    • 0001584956 scopus 로고    scopus 로고
    • Vav and SLP-76 interact and functionally cooperate in IL-2 gene activation
    • 32. Wu J, Motto DG, Koretzky GA, Weiss A (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
  • 33
    • 0030499383 scopus 로고    scopus 로고
    • Functional and physical interactions of Syk family kinases with the Vav proto-oncogene product
    • 33. Deckert M, Tartare-Deckert S, Couture C, Mustelin T, Altman A (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
  • 34
    • 0030914118 scopus 로고    scopus 로고
    • The Vav binding site (Y315) in ZAP-70 is critical for antigen receptor-mediated signal transduction
    • 34. Wu J, Zhao Q, Kurosaki T, Weiss A (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
  • 35
    • 0031007093 scopus 로고    scopus 로고
    • Role of the vav proto-oncogene product (Vav) in erythropoietin-mediated cell proliferation and phosphatidylinositol 3-kinase activity
    • 35. Shigematsu H, Iwasaki H, Otsuka T, Ohno Y, Arima F, Niho Y (1997) Role of the vav proto-oncogene product (Vav) in erythropoietin-mediated cell proliferation and phosphatidylinositol 3-kinase activity. J Biol Chem 272:14334-14340
    • (1997) J Biol Chem , vol.272 , pp. 14334-14340
    • Shigematsu, H.1    Iwasaki, H.2    Otsuka, T.3    Ohno, Y.4    Arima, F.5    Niho, Y.6
  • 36
    • 0029985426 scopus 로고    scopus 로고
    • SH3 domain-dependent interaction of the protooncogene product Vav with the focal contact protein zyxin
    • 36. Hobert O, Schilling JW, Beckerle MC, Ullrich A, Jallal B (1996) SH3 domain-dependent interaction of the protooncogene 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
  • 37
    • 0030713407 scopus 로고    scopus 로고
    • Cbl-b, a member of the Sli-1/c-Cbl protein family, inhibits Vav-mediated c-Jun N-terminal kinase activation
    • 37. Bustelo XR, Crespo P, Lopez-Barahona M, Gutkind JS, Barbacid M (1997) Cbl-b, a member of the Sli-1/c-Cbl protein family, inhibits Vav-mediated c-Jun N-terminal kinase activation. Oncogene 15:2511-2520
    • (1997) Oncogene , vol.15 , pp. 2511-2520
    • Bustelo, X.R.1    Crespo, P.2    Lopez-Barahona, M.3    Gutkind, J.S.4    Barbacid, M.5
  • 38
    • 0028114049 scopus 로고
    • Novel signaling pathway suggested by SH3 domain-mediated p95vav/heterogeneous ribonucleoprotein K interaction
    • 38. Hobert O, Jallal B, Schlessinger J, Ullrich A (1994) Novel signaling pathway suggested by SH3 domain-mediated p95vav/heterogeneous ribonucleoprotein K interaction. J Biol Chem 269:20225-20258
    • (1994) J Biol Chem , vol.269 , pp. 20225-20258
    • Hobert, O.1    Jallal, B.2    Schlessinger, J.3    Ullrich, A.4
  • 41
    • 0026535589 scopus 로고
    • Tyrosine phosphorylation of vav proto-oncogene product containing SH2 domain and transcription factor motifs
    • see comments
    • 41. Margolis B, Hu P, Katzav S, Li W, Oliver JM, Ullrich A, Weiss A, Schlessinger J (1992) Tyrosine phosphorylation of vav proto-oncogene product containing SH2 domain and transcription factor motifs [see comments]. Nature 356:71-74
    • (1992) Nature , vol.356 , pp. 71-74
    • Margolis, B.1    Hu, P.2    Katzav, S.3    Li, W.4    Oliver, J.M.5    Ullrich, A.6    Weiss, A.7    Schlessinger, J.8
  • 42
    • 0026633378 scopus 로고
    • Tyrosine phosphorylation of the vav proto-oncogene product in activated B cells
    • 42. Bustelo XR, Barbacid M (1992) Tyrosine phosphorylation of the vav proto-oncogene product in activated B cells. Science 256:1196-1199
    • (1992) Science , vol.256 , pp. 1196-1199
    • Bustelo, X.R.1    Barbacid, M.2
  • 43
    • 0028999988 scopus 로고
    • A functional T-cell receptor signaling pathway is required for p95vav activity
    • 43. Wu J, Katzav S, Weiss A (1995) A functional T-cell receptor signaling pathway is required for p95vav activity. Mol Cell Biol 15:4337-4346
    • (1995) Mol Cell Biol , vol.15 , pp. 4337-4346
    • Wu, J.1    Katzav, S.2    Weiss, A.3
  • 44
    • 0031051776 scopus 로고    scopus 로고
    • Targets of p56(lck) activity in immature thymoblasts: Stimulation of the Ras/Raf/MAPK pathway
    • 44. Lin K, Abraham KM (1997) Targets of p56(lck) activity in immature thymoblasts: stimulation of the Ras/Raf/MAPK pathway. Int Immunol 9:291-306
    • (1997) Int Immunol , vol.9 , pp. 291-306
    • Lin, K.1    Abraham, K.M.2
  • 45
    • 0031569224 scopus 로고    scopus 로고
    • Constitutive tyrosine phosphorylation of the vav proto-oncogene product in MRL/Mp-lpr/lpr mice
    • 45. Mimura T, Minota S, Nojima Y, Morino N, Hamasaki K, Furuya H, Yazaki Y(1997) Constitutive tyrosine phosphorylation of the vav proto-oncogene product in MRL/Mp-lpr/lpr mice. J Immunol 158:2977-2983
    • (1997) J Immunol , vol.158 , pp. 2977-2983
    • Mimura, T.1    Minota, S.2    Nojima, Y.3    Morino, N.4    Hamasaki, K.5    Furuya, H.6    Yazaki, Y.7
  • 46
    • 0028595695 scopus 로고
    • The protein tyrosine kinase ZAP-70 can associate with the SH2 domain of proto-Vav
    • 46. Katzav S, Sutherland M, Packham G, Yi T, Weiss A (1994) The protein tyrosine kinase ZAP-70 can associate with the SH2 domain of proto-Vav. J Biol Chem 269:32579-32785
    • (1994) J Biol Chem , vol.269 , pp. 32579-32785
    • Katzav, S.1    Sutherland, M.2    Packham, G.3    Yi, T.4    Weiss, A.5
  • 47
    • 0030906543 scopus 로고    scopus 로고
    • Regulation of Vav-SLP-76 binding by ZAP-70 and its relevance to TCR zeta/CD3 induction of interleukin-2
    • 47. Raab M, da Silva AJ, Findell PR, Rudd CE (1997) Regulation of Vav-SLP-76 binding by ZAP-70 and its relevance to TCR zeta/CD3 induction of interleukin-2. Immunity 6:155-164
    • (1997) Immunity , vol.6 , pp. 155-164
    • Raab, M.1    Da Silva, A.J.2    Findell, P.R.3    Rudd, C.E.4
  • 48
    • 0030869427 scopus 로고    scopus 로고
    • Identification of two tyrosine phosphoproteins, pp70 and pp68, which interact with phospholipase Cgamma, Grb2, and Vav after B cell antigen receptor activation
    • 48. Fu C, Chan AC (1997) Identification of two tyrosine phosphoproteins, pp70 and pp68, which interact with phospholipase Cgamma, Grb2, and Vav after B cell antigen receptor activation. J Biol Chem 272:27362-27368
    • (1997) J Biol Chem , vol.272 , pp. 27362-27368
    • Fu, C.1    Chan, A.C.2
  • 49
    • 0030820813 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the CD3-epsilon subunit of the T cell antigen receptor mediates enhanced association with phosphatidylinositol 3-kinase in jurkat T cells
    • 49. de Aos I, Metzger MH, Exley M, Dahl CE, Misra S, Zheng D, Varticovski L, Terhorst C, Sancho J (1997) Tyrosine phosphorylation of the CD3-epsilon subunit of the T cell antigen receptor mediates enhanced association with phosphatidylinositol 3-kinase in Jurkat T cells. J Biol Chem 272:25310-25318
    • (1997) J Biol Chem , vol.272 , pp. 25310-25318
    • De Aos, I.1    Metzger, M.H.2    Exley, M.3    Dahl, C.E.4    Misra, S.5    Zheng, D.6    Varticovski, L.7    Terhorst, C.8    Sancho, J.9
  • 50
    • 0029931976 scopus 로고    scopus 로고
    • Two distinct intracytoplasmic regions of the T-cell adhesion molecule CD28 participate in phosphatidylinositol 3-kinase association
    • 50. Pages F, Ragueneau M, Klasen S, Battifora M, Couez D, Sweet R, Truneh A, Ward SG, Olive D (1996) Two distinct intracytoplasmic regions of the T-cell adhesion molecule CD28 participate in phosphatidylinositol 3-kinase association. J Biol Chem 271:9403-9409
    • (1996) J Biol Chem , vol.271 , pp. 9403-9409
    • Pages, F.1    Ragueneau, M.2    Klasen, S.3    Battifora, M.4    Couez, D.5    Sweet, R.6    Truneh, A.7    Ward, S.G.8    Olive, D.9
  • 51
    • 0028910221 scopus 로고
    • CTLA-4 binding to the lipid kinase phosphatidylinositol 3-kinase in T cells
    • 51. Schneider H, Prasad KV, Shoelson SE, Rudd CE (1995) CTLA-4 binding to the lipid kinase phosphatidylinositol 3-kinase in T cells. J Exp Med 181:351-355
    • (1995) J Exp Med , vol.181 , pp. 351-355
    • Schneider, H.1    Prasad, K.V.2    Shoelson, S.E.3    Rudd, C.E.4
  • 52
    • 0032498231 scopus 로고    scopus 로고
    • LAT: The Zap-70 tyrosine kinase substrate that links T cell receptor to cellular activation
    • 52. Zhang W, Sloan-Lancaster J, Kitchen J, Trible RP, Samelson LE (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
  • 53
    • 0028146530 scopus 로고
    • CD28 is associated with and induces the immediate tyrosine phosphorylation and activation of the Tec family kinase ITK/EMT in the human Jurkat leukemic T-cell line
    • 53. August A, Gibson S, Kawakami Y, Kawakami T, Mills GB, Dupont B (1994) CD28 is associated with and induces the immediate tyrosine phosphorylation and activation of the Tec family kinase ITK/EMT in the human Jurkat leukemic T-cell line. Proc Natl Acad Sci USA 91:9347-9351
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 9347-9351
    • August, A.1    Gibson, S.2    Kawakami, Y.3    Kawakami, T.4    Mills, G.B.5    Dupont, B.6
  • 54
    • 0030834178 scopus 로고    scopus 로고
    • Counterregulation by the coreceptors CD19 and CD22 of MAP kinase activation by membrane immunoglobulin
    • 54. Tooze RM, Doody GM, Fearon DT (1997) Counterregulation by the coreceptors CD19 and CD22 of MAP kinase activation by membrane immunoglobulin. Immunity 7:59-67
    • (1997) Immunity , vol.7 , pp. 59-67
    • Tooze, R.M.1    Doody, G.M.2    Fearon, D.T.3
  • 56
    • 0030053270 scopus 로고    scopus 로고
    • Involvement of p72syk kinase, p53/56lyn kinase and phosphatidyl inositol-3 kinase in signal transduction via the human B lymphocyte antigen CD22
    • 56. Tuscano JM, Engel P, Tedder TF, Agarwal A, Kehrl JH (1996) Involvement of p72syk kinase, p53/56lyn kinase and phosphatidyl inositol-3 kinase in signal transduction via the human B lymphocyte antigen CD22. Eur J Immunol 26:1246-1252
    • (1996) Eur J Immunol , vol.26 , pp. 1246-1252
    • Tuscano, J.M.1    Engel, P.2    Tedder, T.F.3    Agarwal, A.4    Kehrl, J.H.5
  • 57
    • 0028597993 scopus 로고
    • Signaling through CD19 activates Vav/mitogen-activated protein kinase pathway and induces formation of a CD19/Vav/phosphatidylinositol 3-kinase complex in human B cell precursors
    • 57. Weng WK, Jarvis L, LeBien TW (1994) Signaling through CD19 activates Vav/mitogen-activated protein kinase pathway and induces formation of a CD19/Vav/phosphatidylinositol 3-kinase complex in human B cell precursors. J Biol Chem 269:32514-32521
    • (1994) J Biol Chem , vol.269 , pp. 32514-32521
    • Weng, W.K.1    Jarvis, L.2    Lebien, T.W.3
  • 58
    • 0031570447 scopus 로고    scopus 로고
    • Role of CD19 tyrosine 391 in synergistic activation of B lymphocytes by coligation of CD19 and membrane Ig
    • 58. Li X, Sandoval D, Freeberg L, Carter RH (1997) Role of CD19 tyrosine 391 in synergistic activation of B lymphocytes by coligation of CD19 and membrane Ig. J Immunol 158:5649-5657
    • (1997) J Immunol , vol.158 , pp. 5649-5657
    • Li, X.1    Sandoval, D.2    Freeberg, L.3    Carter, R.H.4
  • 59
    • 0030667288 scopus 로고    scopus 로고
    • CD19 and CD22 expression reciprocally regulates tyrosine phosphorylation of Vav protein during B lymphocyte signaling
    • 59. Sato S, Jansen PJ, Tedder TF (1997) CD19 and CD22 expression reciprocally regulates tyrosine phosphorylation of Vav protein during B lymphocyte signaling. Proc Natl Acad Sci USA 94:13158-13162
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 13158-13162
    • Sato, S.1    Jansen, P.J.2    Tedder, T.F.3
  • 60
  • 61
    • 0030664126 scopus 로고    scopus 로고
    • Control of B cell development by Ras-mediated activation of Raf
    • 61. Iritani BM, Forbush KA, Farrar MA, Perlmutter RM (1997) Control of B cell development by Ras-mediated activation of Raf. EMBO J 16:7019-7031
    • (1997) EMBO J , vol.16 , pp. 7019-7031
    • Iritani, B.M.1    Forbush, K.A.2    Farrar, M.A.3    Perlmutter, R.M.4
  • 62
    • 0029094609 scopus 로고
    • Abnormal B lymphocyte development, activation, and differentiation in mice that lack or overexpress the CD19 signal transduction molecule
    • 62. Engel P, Zhou LJ, Ord DC, Sato S, Koller B, Tedder TF (1995) Abnormal B lymphocyte development, activation, and differentiation in mice that lack or overexpress the CD19 signal transduction molecule. Immunity 3:39-50
    • (1995) Immunity , vol.3 , pp. 39-50
    • Engel, P.1    Zhou, L.J.2    Ord, D.C.3    Sato, S.4    Koller, B.5    Tedder, T.F.6
  • 63
    • 0029065488 scopus 로고
    • Crucial role of the pre-T-cell receptor alpha gene in development of alpha beta but not gamma delta T cells
    • 63. Fehling HJ, Krotkova A, Saint-Ruf C, von Boehmer H (1995) Crucial role of the pre-T-cell receptor alpha gene in development of alpha beta but not gamma delta T cells. Nature 375:795-798
    • (1995) Nature , vol.375 , pp. 795-798
    • Fehling, H.J.1    Krotkova, A.2    Saint-Ruf, C.3    Von Boehmer, H.4
  • 64
    • 0030966756 scopus 로고    scopus 로고
    • Positive selection of thymocytes bearing alphabeta T cell receptors
    • 64. Marrack P, Kappler J (1997) Positive selection of thymocytes bearing alphabeta T cell receptors. Curr Opin Immunol 9:250-255.
    • (1997) Curr Opin Immunol , vol.9 , pp. 250-255
    • Marrack, P.1    Kappler, J.2
  • 66
    • 0030466893 scopus 로고    scopus 로고
    • Faciogenital dysplasia protein (FGD1) and Vav, two related proteins required for normal embryonic development, are upstream regulators of Rho GTPases
    • 66. Olson MF, Pasteris NG, Gorski JL, Hall A (1996) Faciogenital dysplasia protein (FGD1) and Vav, two related proteins required for normal embryonic development, are upstream regulators of Rho GTPases. Curr Biol 6:1628-1633
    • (1996) Curr Biol , vol.6 , pp. 1628-1633
    • Olson, M.F.1    Pasteris, N.G.2    Gorski, J.L.3    Hall, A.4
  • 67
    • 0015415283 scopus 로고
    • Ligand-induced movement of lymphocyte membrane macromolecules. I. Analysis by immunofluorescence and ultrastructural radioautography
    • 67. Unanue ER, Perkins WD, Karnovsky MJ (1972) Ligand-induced movement of lymphocyte membrane macromolecules. I. Analysis by immunofluorescence and ultrastructural radioautography. J Exp Med 136:885-906
    • (1972) J Exp Med , vol.136 , pp. 885-906
    • Unanue, E.R.1    Perkins, W.D.2    Karnovsky, M.J.3
  • 68
    • 0030221722 scopus 로고    scopus 로고
    • Association of murine splenocyte CD3 complex to the cytoskeleton: Absence of modulation by exogenous fatty acids
    • 68. Peck MD, Li Z, Jy W, Chu AJ, Bourguignon LY(1996) Association of murine splenocyte CD3 complex to the cytoskeleton: absence of modulation by exogenous fatty acids. Cell Biol Int 20:531-537
    • (1996) Cell Biol Int , vol.20 , pp. 531-537
    • Peck, M.D.1    Li, Z.2    Jy, W.3    Chu, A.J.4    Bourguignon, L.Y.5
  • 69
    • 0028961573 scopus 로고
    • Sustained signaling leading to T cell activation results from prolonged T cell receptor occupancy. Role of T cell actin cytoskeleton
    • 69. Valitutti S, Dessing M, Aktories K, Gallati H, Lanzavecchia A (1995) Sustained signaling leading to T cell activation results from prolonged T cell receptor occupancy. Role of T cell actin cytoskeleton. J Exp Med 181:577-584
    • (1995) J Exp Med , vol.181 , pp. 577-584
    • Valitutti, S.1    Dessing, M.2    Aktories, K.3    Gallati, H.4    Lanzavecchia, A.5
  • 70
    • 0030927323 scopus 로고    scopus 로고
    • Making the T cell receptor go the distance: A topological view of T cell activation
    • 70. Shaw AS, Dustin ML (1997) Making the T cell receptor go the distance: a topological view of T cell activation. Immunity 6:361-369
    • (1997) Immunity , vol.6 , pp. 361-369
    • Shaw, A.S.1    Dustin, M.L.2
  • 71
    • 0026600993 scopus 로고
    • Src-related protein tyrosine kinases and T-cell receptor signalling
    • 71. Veillette A, Davidson D (1992) Src-related protein tyrosine kinases and T-cell receptor signalling. Trends Genet 8:61-66
    • (1992) Trends Genet , vol.8 , pp. 61-66
    • Veillette, A.1    Davidson, D.2
  • 72
    • 0031050449 scopus 로고    scopus 로고
    • Molecular interactions in cell adhesion complexes
    • 72. Yamada KM, Geiger B (1997) Molecular interactions in cell adhesion complexes. Curr Opin Cell Biol 9:76-85
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 76-85
    • Yamada, K.M.1    Geiger, B.2
  • 73
    • 0028851581 scopus 로고
    • Tyrosine-phosphorylated T cell receptor zeta chain associates with the actin cytoskeleton upon activation of mature T lymphocytes
    • 73. Rozdzial MM, Malissen B, Finkel TH (1995) Tyrosine-phosphorylated T cell receptor zeta chain associates with the actin cytoskeleton upon activation of mature T lymphocytes. Immunity 3:623-633
    • (1995) Immunity , vol.3 , pp. 623-633
    • Rozdzial, M.M.1    Malissen, B.2    Finkel, T.H.3
  • 74
    • 0029943112 scopus 로고    scopus 로고
    • Regulation of vinculin binding to talin and actin by phosphatidyl-inositol-4-5-bisphosphate
    • 74. Gilmore AP, Burridge K (1996) Regulation of vinculin binding to talin and actin by phosphatidyl-inositol-4-5-bisphosphate. Nature 381:531-535
    • (1996) Nature , vol.381 , pp. 531-535
    • Gilmore, A.P.1    Burridge, K.2
  • 75
    • 0031202421 scopus 로고    scopus 로고
    • Cross-linking of the IgM receptor induces rapid translocation of IgM-assodated Ig alpha, Lyn, and Syk tyrosine kinases to the membrane skeleton
    • 75. Jugloff LS, Jongstra-Bilen J (1997) Cross-linking of the IgM receptor induces rapid translocation of IgM-assodated Ig alpha, Lyn, and Syk tyrosine kinases to the membrane skeleton. J Immunol 159:1096-1106
    • (1997) J Immunol , vol.159 , pp. 1096-1106
    • Jugloff, L.S.1    Jongstra-Bilen, J.2
  • 76
    • 0025187903 scopus 로고
    • Co-capping of ras proteins with surface immunoglobulins in B lymphocytes
    • 76. Graziadei L, Riabowol K, Bar-Sagi D (1990) Co-capping of ras proteins with surface immunoglobulins in B lymphocytes. Nature 347:396-400
    • (1990) Nature , vol.347 , pp. 396-400
    • Graziadei, L.1    Riabowol, K.2    Bar-Sagi, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.