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A complex of Grb2 adaptor protein, Sos exchange factor and a 36 kDa membrane bound tyrosine phosphoprotein is implicated in Ras activation in T cells
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SH3 domains of the adapter molecule Grb-2 complex with two proteins in T cells: The guanine nucleotide exchange protein SOS and a 75-kDa protein that is a substrate for T cell antigen receptor-activated tyrosine kinases
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LAT: The ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation
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0031033292
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Phosphotyrosine-dependent activation of Rac-1 GDP/GTP exchange by the vav proto-oncogene product
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of special interest. This paper, together with Han et al., 1997 [14], demonstrates that Vav has catalytic function as Rac guanine nucleotide exchange factor (GEF) in model cell systems. They illustrate that optimal functioning of Vav1 as a Rac GEF is dependent on Vav tyrosine phosphorylation. The critical tyrosine residues required for Vav GEF function have not been identified so it cannot be assumed that Vav tyrosine phosphorylation will always indicate activation of Vav GEF activity. Regulation of Vav subcellular localisation of Vav may also be important.
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Crespo P, Schuebel KE, Ostrom AA, Gutkind JS, Bustelo XR. Phosphotyrosine-dependent activation of Rac-1 GDP/GTP exchange by the vav proto-oncogene product. of special interest Nature. 385:1997;169-172 This paper, together with Han et al., 1997 [14], demonstrates that Vav has catalytic function as Rac guanine nucleotide exchange factor (GEF) in model cell systems. They illustrate that optimal functioning of Vav1 as a Rac GEF is dependent on Vav tyrosine phosphorylation. The critical tyrosine residues required for Vav GEF function have not been identified so it cannot be assumed that Vav tyrosine phosphorylation will always indicate activation of Vav GEF activity. Regulation of Vav subcellular localisation of Vav may also be important.
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Nature
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Crespo, P.1
Schuebel, K.E.2
Ostrom, A.A.3
Gutkind, J.S.4
Bustelo, X.R.5
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14
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0031034050
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Lck regulates Vav activation of members of the Rho family of GTPases
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of special interest. This paper, together with Crespo et al., 1997 [13], demonstrates that Vav has catalytic function as Rac guanine nucleotide exchange factor (GEF) in model cell systems. They illustrate that optimal functioning of Vav1 as a Rac GEF is dependent on Vav tyrosine phosphorylation. The critical tyrosine residues required for Vav GEF function have not been identified so it cannot be assumed that Vav tyrosine phosphorylation will always indicate activation of Vav GEF activity. Regulation of Vav subcellular localisation of Vav may also be important.
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Han J, Das B, Wei W, vanAelst L, Mosteller RD, Khosravi-Far R, Westwick JK, Channing JD, Broek D. Lck regulates Vav activation of members of the Rho family of GTPases. of special interest Mol Cell Biol. 17:1997;1346-1353 This paper, together with Crespo et al., 1997 [13], demonstrates that Vav has catalytic function as Rac guanine nucleotide exchange factor (GEF) in model cell systems. They illustrate that optimal functioning of Vav1 as a Rac GEF is dependent on Vav tyrosine phosphorylation. The critical tyrosine residues required for Vav GEF function have not been identified so it cannot be assumed that Vav tyrosine phosphorylation will always indicate activation of Vav GEF activity. Regulation of Vav subcellular localisation of Vav may also be important.
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Mol Cell Biol
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Han, J.1
Das, B.2
Wei, W.3
Vanaelst, L.4
Mosteller, R.D.5
Khosravi-Far, R.6
Westwick, J.K.7
Channing, J.D.8
Broek, D.9
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15
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Defective signalling through the T- And B-cell antigen receptors in lymphoid cells lacking the vav proto-oncogene
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Zhang R, Alt FW, Davidson L, Orkin SH, Swat W. Defective signalling through the T- and B-cell antigen receptors in lymphoid cells lacking the vav proto-oncogene. Nature. 374:1995;470-473.
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Zhang, R.1
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Tarakhovsky A, Turner M, Schaal S, Mee PJ, Duddy LP, Rajewsky K, Tybulewicz VLJ. Defective antigen receptor-mediated proliferation of B and T cells in the absence of Vav. Nature. 374:1995;467-470.
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Turner M, Mee PJ, Walters AE, Quinn ME, Mellor AL, Zamoyska R, Tybulewicz VLJ. A requirement for the Rho-family GTP exchange factor Vav in positive and negative selection of thymocytes. Immunity. 7:1997;451-460.
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19
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0028169441
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The role of p21ras in CD28 signal transduction: Triggering of CD28 with antibodies, but not the ligand B7-1 activates p21ras
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Nunes JA, Collette Y, Truneh A, Olive D, Cantrell DA. The role of p21ras in CD28 signal transduction: Triggering of CD28 with antibodies, but not the ligand B7-1 activates p21ras. J Exp Med. 180:1994;1067-1076.
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Nunes, J.A.1
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Cantrell, D.A.5
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21
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0029658306
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P95vav associates with tyrosine-phosphorylated SLP-76 in antigen-stimulated T cells
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of special interest. This study, together with Nunes et al., 1994 [20], shows that Vav tyrosine phosphorylation can be induced by triggering of CD28 with its physiological ligands B7-1 and B7-2. Initial observations were in the Jurkat cell line but more recent work has confirmed this result in T cell clones and has shown that contact between T cells and antigen-presenting cells in the absence of TCR ligation can stimulate Vav tyrosine phosphorylation.
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Tuosto L, Michel F, Acuto O. p95vav associates with tyrosine-phosphorylated SLP-76 in antigen-stimulated T cells. of special interest J Exp Med. 184:1996;1161-1166 This study, together with Nunes et al., 1994 [20], shows that Vav tyrosine phosphorylation can be induced by triggering of CD28 with its physiological ligands B7-1 and B7-2. Initial observations were in the Jurkat cell line but more recent work has confirmed this result in T cell clones and has shown that contact between T cells and antigen-presenting cells in the absence of TCR ligation can stimulate Vav tyrosine phosphorylation.
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J Exp Med
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Tuosto, L.1
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0028597993
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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
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Weng WK, Jarvis L, LeBien TW. 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. 269:1994;32514-32521.
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0030820924
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A comparative analysis of the phosphoinositide binding specificity of pleckstrin homology domains
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25
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Role of substrates and products of PI3-kinase in regulating activation of Rac-related guanosine triphosphatases by Vav
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of outstanding interest. This provides evidence for the dual regulation of the Rac-specific guanine nucleotide exchange activity of Vav by phsphatidylinositol 3-kinase (PI3K) and PTK. Phosphatidylinositol-3,4,5-triphosphates, products of PI3K activity, bind to the pleckstrin homology domain of Vav and enhance its phosphorylation and activation by p56lck.
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Han J, Luby-Phelps K, Das K, Shu X, Xia Y, Mosteller RD, Krishna UM, Falck JR, White MA, Broek D. Role of substrates and products of PI3-kinase in regulating activation of Rac-related guanosine triphosphatases by Vav. of outstanding interest Science. 279:1998;558-560 This provides evidence for the dual regulation of the Rac-specific guanine nucleotide exchange activity of Vav by phsphatidylinositol 3-kinase (PI3K) and PTK. Phosphatidylinositol-3,4,5-triphosphates, products of PI3K activity, bind to the pleckstrin homology domain of Vav and enhance its phosphorylation and activation by p56lck.
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Science
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Han, J.1
Luby-Phelps, K.2
Das, K.3
Shu, X.4
Xia, Y.5
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Krishna, U.M.7
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Phosphatidylinositol 3-kinase signals activate a selective subset of Rac/Rho-dependent effector pathways
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Reif K, Nobes CD, Thomas G, Hall A, Cantrell DA. Phosphatidylinositol 3-kinase signals activate a selective subset of Rac/Rho-dependent effector pathways. Curr Biol. 6:1996;1445-1455.
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Reif, K.1
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Rao A, Luo C, Hogan PG. Transcription factors of the NFAT family: regulation and function. Annu Rev Immunol. 15:1997;707-747.
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Hogan, P.G.3
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P21ras and calcineurin synergize to regulate the nuclear factor of activated T cells
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Woodrow M, Clipstone NA, Cantrell D. p21ras and calcineurin synergize to regulate the nuclear factor of activated T cells. J Exp Med. 178:1993;1517-1522.
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Involvement of p21ras distinguishes positive and negative selection in thymocytes
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Swan KA, Alberola-Ila J, Gross JA, Appleby MW, Forbush KA, Thomas JF, Perlmutter RM. Involvement of p21ras distinguishes positive and negative selection in thymocytes. EMBO. 14:1995;276-285.
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Swan, K.A.1
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Thomas, J.F.6
Perlmutter, R.M.7
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0030812812
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Maintenance of human T cell anergy: Blocking of IL-2 gene transcription by activated Rap1
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of outstanding interest. This study suggests Rap1 both as a negative regulator of TCR-mediated IL-2 gene transcription and as being responsible for maintaining T cell anergy by inhibiting IL-2 production. High levels of activated Rap1 are found in anergic T cells, and forced overexpression of Rap1 in Jurkat cells prevents IL-2 gene induction. The proposed mechanisms for the negative regulatory role of Rap1 is that it competitively inhibits interactions between Ras and Raf-1.
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Boussiotis VA, Freeman GJ, Berezovskaya A, Barber DL, Nadler LM. Maintenance of human T cell anergy: blocking of IL-2 gene transcription by activated Rap1. of outstanding interest Science. 278:1997;124-128 This study suggests Rap1 both as a negative regulator of TCR-mediated IL-2 gene transcription and as being responsible for maintaining T cell anergy by inhibiting IL-2 production. High levels of activated Rap1 are found in anergic T cells, and forced overexpression of Rap1 in Jurkat cells prevents IL-2 gene induction. The proposed mechanisms for the negative regulatory role of Rap1 is that it competitively inhibits interactions between Ras and Raf-1.
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Science
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Boussiotis, V.A.1
Freeman, G.J.2
Berezovskaya, A.3
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P21ras couples the T cell antigen receptor to Extracellular Signal-regulated Kinase 2 in T lymphocytes
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Izquierdo M, Leevers SJ, Marshall C, Cantrell DA. p21ras couples the T cell antigen receptor to Extracellular Signal-regulated Kinase 2 in T lymphocytes. J Exp Med. 178:1993;1199-1208.
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0031026474
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Distinct Ras effector pathways are involved in FcεR1 regulation of the transcriptional activity of Elk-1 and NFAT in mast cells
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of special interest. This paper, together with that of Genot et al., 1996 [36], shows that multiple Ras effector pathways are involved in the regulation of nuclear factor of activated T cells (NFAT) transcription factors in T cells and mast cells. Both studies provide evidence that Rac signals are necessary, although not sufficient, for NFAT activation.
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Turner H, Cantrell DA. Distinct Ras effector pathways are involved in FcεR1 regulation of the transcriptional activity of Elk-1 and NFAT in mast cells. of special interest J Exp Med. 185:1997;43-57 This paper, together with that of Genot et al., 1996 [36], shows that multiple Ras effector pathways are involved in the regulation of nuclear factor of activated T cells (NFAT) transcription factors in T cells and mast cells. Both studies provide evidence that Rac signals are necessary, although not sufficient, for NFAT activation.
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J Exp Med
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Turner, H.1
Cantrell, D.A.2
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0029777285
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Multiple p21ras effector pathways regulate nuclear factor of activated T cells
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of special interest. This paper, together with that of Turner and Cantrell, 1997 [35], shows that multiple Ras effector pathways are involved in the regulation of nuclear factor of activated T cells (NFAT) transcription factors in T cells and mast cells. Both studies provide evidence that Rac signals are necessary, although not sufficient, for NFAT activation.
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Genot E, Cleverley S, Henning S, Cantrell DA. Multiple p21ras effector pathways regulate nuclear factor of activated T cells. of special interest EMBO J. 15:1996;3923-3933 This paper, together with that of Turner and Cantrell, 1997 [35], shows that multiple Ras effector pathways are involved in the regulation of nuclear factor of activated T cells (NFAT) transcription factors in T cells and mast cells. Both studies provide evidence that Rac signals are necessary, although not sufficient, for NFAT activation.
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EMBO J
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Westwick JK, Lambert QT, Clark GJ, Symons M, Van Aelst L, Pestell RG, Der CJ. Rac regulation of transformation, gene expression, and actin organization by multiple PAK-independent pathways. Mol Cell Biol. 17:1997;1324-1335.
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Westwick, J.K.1
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Rac and Cdc42 induce actin polymerization and G1 cell cycle progression independently of p65PAK and the JNK/SAPK MAP kinase cascade
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Lamarche N, Tapon N, Stowers L, Burbelo PD, Aspenstrom P, Bridges T, Chant J, Hall A. Rac and Cdc42 induce actin polymerization and G1 cell cycle progression independently of p65PAK and the JNK/SAPK MAP kinase cascade. Cell. 87:1997;519-529.
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Lamarche, N.1
Tapon, N.2
Stowers, L.3
Burbelo, P.D.4
Aspenstrom, P.5
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Hall, A.8
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41
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Aspects of lymphocyte developmental biology
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Von Boehmer H. Aspects of lymphocyte developmental biology. Immunol Today. 18:1997;260-262.
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Von Boehmer, H.1
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42
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0030946814
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The GTPase Rho has a critical regulatory role in thymocyte development
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of special interest. Using a transgenic model this study, together with Galandrini et al., 1997 [43], documents the role for Rho in thymocyte development and show that this GTPase has important functions in controlling cell survival in early thymocyte progenitors. Note that the phenotype of thymi lacking Rho function most closely resembles the thymic phenotype of mice lacking components of the IL-7 receptor complex, implying that Rho regulates cell survival signals induced by IL-7.
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Henning S, Galandrini R, Hall A, Cantrell DA. The GTPase Rho has a critical regulatory role in thymocyte development. of special interest EMBO J. 16:1997;2397-2407 Using a transgenic model this study, together with Galandrini et al., 1997 [43], documents the role for Rho in thymocyte development and show that this GTPase has important functions in controlling cell survival in early thymocyte progenitors. Note that the phenotype of thymi lacking Rho function most closely resembles the thymic phenotype of mice lacking components of the IL-7 receptor complex, implying that Rho regulates cell survival signals induced by IL-7.
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(1997)
EMBO J
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Henning, S.1
Galandrini, R.2
Hall, A.3
Cantrell, D.A.4
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43
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0030806477
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Different functions of the GTPase Rho in pro-thymocytes and late pre-T cells
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of special interest. Using a transgenic model this study, together with Henning et al., 1997 [42], documents the role for Rho in thymocyte development and show that this GTPase has important functions in controlling cell survival in early thymocyte progenitors. Note that the phenotype of thymi lacking Rho function most closely resembles the thymic phenotype of mice lacking components of the IL-7 receptor complex, implying that Rho regulates cell survival signals induced by IL-7.
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Galandrini R, Henning SW, Cantrell DA. Different functions of the GTPase Rho in pro-thymocytes and late pre-T cells. of special interest Immunity. 7:1997;163-174 Using a transgenic model this study, together with Henning et al., 1997 [42], documents the role for Rho in thymocyte development and show that this GTPase has important functions in controlling cell survival in early thymocyte progenitors. Note that the phenotype of thymi lacking Rho function most closely resembles the thymic phenotype of mice lacking components of the IL-7 receptor complex, implying that Rho regulates cell survival signals induced by IL-7.
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(1997)
Immunity
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Galandrini, R.1
Henning, S.W.2
Cantrell, D.A.3
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44
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0028929565
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Lymphopenia in interleukin (IL)-7 gene-deleted mice identifies IL-7 as a nonredundant cytokine
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Von Freeden-Jeffry U, Vieira P, Lucian LA, McNeil T, Burdach SEG, Murray R. Lymphopenia in interleukin (IL)-7 gene-deleted mice identifies IL-7 as a nonredundant cytokine. J Exp Med. 181:1995;1519-1526.
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Von Freeden-Jeffry, U.1
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Lucian, L.A.3
McNeil, T.4
Burdach, S.E.G.5
Murray, R.6
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45
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Defects in B lymphocyte maturation and T lymphocyte activation in mice lacking JAK3
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Thomis DC, Gurniak CB, Tivol E, Sharpe AH, Berg LJ. Defects in B lymphocyte maturation and T lymphocyte activation in mice lacking JAK3. Science. 270:1995;794-797.
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Science
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Thomis, D.C.1
Gurniak, C.B.2
Tivol, E.3
Sharpe, A.H.4
Berg, L.J.5
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46
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Early lymphocyte expansion is severely impaired in interleukin 7 receptor-deficient mice
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Peschon JJ, Morrissey PJ, Grabstein KH, Ramsdell FJ, Maraskovsky E, Gliniak BC, Park LS, Ziegler SF, Williams DE, Ware CB, et al. Early lymphocyte expansion is severely impaired in interleukin 7 receptor-deficient mice. J Exp Med. 180:1994;1955-1960.
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Peschon, J.J.1
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Gliniak, B.C.6
Park, L.S.7
Ziegler, S.F.8
Williams, D.E.9
Ware, C.B.10
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47
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0028925778
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Defective lymphoid development in mice lacking expression of the common cytokine receptor γ chain
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Cao X, Shores EW, Hu-Li J, Anver M, Kelsall BL, Russell SM, Drago J, Noguchi M, Grinberg A, Bloom ET, et al. Defective lymphoid development in mice lacking expression of the common cytokine receptor γ chain. Immunity. 2:1995;223-238.
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Cao, X.1
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Drago, J.7
Noguchi, M.8
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Bloom, E.T.10
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49
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Bcl-2 rescues T lymphopoiesis in interleukin-7 receptor-deficient mice
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Akashi K, Kondo M, von Freeden-Jeffry U, Murray R, Weissman I. Bcl-2 rescues T lymphopoiesis in interleukin-7 receptor-deficient mice. Cell. 89:1997;1033-1041.
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Akashi, K.1
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50
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0030874326
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The earliest T lineage-commited cells depend on IL-7 for Bcl-2 expression and normal cell cycle progression
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Von Freeden-Jeffry U, Solvason N, Howard M, Murray R. The earliest T lineage-commited cells depend on IL-7 for Bcl-2 expression and normal cell cycle progression. Immunity. 7:1997;147-154.
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Von Freeden-Jeffry, U.1
Solvason, N.2
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51
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Rho prevents apoptosis through Bcl-2 expression: Implications for interleukin-2 receptor signal transduction
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Gomez J, Martinez-A C, Giry M, Garcia A, Rebollo A. Rho prevents apoptosis through Bcl-2 expression: implications for interleukin-2 receptor signal transduction. Eur J Immunol. 27:1997;2793-2799.
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52
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0031042493
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Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton
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Tapon N, Hall A. Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton. Curr Opin Cell Biol. 9:1997;86-92.
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Tapon, N.1
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53
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0029008280
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Regulation of the polarization of T cells towards antigen-presenting cells by Ras-related GTPase Cdc42
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Stowers L, Yelon D, Berg LJ, Chant J. Regulation of the polarization of T cells towards antigen-presenting cells by Ras-related GTPase Cdc42. Proc Natl Acad Sci USA. 92:1995;5027-5031.
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Yelon, D.2
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54
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Disease mechanism: Unravelling Wiskott-Aldrich syndrome
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Kirchhausen T, Rosen FS. Disease mechanism: unravelling Wiskott-Aldrich syndrome. Curr Biol. 6:1996;676-678.
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Rosen, F.S.2
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55
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0028961293
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Rho, Rac and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibres, lamellipodia and filopodia
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Nobes C, Hall A. Rho, Rac and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibres, lamellipodia and filopodia. Cell. 81:1995;53-62.
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Nobes, C.1
Hall, A.2
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56
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0026650402
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ADP-ribosylation of the ras-related, GTP-binding protein rhoA inhibits lymphocyte-mediated cytotoxicity
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Lang P, Guizani L, Vitte-Mony I, Stancout R, Dorseuil O, Gacon G, Bertoglio J. ADP-ribosylation of the ras-related, GTP-binding protein rhoA inhibits lymphocyte-mediated cytotoxicity. J Biol Chem. 267:1992;11677-11680.
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Lang, P.1
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Stancout, R.4
Dorseuil, O.5
Gacon, G.6
Bertoglio, J.7
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57
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0030059222
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Role of Rho in chemoattractant-activated leukocyte adhesion through integrins
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of special interest. A further example for Rho function in lymphocyte biology. This paper shows that agonist stimulation of chemoattractant receptors in lymphocytes activates the nucleotide exchange of Rho and that inactivation of Rho blocks agonist-induced lymphocyte adhesion through integrin receptors. The authors suggest a role for Rho in the signalling pathways, emerging from chemoattractant receptors, that trigger rapid adhesion of leukocytes.
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Laudanna C, Campbell JJ, Butcher EC. Role of Rho in chemoattractant-activated leukocyte adhesion through integrins. of special interest Science. 271:1996;981-983 A further example for Rho function in lymphocyte biology. This paper shows that agonist stimulation of chemoattractant receptors in lymphocytes activates the nucleotide exchange of Rho and that inactivation of Rho blocks agonist-induced lymphocyte adhesion through integrin receptors. The authors suggest a role for Rho in the signalling pathways, emerging from chemoattractant receptors, that trigger rapid adhesion of leukocytes.
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(1996)
Science
, vol.271
, pp. 981-983
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Laudanna, C.1
Campbell, J.J.2
Butcher, E.C.3
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58
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0032570874
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Costimulation through CD28 suppresses T cell receptor-dependent activation of the Ras-like small GTPase Rap1 in human T lymphocytes
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of special interest. This provides further evidence for a model which envisions Rap1 as a negative regulatory element in T cell activation. This paper shows that signals generated by the costimulatory molecule CD28 are able to inhibit TCR-mediated activation of Rap1, suggesting that subversion of Rap1 activation is required for optimal T cell responses
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Reedquist KA, Bos JL. Costimulation through CD28 suppresses T cell receptor-dependent activation of the Ras-like small GTPase Rap1 in human T lymphocytes. of special interest J Biol Chem. 273:1998;4944-4949 This provides further evidence for a model which envisions Rap1 as a negative regulatory element in T cell activation. This paper shows that signals generated by the costimulatory molecule CD28 are able to inhibit TCR-mediated activation of Rap1, suggesting that subversion of Rap1 activation is required for optimal T cell responses.
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J Biol Chem
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Reedquist, K.A.1
Bos, J.L.2
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59
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0028264812
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C3G, a guanine nucleotide-releasing protein expressed ubiquitously, binds to the Src homology 3 domains of CRK and GRB2/ASH proteins
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Tanaka S, Morishita T, Hashimoto Y, Hattori S, Nakamura S, Shibuya M, Matuoka K, Takenawa T, Kurata T, Nagashima K, Matsuda M. C3G, a guanine nucleotide-releasing protein expressed ubiquitously, binds to the Src homology 3 domains of CRK and GRB2/ASH proteins. Proc Natl Acad Sci USA. 91:1994;3443-3447.
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Tanaka, S.1
Morishita, T.2
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Hattori, S.4
Nakamura, S.5
Shibuya, M.6
Matuoka, K.7
Takenawa, T.8
Kurata, T.9
Nagashima, K.10
Matsuda, M.11
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60
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0028881018
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Identification of Rap1 as a target for the Crk SH3 domain-binding guanine nucleotide-releasing factor C3G
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Gotoh T, Hattori S, Nakamura S, Kitayama H, Noda M, Takai Y, Kaibuchi K, Matsui H, Hatase O, Takahashi H, et al. Identification of Rap1 as a target for the Crk SH3 domain-binding guanine nucleotide-releasing factor C3G. Mol Cell Biol. 15:1995;6746-6753.
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Gotoh, T.1
Hattori, S.2
Nakamura, S.3
Kitayama, H.4
Noda, M.5
Takai, Y.6
Kaibuchi, K.7
Matsui, H.8
Hatase, O.9
Takahashi, H.10
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61
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0024600222
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A ras-related gene with transformation suppressor activity
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Kitayama H, Sugimoto Y, Matsuzaki T, Ikawa Y, Noda M. A ras-related gene with transformation suppressor activity. Cell. 56:1989;77-84.
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(1989)
Cell
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Kitayama, H.1
Sugimoto, Y.2
Matsuzaki, T.3
Ikawa, Y.4
Noda, M.5
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62
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0023721977
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Human cDNA rap1 and rap2 homologous to the Drosophila gene Dras3 encode proteins closely related ras in the 'effector' region
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Pizon V, Chardin P, Lerosey I, Olofsson B, Tavitian A. Human cDNA rap1 and rap2 homologous to the Drosophila gene Dras3 encode proteins closely related ras in the 'effector' region. Oncogene. 3:1988;201-204.
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Oncogene
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Pizon, V.1
Chardin, P.2
Lerosey, I.3
Olofsson, B.4
Tavitian, A.5
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63
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0030963439
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CAMP activates MAP kinase and Elk-1 through a B-raf- And rap1-dependent pathway
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of special interest. This report suggests that Rap1 may also have positive signalling effects. In PC12 cells cAMP is able to induce neuronal differentiation and activation of the Elk-1 transcription factor via the activation of the mitogen-activated protein kinase cascade which is dependent on the expression of B-Raf and Rap1. In B-Raf expressing cells Rap1 can therefore be envisioned as a selective activator of B-Raf and an inhibitor of Raf-1.
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Vossler MR, Yao H, York RD, Pan M-G, Rim CS, Stork PJS. cAMP activates MAP kinase and Elk-1 through a B-raf- and rap1-dependent pathway. of special interest Cell. 89:1997;73-82 This report suggests that Rap1 may also have positive signalling effects. In PC12 cells cAMP is able to induce neuronal differentiation and activation of the Elk-1 transcription factor via the activation of the mitogen-activated protein kinase cascade which is dependent on the expression of B-Raf and Rap1. In B-Raf expressing cells Rap1 can therefore be envisioned as a selective activator of B-Raf and an inhibitor of Raf-1.
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(1997)
Cell
, vol.89
, pp. 73-82
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-
Vossler, M.R.1
Yao, H.2
York, R.D.3
Pan M-G4
Rim, C.S.5
Stork, P.J.S.6
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