Flesh and blood: The story of Vav1, a gene that signals in hematopoietic cells but can be transforming in human malignancies

Cancer Letters

Volumn 255, Issue 2, 2007, Pages 241-254

  Katzav, Shulamit ^a  

^a HEBREW UNIVERSITY OF JERUSALEM   (Israel)

Author keywords

Cancer; Neuroblastoma; Pancreas; Vav1

Indexed keywords

CRK LIKE PROTEIN; GROWTH FACTOR RECEPTOR BOUND PROTEIN 2; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE KINASE 4; PROTEIN SHC; RAC PROTEIN; RAS PROTEIN; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; T LYMPHOCYTE RECEPTOR; TRANSCRIPTION FACTOR NFAT; TYROSINE;

ARTICLE; CELL MATURATION; CHRONIC LYMPHATIC LEUKEMIA; GENE ACTIVATION; HEMATOPOIETIC CELL; HUMAN; MALIGNANT TRANSFORMATION; MELANOMA; NEUROBLASTOMA; NONHUMAN; ONCOGENE; PANCREAS ADENOCARCINOMA; PRIORITY JOURNAL; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION; T LYMPHOCYTE ACTIVATION; VAV1 GENE;

CELL TRANSFORMATION, NEOPLASTIC; HEMATOPOIETIC STEM CELLS; HUMANS; NEOPLASMS; PROTO-ONCOGENE PROTEINS C-VAV; SIGNAL TRANSDUCTION;

MAMMALIA;

EID: 34547957796     PISSN: 03043835     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.canlet.2007.04.015     Document Type: Article

References (140)

1. Sjoblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., and Velculescu V.E. The consensus coding sequences of human breast and colorectal cancers. Science 314 (2006) 268-274
2. Shih C., Shilo B.Z., Goldfarb M.P., Dannenberg A., and Weinberg R.A. Passage of phenotypes of chemically transformed cells via transfection of DNA and chromatin. Proc. Natl. Acad. Sci. USA 76 (1979) 5714-5718
3. Perucho M., Goldfarb M., Shimizu K., Lama C., Fogh J., and Wigler M. Human-tumor-derived cell lines contain common and different transforming genes. Cell 27 (1981) 467-476
4. Pulciani S., Santos E., Lauver A.V., Long L.K., Robbins K.C., and Barbacid M. Oncogenes in human tumor cell lines: molecular cloning of a transforming gene from human bladder carcinoma cells. Proc. Natl. Acad. Sci. USA 79 (1982) 2845-2849
5. Katzav S., Martin-Zanca D., and Barbacid M. vav, a novel human oncogene derived from a locus ubiquitously expressed in hematopoietic cells. EMBO J. 8 (1989) 2283-2290
6. Katzav S., Cleveland J.L., Heslop H.E., and Pulido D. Loss of the aminoterminal helix-loop-helix domain of the vav proto-oncogene activates its transforming potential. Mol. Cell. Biol. 11 (1991) 1912-1920
7. Coppola J., Bryant S., Koda T., Conway D., and Barbacid M. Mechanism of activation of the vav protooncogene. Cell Growth Differ. 2 (1991) 95-105
8. Henske E.P., Short M.P., Jozwiak S., Bovey C.M., Ramlakhan S., Haines J.L., and Kwiatkowski D.J. Identification of VAV2 on 9q34 and its exclusion as the tuberous sclerosis gene TSC1. Ann. Hum. Genet. 59 (1995) 25-37
9. Movilla N., and Bustelo X.R. Biological and regulatory properties of Vav-3, a new member of the Vav family of oncoproteins. Mol. Cell. Biol. 19 (1999) 7870-7885
10. Dekel I., Russek N., Jones T., Mortin M.A., and Katzav S. Identification of the Drosophila melanogaster homologue of the mammalian signal transducer protein, Vav. FEBS Lett. 472 (2000) 99-104
11. Yoo A.S., and Greenwald I. LIN-12/Notch activation leads to microRNA-mediated down-regulation of Vav in C. elegans. Science 310 (2005) 1330-1333
12. Norman K.R., Fazzio R.T., Mellem J.E., Espelt M.V., Strange K., Beckerle M.C., and Maricq A.V. The Rho/Rac-family guanine nucleotide exchange factor VAV-1 regulates rhythmic behaviors in C. elegans. Cell 123 (2005) 119-132
13. Katzav S. Vav1 - an oncogene that regulates specific transcriptional activation of T cells. Blood 103 (2004) 2443-2451
14. Tybulewicz V.L. Vav-family proteins in T-cell signalling. Curr. Opin. Immunol. 17 (2005) 267-274
15. Bustelo X.R. Regulatory and signaling properties of the Vav family. Mol. Cell. Biol. 20 (2000) 1461-1477
16. Margolis B., Hu P., Katzav S., Li W., Oliver J.M., Ulrich A., Weiss A., and Schlessinger J. Tyrosine phosphorylation of vav; a proto-oncogene combining SH2 and SH3 domains with motifs found in transcription factors. Nature 356 (1992) 71-74
17. Bustelo X.R., and Barbacid M. Tyrosine phosphorylation of the vav proto-oncogene product in activated B cells. Science 256 (1992) 1196-1199
18. Manetz T.S., Gonzalez-Espinosa C., Arudchandran R., Xirasagar S., Tybulewicz V., and Rivera J. Vav1 regulates phospholipase cgamma activation and calcium responses in mast cells. Mol. Cell. Biol. 21 (2001) 3763-3774
19. Reynolds L.F., Smyth L.A., Norton T., Freshney N., Downward J., Kioussis D., and 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
20. Evans G.A., Howard O.M., Erwin R., and Farrar W.L. Interleukin-2 induces tyrosine phosphorylation of the vav proto-oncogene product in human T cells: lack of requirement for the tyrosine kinase lck. Biochem. J. 294 (1993) 339-342
21. Vicente-Manzanares M., Cruz-Adalia A., Martin-Cofreces N.B., Cabrero J.R., Dosil M., Alvarado-Sanchez B., Bustelo X.R., and Sanchez-Madrid F. Control of lymphocyte shape and the chemotactic response by the GTP exchange factor Vav. Blood 105 (2005) 3026-3034
22. Zheng L., Sjolander A., Eckerdal J., and Andersson T. Antibody-induced engagement of beta 2 integrins on adherent human neutrophils triggers activation of p21ras through tyrosine phosphorylation of the protooncogene product Vav. Proc. Natl. Acad. Sci. USA 93 (1996) 8431-8436
23. Cichowski K., Brugge J.S., and Brass L.F. Thrombin receptor activation and integrin engagement stimulate tyrosine phosphorylation of the proto-oncogene product, p95vav, in platelets. J. Biol. Chem. 271 (1996) 7544-7550
24. Alai M., Mui A.L., Cutler R.L., Bustelo X.R., Barbacid M., and Krystal G. Steel factor stimulates the tyrosine phosphorylation of the proto-oncogene product, p95vav, in human hemopoietic cells. J. Biol. Chem. 267 (1992) 18021-18025
25. Wu J., Katzav S., and Weiss A. A functional T-cell receptor signaling pathway is required for p95vav activity. Mol. Cell. Biol. 15 (1995) 4337-4346
26. Clipstone N.A., and Crabtree G.R. Identification of calcineurin as a key signalling enzyme in T-lymphocyte activation. Nature 357 (1992) 695-697
27. Masuda E.S., Imamura R., Amasaki Y., Arai K., and Arai N. Signalling into the T-cell nucleus: NFAT regulation. Cell. Signal. 10 (1998) 599-611
28. Rao A., Luo C., and Hogan P.G. Transcription factors of the NFAT family: regulation and function. Annu. Rev. Immunol. 15 (1997) 707-747
29. Marth J.D., Lewis D.B., Wilson C.B., Gearn M.E., Krebs E.G., and Perlmutter R.M. Regulation of pp56lck during T-cell activation: functional implications for the src-like protein tyrosine kinases. EMBO J. 6 (1987) 2727-2734
30. Samelson L.E., Phillips A.F., Luong E.T., and Klausner R.D. Association of the fyn protein-tyrosine kinase with the T-cell antigen receptor. Proc. Natl. Acad. Sci. USA 87 (1990) 4358-4362
31. Rozdzial M.M., Malissen B., and Finkel T.H. Tyrosine-phosphorylated T cell receptor zeta chain associates with the actin cytoskeleton upon activation of mature T lymphocytes. Immunity 5 (1995) 623-633
32. Neumeister E.N., Zhu Y., Richard S., Terhorst C., Chan A.C., and Shaw A.S. Binding of ZAP-70 to phosphorylated T-cell receptor zeta and eta enhances its autophosphorylation and generates specific binding sites for SH2 domain-containing proteins. Mol. Cell. Biol. 15 (1995) 3171-3178
33. Crespo P., Schuebel K.E., Ostrom A.A., Gutkind J.S., and Bustelo X.R. Phosphotyrosine-dependent activation of Rac-1 GDP/GTP exchange by the vav proto-oncogene product. Nature 385 (1997) 169-172
34. Hornstein I., Alcover A., and Katzav S. Vav proteins, masters of the world of cytoskeleton organization. Cell. Signal. 16 (2004) 1-11
35. Holsinger L.J., Graef I.A., Swat W., Chi T., Bautista D.M., Davidson L., Lewis R.S., Alt F.W., and Crabtree G.R. Defects in actin-cap formation in Vav-deficient mice implicate an actin requirement for lymphocyte signal transduction. Curr. Biol. 8 (1998) 563-572
36. Fischer K.D., Kong Y.Y., Nishina H., Tedford K., Marengere L.E., Kozieradzki I., Sasaki T., Starr M., Chan G., Gardener S., Nghiem M.P., Bouchard D., Barbacid M., Bernstein A., and Penninger J.M. Vav is a regulator of cytoskeletal reorganization mediated by the T-cell receptor. Curr. Biol. 8 (1998) 554-562
37. Lewis C.M., Broussard C., Czar M.J., and Schwartzberg P.L. Tec kinases: modulators of lymphocyte signalling and development. Curr. Opin. Immunol. 13 (2001) 317-325
38. Reynolds L.F., de Bettignies C., Norton T., Beeser A., Chernoff J., and Tybulewicz V.L.J. Vav1 transduces T cell receptor signals to the activation of the Ras/ERK pathway via LAT, Sos and RasGRP1. J. Biol. Chem. 279 (2004) 18239-18246
39. Caloca M.J., Zugaza J.L., and Bustelo X.R. Exchange factors of the RasGRP family mediate Ras activation in the Golgi. J. Biol. Chem. 278 (2003) 33465-33473
40. Michel F., Mangino G., Attal-Bonnefoy G., Tuosto L., Alcover A., Roumier A., Olive D., and Acuto O. J. CD28 utilizes Vav-1 to enhance TCR-proximal signaling and NF-AT activation. Immunology 165 (2000) 3820-3829
41. Bluestone J.A. New perspectives of CD28-B7-mediated T cell costimulation. Immunity 2 (1995) 555-559
42. Viola A., and Lanzavecchia A. T cell activation determined by T cell receptor number and tunable thresholds. Science 273 (1996) 104-106
43. Shahinian A., Pfeffer K., Lee K.P., Kundig T.M., Kishihara K., Wakeham A., Kawai K., Ohashi P.S., Thompson C.B., and Mak T.W. Science 261 (1993) 609-612
44. Dennehy K.M., Elias F., Na S.Y., Fischer K.D., Hunig T., and Luhder F. Mitogenic CD28 Signals Require the Exchange Factor Vav1 to Enhance TCR Signaling at the SLP-76-Vav-Itk Signalosome. J. Immunol. 178 (2007) 1363-1371
45. Blanchet F., Cardona A., Letimier F.A., Hershfield M.S., and Acuto O. CD28 costimulatory signal induces protein arginine methylation in T cells. J. Exp. Med. 202 (2005) 371-377
46. Nunes J.A., Collette Y., Truneh A., Olive D., and Cantrell D.A. 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
47. Blanchet F., Schurter B.T., and Acuto O. Protein arginine methylation in lymphocyte signaling. Curr. Opin. Immunol. 18 (2006) 321-328
48. Grakoui A., Bromley S.K., Sumen C., Davis M.M., Shaw A.S., Allen P.M., and Dustin M.L. The immunological synapse: a molecular machine controlling T cell activation. Science 285 (1999) 221-227
49. Dustin M.L., and Shaw A.S. Costimulation: building an immunological synapse. Science 283 (1999) 649-650
50. Simons K., and Ikonen E. Functional rafts in cell membranes. Nature 387 (1997) 569-572
51. Villalba M., Bi K., Rodriguez F., Tanaka Y., Schoenberger S., and Altman A. Vav1/Rac-dependent actin cytoskeleton reorganization is required for lipid raft clustering in T cells. J. Cell Biol. 155 (2001) 331-338
52. Wulfing C., Bauch A., Crabtree G.R., and Davis M.M. The vav exchange factor is an essential regulator in actin-dependent receptor translocation to the lymphocyte-antigen-presenting cell interface. Proc. Natl. Acad. Sci. USA 97 (2000) 10150-10155
53. Ardouin L., Bracke M., Mathiot A., Pagakis S.N., Norton T., Hogg N., and Tybulewicz V.L. Vav1 transduces TCR signals required for LFA-1 function and cell polarization at the immunological synapse. Eur. J. Immunol. 33 (2003) 790-797
54. Han J., Das B., Wei W., Van Aelst L., Mosteller R.D., Khosravi-Far R., Westwick J.K., Der C.J., and Broek D. Lck regulates Vav activation of members of the Rho family of GTPases. Mol. Cell. Biol. 17 (1997) 1346-1353
55. Kuhne M.R., Ku G., and Weiss A. A guanine nucleotide exchange factor-independent function of Vav1 in transcriptional activation. J. Biol. Chem. 275 (2000) 2185-2190
56. Kjoller L., and Hall A. Signaling to Rho GTPases. Exp. Cell Res. 253 (1999) 166-179
57. Vigorito E., Billadeu D.D., Savoy D., McAdam S., Doody G., Fort P., and Turner M. RhoG regulates gene expression and the actin cytoskeleton in lymphocytes. Oncogene 22 (2003) 330-342
58. Thrasher A.J. WASp in immune-system organization and function. Nat. Rev. Immunol. 2 (2002) 635-646
59. Snapper S.B., Rosen F.S., Mizoguchi E., Cohen P., Khan W., Liu C.H., Hagemann T.L., Kwan S.P., Ferrini R., Davidson L., Bhan A.K., and Alt F.W. Wiskott-Aldrich syndrome protein-deficient mice reveal a role for WASP in T but not B cell activation. Immunity 9 (1998) 81-91
60. Stowers L., Yelon D., Berg L.J., and Chant J. Regulation of the polarization of T cells toward antigen-presenting cells by Ras-related GTPase CDC42. Proc. Natl. Acad. Sci. USA 92 (1995) 5027-5031
61. Movilla N., Dosil M., Zheng Y., and Bustelo X.R. How Vav proteins discriminate the GTPases Rac1 and RhoA from Cdc42. Oncogene 20 (2001) 8057-8065
62. Villalba M., Coudronniere N., Deckert M., Teixeiro E., Mas P., and Altman A. A novel functional interaction between Vav and PKCtheta is required for TCR-induced T cell activation. Immunity 12 (2000) 151-160
63. Turner M., Mee P.J., Walters A., Quinn M.E., Mellor A.L., Zamoyska R., and Tybulewicz V.L.J. A requirement for the Rho-family GTP exchange factor Vav in positive and negative selection of thymocytes. Immunity 7 (1997) 451-460
64. Kong Y.Y., Fischer K.D., Bachmann M.F., Mariathasan S., Kozieradzki I., Nghiem M.P., Bouchard D., Bernstein A., Ohashi P.S., and Penninger J.M. Vav regulates peptide-specific apoptosis in thymocytes. J. Exp. Med. 188 (1998) 2099-2111
65. Doody G.M., Bell S.E., Vigorito E., Clayton E., McAdam S., Tooze R., Fernandez C., Lee I.J., and Turner M. Signal transduction through Vav-2 participates in humoral immune responses and B cell maturation. Nat. Immunol. 2 (2001) 542-547
66. Fujikawa K., Miletic A.V., Alt F.W., Faccio R., Brown T., Hoog J., Fredericks J., Nishi S., Mildiner S., Moores S.L., Brugge J., Rosen F.S., and Swat W. Vav1/2/3-null Mice Define an Essential Role for Vav Family Proteins in Lymphocyte Development and Activation but a Differential Requirement in MAPK Signalling in T and B Cells. J. Exp. Med. 198 (2003) 1595-1608
67. Tedford K., Nitschke L., Girkontaite I., Charlesworth A., Chan G., Sakk V., Barbacid M., and Fischer K.D. Compensation between Vav-1 and Vav-2 in B cell development and antigen receptor signalling. Nat. Immunol. 2 (2001) 548-555
68. del Peso L., Hernandez-Alcoceba R., Embade N., Carnero A., Esteve P., Paje C., and Lacal J.C. Rho proteins induce metastatic properties in vivo. Oncogene 15 (1997) 3047-3057
69. Abe K., Whitehead I.P., O'Bryan J.P., and Der C.J. Involvement of NH(2)-terminal sequences in the negative regulation of Vav signaling and transforming activity. J. Biol. Chem. 274 (1999) 30410-30418
70. Gimona M., and Winder S.J. Single calponin homology domains are not actin-binding domains. Curr. Biol. 8 (1998) R674-R675
71. De Sepulveda P., Okkenhaug K., Rose J.L., Hawley R.G., Dubreuil P., and Rottapel R. Socs1 binds to multiple signalling proteins and suppresses steel factor-dependent proliferation. EMBO J. 18 (1999) 904-915
72. Hobert O., Jallal B., and Ullrich A. Interaction of Vav with ENX-1, a putative transcriptional regulator of homeobox gene expression. Mol. Cell. Biol. 16 (1996) 3066-3073
73. Groysman M., Russek N., Shifrin C., and Katzav S. Vav, a GDP/GTP nucleotide exchange factor, interacts with GDIs, proteins that inhibit GDP/GTP dissociation. FEBS Lett. 467 (2000) 75-80
74. Groysman M., Hornstein I., Alcover A., and Katzav S. Vav1 and Ly-GDI two regulators of Rho GTPases, function cooperatively as signal transducers in T cell antigen receptor-induced pathways. J. Biol. Chem. 277 (2002) 50121-50130
75. Khosravi-Far R., Chrzanowska-Wodnicka M., Solski P.A., Eva A., Burridge K., and Der C.J. Dbl and Vav mediate transformation via mitogen-activated protein kinase pathways that are distinct from those activated by oncogenic Ras. Mol. Cell. Biol. 14 (1994) 6848-6857
76. Zugaza J.L., Lopez-Lago M.A., Caloca M.J., Dosil M., Movilla N., and Bustelo X.R. Structural determinants for the biological activity of Vav proteins. J. Biol. Chem. 277 (2002) 45377-45392
77. Aghazadeh B., Lowry W.E., Huang X.Y., and Rosen M.K. Structural basis for relief of autoinhibition of the Dbl homology domain of proto-oncogene Vav by tyrosine phosphorylation. Cell 102 (2000) 625-633
78. Palmby T.R., Abe K., Karnoub A.E., and Der C.J. Vav transformation requires activation of multiple GTPases and regulation of gene expression. Mol. Cancer Res. 2 (2004) 702-711
79. Katzav S., Sutherland M., Packham G., Yi T., and Weiss A. The protein tyrosine kinase ZAP-70 can associate with the SH2 domain of proto-Vav. J. Biol. Chem. 269 (1994) 32579-32585
80. Wu J., Motto D.G., Koretzky G.A., and Weiss A. Vav and SLP-76 interact and functionally cooperate in IL-2 gene activation. Immunity 4 (1996) 593-602
81. Kiener P.A., Rankin B.M., Burkhardt A.L., Schieven G.L., Gilliland L.K., Rowley R.B., Bolen J.B., and Ledbetter J.A. Cross-linking of Fc gamma receptor I (Fc gamma RI) and receptor II (Fc gamma RII) on monocytic cells activates a signal transduction pathway common to both Fc receptors that involves the stimulation of p72 Syk protein tyrosine kinase. J. Biol. Chem. 268 (1993) 24442-24448
82. Fu C., Turck C.W., Kurosaki T., and Chan A.C. BLNK: a central linker protein in B cell activation. Immunity 9 (1998) 93-103
83. Bustelo X.R., Ledbetter J.A., and Barbacid M. Product of vav proto-oncogene defines a new class of tyrosine protein kinase substrates. Nature 356 (1992) 68-71
84. Katzav S. Single point mutations in the SH2 domain impair the transforming potential of vav and fail to activate proto-vav. Oncogene 8 (1993) 1757-1763
85. Paccani S.R., Boncristiano M., Patrussi L., Ulivieri C., Wack A., Valensin S., Hirst T.R., Amedei A., Del Prete G., Telford J.L., D'Elios M.M., and Baldari C.T. Defective Vav expression and impaired F-actin reorganization in a subset of patients with common variable immunodeficiency characterized by T-cell defects. Blood 106 (2005) 626-634
86. Ye Z.S., and Baltimore D. Binding of Vav to Grb2 through dimerization of Src homology 3 domains. Proc. Natl. Acad. Sci. USA 91 (1994) 12629-12633
87. Salojin K.V., Zhang J., and Delovitch T.L. TCR and CD28 are coupled via ZAP-70 to the activation of the Vav/Rac-1-/PAK-1/p38 MAPK signaling pathway. J. Immunol. 163 (1999) 844-853
88. Groysman M., Nagano M., Shaanan B., and Katzav S. Mutagenic analysis of Vav reveals that an intact SH3 domain is required for transformation. Oncogene 17 (1998) 1597-1606
89. Hobert O., Jallal B., Schlessinger J., and Ullrich A. Novel signaling pathway suggested by SH3 domain-mediated p95vav/heterogeneous ribonucleoprotein K interaction. J. Biol. Chem. 269 (1994) 20225-20228
90. Bustelo X.R., Suen K.L., Michael W.M., Dreyfuss G., and Barbacid M. Association of the vav proto-oncogene product with poly(rC)-specific RNA-binding proteins. Mol. Cell. Biol. 15 (1995) 1324-1332
91. Hobert O., Schilling J.W., Beckerle M.C., Ullrich A., and Jallal B. SH3 domain-dependent interaction of the proto-oncogene product Vav with the focal contact protein zyxin. Oncogene 12 (1996) 1577-1581
92. Romero F., Dargemont C., Pozo F., Reeves W.H., Camonis J., Gisselbrech S., and Fischer S. p95vav associates with the nuclear protein Ku-70. Mol. Cell. Biol. 16 (1996) 37-44
93. Marengere L.E., Mirtsos C., Kozieradzki I., Veillette A., Mak T.W., and Penninger J.M. Proto-oncoprotein Vav interacts with c-Cbl in activated thymocytes and peripheral T cells. J. Immunol. 159 (1997) 70-76
94. Fackler O.T., Luo W., Geyer M., Alberts A.S., and Peterlin B.M. Activation of Vav by Nef induces cytoskeletal rearrangements and downstream effector functions. Mol. Cell 3 (1999) 729-739
95. Houlard M., Romero-Portillo F., Germani A., Depaux A., Regnier-Ricard F., Gisselbrecht S., and Varin-Blank N. Characterization of VIK-1: a new Vav-interacting Kruppel-like protein. Oncogene 24 (2005) 28-38
96. Gomez T.S., Hamann M.J., McCarney S., Savoy D.N., Lubking C.M., Heldebrant M.P., Labno C.M., McKean D.J., McNiven M.A., Burkhardt J.K., and Billadeau D.D. Dynamin 2 regulates T cell activation by controlling actin polymerization at the immunological synapse. Nat. Immunol. 6 (2005) 261-270
97. Han J., Luby-Phelps K., Das B., Shu X., Xia Y., Mosteller R.D., Krishna U.M., Falck J.R., White M.A., and Broek D. Role of substrates and products of PI 3-kinase in regulating activation of Rac-related guanosine triphosphatases by Vav. Science 279 (1998) 558-560
98. Das B., Shu X., Day G.J., Han J., Krishna U.M., Falck J.R., and Broek D. Control of intramolecular interactions between the pleckstrin homology and Dbl homology domains of Vav and Sos1 regulates Rac binding. J. Biol. Chem. 275 (2000) 15074-15081
99. Ma A.D., Metjian A., Bagrodia S., Taylor S., and Abrams C.S. Cytoskeletal reorganization by G protein-coupled receptors is dependent on phosphoinositide 3-kinase gamma, a Rac guanosine exchange factor, and Rac. Mol. Cell. Biol. 18 (1998) 4744-4751
100. Booden M.A., Campbell S.L., and Der C.J. Critical but distinct roles for the pleckstrin homology and cysteine-rich domains as positive modulators of Vav2 signaling and transformation. Mol. Cell. Biol. 22 (2002) 2487-2497
101. Katzav S., Packham G., Sutherland M., Aroca P., Santos E., and Cleveland J.L. Vav and Ras induce fibroblast transformation by overlapping signaling pathways which require c-Myc function. Oncogene 11 6 (1995) 1079-1088
102. Bustelo X.R., Suen K.L., Leftheris K., Meyers C.A., and Barbacid M. Vav cooperates with Ras to transform rodent fibroblasts but is not a Ras GDP/GTP exchange factor. Oncogene 9 (1994) 2405-2413
103. Villalba M., Hernandez J., Deckert M., Tanaka Y., and Altman A. Vav modulation of the Ras/MEK/ERK signaling pathway plays a role in NFAT activation and CD69 up-regulation. Eur. J. Immunol. 30 (2000) 1587-1596
104. Costello P.S., Walters A.E., Mee P.J., Turner M., Reynolds L.F., Prisco A., Sarner N., Zamoyska R., and Tybulewicz V.L. The Rho-family GTP exchange factor Vav is a critical transducer of T cell receptor signals to the calcium, ERK, and NF-kappaB pathways. Proc. Natl. Acad. Sci. USA 96 (1999) 3035-3040
105. Lee I.S., Liu Y., Narazaki M., Hibi M., Kishimoto T., and Taga T. Vav is associated with signal transducing molecules gp130, Grb2 and Erk2, and is tyrosine phosphorylated in response to interleukin-6. FEBS Lett. 401 (1997) 133-137
106. Crespo P., Bustelo X.R., Aaronson D.S., Coso O.A., Lopez-Barahona M., Barbacid M., and Gutkind J.S. Rac-1 dependent stimulation of the JNK/SAPK signaling pathway by Vav. Oncogene 13 (1996) 455-460
107. Song J.S., Haleem-Smith H., Arudchandran R., Gomez J., Scott P.M., Mill J.F., Tan T.H., and Rivera J. Tyrosine phosphorylation of Vav stimulates IL-6 production in mast cells by a Rac/c-Jun N-terminal kinase-dependent pathway. J. Immunol. 162 (1999) 802-810
108. Schapira V., Lazer G., and Katzav S. Osteopontin is an oncogenic Vav1- but not wild-type Vav1-responsive gene: implications for fibroblast transformation. Cancer Res. 66 (2006) 6183-6191
109. Rittling S.R., and Chambers A.F. Role of osteopontin in tumour progression. Br. J. Cancer 90 (2004) 1877-1881
110. Wai P.Y., and Kuo P.C. The role of Osteopontin in tumor metastasis. J. Surg. Res. 121 (2004) 228-241
111. Medico E., Gentile A., Lo Celso C., Williams T.A., Gambarotta G., Trusolino L., and Comoglio P.M. Osteopontin is an autocrine mediator of hepatocyte growth factor-induced invasive growth. Cancer Res. 61 (2001) 5861-5868
112. Fernandez-Zapico M.E., Gonzalez-Paz N.C., Weiss E E., Savoy D.N., Molina J.R., Fonseca R., Smyrk T.C., Chari S.T., Urrutia R., and Billadeau D.D. Ectopic expression of VAV1 reveals an unexpected role in pancreatic cancer tumorigenesis. Cancer Cell 7 (2005) 39-49
113. Takahashi M., Ritz J., and Cooper G.M. Activation of a novel human transforming gene, ret, by DNA rearrangement. Cell 42 (1985) 581-588
114. Nakamura T., Hillova J., Mariage-Samson R., and Hill M. Molecular cloning of a novel oncogene generated by DNA recombination during transfection. Oncogene Res. 2 (1988) 357-370
115. Zhan X., Culpepper A., Reddy M., Loveless J., and Goldfarb M. Human oncogenes detected by a defined medium culture assay. Oncogene 1 (1987) 369-376
116. Ishikawa F., Takaku F., Nagao M., and Sugimura T. Rat c-raf oncogene activation by a rearrangement that produces a fused protein. Mol. Cell. Biol. 7 (1987) 1226-1232
117. Stanton Jr. V.P., and Cooper G.M. Activation of human raf transforming genes by deletion of normal amino-terminal coding sequences. Mol. Cell. Biol. 7 (1987) 1171-1179
118. Neckameyer W.S., Shibuya M., Hsu M.T., and Wang L.H. Proto-oncogene c-ros codes for a molecule with structural features common to those of growth factor receptors and displays tissue specific and developmentally regulated expression. Mol. Cell. Biol. 6 (1986) 1478-1486
119. Martin-Zanca D., Hughes S.H., and Barbacid M. A human oncogene formed by the fusion of truncated tropomyosin and protein tyrosine kinase sequences. Nature 319 (1986) 743-748
120. Oskam R., Coulier F., Ernst M., Martin-Zanca D., and Barbacid M. Frequent generation of oncogenes by in vitro recombination of TRK protooncogene sequences. Proc. Natl. Acad. Sci. USA 85 (1988) 2964-2968
121. Ullrich A., and Schlessinger J. Signal transduction by receptors with tyrosine kinase activity. Cell 61 (1990) 203-212
122. Cantley L.C., Auger K.R., Carpenter C., Duckworth B., Graziani A., Kapeller R., and Soltoff S. Oncogenes and signal transduction. Cell 64 (1991) 281-302
123. Ball D.W. Medullary thyroid cancer: therapeutic targets and molecular markers. Curr. Opin. Oncol. 19 (2007) 18-23
124. Greco A., Roccato E., and Pierotti M.A. TRK oncogenes in papillary thyroid carcinoma. Cancer Treat. Res. 122 (2004) 207-219
125. Schramm A., Schulte J.H., Astrahantseff K., Apostolov O., Limpt V., Sieverts H., Kuhfittig-Kulle S., Pfeiffer P., Versteeg R., and Eggert A. Biological effects of TrkA and TrkB receptor signaling in neuroblastoma. Cancer Lett. 228 (2005) 143-153
126. Yayon A., and Klagsbrun M. Autocrine regulation of cell growth and transformation by basic fibroblast growth factor. Cancer Metastasis Rev. 9 (1990) 191-202
127. Schreck R., and Rapp U.R. Raf kinases: oncogenesis and drug discovery. Int. J. Cancer 119 (2006) 2261-2271
128. Gollob J.A., Wilhelm S., Carter C., and Kelley S.L. Role of Raf kinase in cancer: therapeutic potential of targeting the Raf/MEK/ERK signal transduction pathway. Semin. Oncol. 33 (2006) 392-406
129. Martinerie C., Cannizzaro L.A., Croce C.M., Huebner K., Katzav S., and Barbacid M. The human VAV proto-oncogene maps to chromosome region 19p12-19p13.2. Hum. Genet. 86 (1990) 65-68
130. Hornstein I., Pikarsky E., Groysman M., Amir G., Peylan-Ramu N., and Katzav S. The haematopoietic specific signal transducer Vav1 is expressed in a subset of human neuroblastomas. J. Pathol. 199 (2003) 526-533
131. Bartolome R.A., Molina-Ortiz I., Samaniego R., Sanchez-Mateos P., Bustelo X.R., and Teixido J. Activation of Vav/Rho GTPase signaling by CXCL12 controls membrane-type matrix metalloproteinase-dependent melanoma cell invasion. Cancer Res. 1 (2006) 248-258
132. Prieto-Sanchez R.M., Hernandez J.A., Garcia J.L., Gutierrez N.C., San Miguel J., Bustelo X.R., and Hernandez J.M. Overexpression of the VAV proto-oncogene product is associated with B-cell chronic lymphocytic leukaemia displaying loss on 13q. Br. J. Haematol. 133 (2006) 642-645
133. Barnes C.J., and Kumar R. Biology of the epidermal growth factor receptor family. Cancer Treat. Res. 119 (2004) 1-13
134. Moores S.L., Selfors L.M., Fredericks J., Breit T., Fujikawa K., Alt F.W., Brugge J.S., and Swat W. Vav family proteins couple to diverse cell surface receptors. Mol. Cell. Biol. 20 (2000) 6364-6373
135. Melamed I., Patel H., Brodie C., and Gelfand E.W. Activation of Vav and Ras through the nerve growth factor and B cell receptors by different kinases. Cell. Immunol. 191 (1999) 83-89
136. Schwab M. Amplification of the MYCN oncogene and deletion of putative tumour suppressor gene in human neuroblastomas. Brain Pathol. 1 (1990) 41-46
137. Brodeur G.M. Molecular basis for heterogeneity in human neuroblastomas. Eur. J. Cancer 4 (1995) 505-510
138. Tonini G.P. Neuroblastoma: the result of multistep transformation?. Stem Cells 11 (1993) 276-282
139. Korc M. Role of growth factors in pancreatic cancer. Surg. Oncol. Clin. N. Am. 7 (1998) 25-41
140. Hirai H., Okabe T., Anraku Y., Fujisawa M., Urabe A., and Takaku F. Activation of the c-K-ras oncogene in a human pancreas carcinoma. Biochem. Biophys. Res. Commun. 127 (1985) 168-174