Lck regulates Vav activation of members of the Rho family of GTPases

Molecular and Cellular Biology

Volumn 17, Issue 3, 1997, Pages 1346-1353

  Han, Jaewon ^a   Das, Balaka ^a   Wei, Wen ^a   Van Aelst, Linda ^b   Mosteller, Raymond D ^a   Khosravi Far, Roya ^c   Westwick, John K ^c   Der, Channing J ^c   Broek, Daniel ^a  

^a UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

^b Howard Hughes Medical Institute Cold Spring Harbor Laboratory Cold Spring Harbor   (United States)

^c UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE EXCHANGE FACTOR;

ARTICLE; BINDING AFFINITY; CATALYSIS; CELL CULTURE; DATA ANALYSIS; ENZYME ACTIVATION; ENZYME ACTIVITY; GENE EXPRESSION REGULATION; GENETIC TRANSFECTION; IMMUNOFLUORESCENCE; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; SACCHAROMYCES CEREVISIAE;

ANIMALIA; SACCHAROMYCES CEREVISIAE;

EID: 0031034050     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.17.3.1346     Document Type: Article

References (51)

1. Adams, J. M., H. Houston, J. Allen, T. Lints, and R. Harvey. 1992. The hematopoietically expressed Vav proto-oncogene shares homology with the dbl GDP-GTP exchange factor, the her gene and a yeast gene (CDC24) involved in cytoskeletal organization. Oncogene 7:611-618.
2. Bender, A., and J. R. Pringle. 1989. Multicopy suppression of the cdc24 budding defect in yeast by CDC42 and three newly identified genes including the ras-related gene RSR1. Proc. Natl. Acad. Sci. USA 86:9976-9980.
3. Boguski, M. S., and F. McCormick. 1993. Proteins regulating Ras and its relatives. Nature 366:643-654.
4. Broek, D., N. Samiy, O. Fasano, A. Fujiyama, F. Tamanoi, J. Northup, and M. Wigler. 1985. Differential activation of yeast adenylate cyclase by wild-type and mutant Ras proteins. Cell 41:763-769.
5. Bustelo, X. R., K. L. Suen, K. Leftheris, C. A. Meyers, and M. Barbacid. 1994. Vav cooperates with Ras to transform rodent fibroblasts but is not a Ras GDP/GTP exchange factor. Oncogene 9:2405-2413.
6. Cen, H., A. G. Papageorge, R. Zippel, D. R. Lowy, and K. Zhang. 1992. Isolation of multiple mouse cDNAs with coding homology to Saccharomyces cerevisiae CDC25: identification of a region related to Bcr, Vav, Dbl and CDC24. EMBO J. 11:4007-4015.
7. Clark, G. J., A. D. Cox, S. M. Graham, and C. J. Der. 1995. Biological assays for Ras transformation. Methods Enzymol. 255:395-412.
8. Coleman, K. G., H. Y. Steensma, D. B. Kaback, and J. R. Pringle. 1986. Molecular cloning of chromosome 1 DNA from Saccharomyces cerevisiae: isolation and characterization of the CDC24 gene and adjacent regions of the chromosome. Mol. Cell. Biol. 6:4516-4525.
9. Coppola, J., S. Bryant, T. Koda, D. Conway, and M. Barbacid. 1991. Mechanism of activation of the Vav protooncogene. Cell Growth Differ. 2:95-105.
10. Coso, O. A., M. Chiariello, J. C. Yu, H. Teramoto, P. Crespo, N. Xu, T. Miki, and J. S. Gutkind. 1995. The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway. Cell 81:1137-1146.
11. Field, J., D. Broek, T. Kataoka, and M. Wigler. 1987. Guanine nucleotide activation of, and competition between. RAS proteins from Saccharomyces cerevisiae. Mol. Cell. Biol. 7:2128-2133.
12. Galland, F., S. Katzav, and D. Birnbaum. 1992. The products of the mcf-2 and vav proto-oncogenes and of the yeast gene cdc-24 share sequence similarities. Oncogene 7:585-587.
13. Gimona, M., A. Watakabe, and D. M. Helfman. 1995. Specificity of dimer formation in tropomyosins: influence of alternatively spliced exons on homodimer and heterodimer assembly. Proc. Natl. Acad. Sci. USA 92:9776-9780.
14. Gulbins, E., K. M. Coggeshall, G. Baier, S. Katzav, P. Burn, and A. Altman. 1993. Tyrosine kinase-stimulated guanine nucleotide exchange activity of Vav in T cell activation. Science 260:822-825.
15. Gulbins, E., K. M. Coggeshall, C. Langlet, G. Baier, N. Bonnefoy-Berard, P. Burn, A. Wittinghofer, S. Katzav, and A. Altman. 1994. Activation of Ras in vitro and in intact fibroblasts by the Vav guanine nucleotide exchange protein. Mol. Cell. Biol. 14:906-913.
16. Gulbins, E., K. M. Coggeshall, G. Baier, D. Telford, C. Langlet, G. Baier-Bitterlich, N. Bonnefoy-Berard, P. Burn, A. Wittinghofer, and A. Altman. 1994. Direct stimulation of Vav guanine nucleotide exchange activity for Ras by phorbol esters and diglycerides. Mol. Cell. Biol. 14:4749-4758.
17. Gupta, S., D. Campbell, B. Derijard, and R. J. Davis. 1995. Transcription factor ATF2 regulation by the JNK signal transduction pathway. Science 267:389-393.
18. Han, J., and D. Broek. Unpublished data.
19. Hart, M. J., A. Eva, T. Evans, S. A. Aaronson, and R. A. Cerione. 1991. Catalysis of guanine nucleotide exchange on the CDC42Hs protein by the dbl oncogene product. Nature 354:311-314.
20. Hart, M. J., A. Evans, D. Zangrilli, S. A. Aaronson, T. Evans, R. A. Cerione, and Y. Zheng. 1994. Cellular transformation and guanine nucleotide exchange activity are catalyzed by a common domain on the dbl oncogene product. J. Biol. Chem. 269:62-65.
21. Hill, C. S., J. Wynne, and R. Treisman. 1995. The Rho family GTPases RhoA, Rac1, and CDC42Hs regulate transcriptional activation by SRF. Cell 81:1159-1170.
22. Johnson, D. I., and J. R. Pringle. 1990. Molecular characterization of CDC42, a Saccharomyces cerevisiae gene involved in the development of cell polarity. J. Cell Biol. 111:143-152.
23. Katzav, S., D. Martin-Zanca, and M. Barbacid. 1989. Vav, a novel human oncogene derived from a locus ubiquitously expressed in hematopoietic cells. EMBO J. 8:2283-2290.
24. Katzav, S., J. L. Cleveland, H. E. Heslop, and D. Pulido. 1991. Loss of the amino-terminal helix-loop-helix domain of the vav proto-oncogene activates its transforming potential. Mol. Cell. Biol. 11:1912-1920.
25. Khosravi-Far, R., M. Chrzanowska-Wodnicka, P. A. Solski, A. Eva, K. Burridge, and C. J. Der. 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.
26. Khosravi-Far, R., P. A. Solski, G. J. Clark, M. S. Kinch, and C. J. Der. 1995. Activation of Rac1, RhoA, and mitogen-activated protein kinases is required for Ras transformation. Mol. Cell. Biol. 15:6443-6453.
27. Kolanus, W., C. Romeo, and B. Seed. 1993. T cell activation by clustered tyrosine kinases. Cell 74:171-183.
28. Kozma, R., S. Ahmed, A. Best, and L. Lim. 1995. The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibroblasts. Mol. Cell. Biol. 15:1942-1952.
29. Manser, E., C. Chong, Z.-S. Zhao, T. Leung, G. Michael, C. Hall, and L. Lim. 1995. Molecular cloning of a new member of the p21-Cdc42/Rac-activated kinase (PAK) family. J. Biol. Chem. 270:25070-25078.
30. Margolis, B., P. Hu, S. Katzav, W. Li, J. M. Oliver, A. Ullrich, A. Weiss, and J. Schlessinger. 1992. Tyrosine phosphorylation of Vav proto-oncogene product containing SH2 domain and transcription factor motifs. Nature 356:71-74.
31. Marth, J. D., R. Peet, E. G. Krebs, and R. M. Perimutter. 1985. A lymphocyte-specific protein-tyrosine kinase gene is rearranged and overexpressed in the murine T cell lymphoma LSTRA. Cell 43:393-404.
32. Minden A., A. Lin, F. X. Claret, A. Abo, and M. Karin. 1995. Selective activation of the JNK signaling cascade and c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs. Cell 81:1147-1157.
33. Mosteller, R. D., J. Han, and D. Broek. 1994. Identification of residues of the H-Ras protein critical for functional interaction with guanine nucleotide exchange factors. Mol. Cell. Biol. 14:1104-1112.
34. Mustelin, T., and P. Burn. 1993. Regulation of src family tyrosine kinases in lymphocytes. Trends Biochem. Sci. 18:215-220.
35. Nobes, C. D., and A. Hall. 1995. Rho. Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81:53-62.
36. Park, W., R. D. Mosteller, and D. Broek. 1994. Amino acid residues in the CDC25 guanine nucleotide exchange factor critical for interaction with Ras. Mol. Cell. Biol. 14:8117-8122.
37. Qiu, R.-G., J. Chen, D. Kirn, F. McCormick, and M. Symons. 1995. An essential role for Rac in Ras transformation. Nature 374:457-459.
38. Quilliam, L. A., S. Y. Huff, K. M. Rabun, W. Wei, W. Park, D. Broek, and C. J. Der. 1994. Membrane-targeting potentiates guanine nucleotide exchange factor CDC25 and SOS1 activation of Ras transforming activity. Proc. Natl. Acad. Sci. USA 91:8512-8516.
39. Ridley, A. J., H. F. Paterson, C. L. Johnston, D. Diekmann, and A. Hall. 1992. The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell 70:401-410.
40. Sanger, F., S. Nicklen, and A. R. Coulson. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74:5463-5467.
41. Sherman, F., G. R. Fink, and J. B. Hicks (ed.). 1986. Laboratory course manual for methods in yeast genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
42. Small, J. V. 1988. The actin cytoskeleton. Electron Microsc. Rev. 1:155-174.
43. Tanaka, M., and W. Herr. 1990. Differential transcriptional activation by Oct-1 and Oct-2: interdependent activation domains induce Oct-2 phosphorylation. Cell 60:375-386.
44. Tarakhovsky, A., M. Turner, S. Schaal, P. J. Mee, L. P. Duddy, K. Rajewsky, and V. L. Tybulewicz. 1995. Defective antigen receptor-mediated proliferation of B and T cells in the absence of Vav. Nature 374:467-470.
45. Weiss, A. 1993. T cell antigen receptor signal transduction: a tale of tails and cytoplasmic protein-tyrosine kinases. Cell 73:209-212.
46. Westwick, J. K., and D. A. Brenner. 1995. Methods for analyzing c-Jun kinase. Methods Enzymol. 255:342-359.
47. Wright, D. D., B. M. Sefton, and M. P. Kamps. 1994. Oncogenic activation of the Lck protein accompanies translocation of the LCK gene in the human HSB2 T-cell leukemia. Mol. Cell. Biol. 14:2429-2437.
48. Young, D., M. Riggs, J. Field, A. Vojtek, D. Broek, and M. Wigler. 1989. The adenylate cyclase gene from Schizosaccharomyces pombe. Proc. Natl. Acad. Sci. USA 86:7989-7993.
49. Zhang S., J. Han, M. A. Sells, J. Chernoff, U. G. Knaus, R. J. Ulevitch, and G. M. Bokoch. 1995. Rho family GTPases regulate p38 mitogen-activated protein kinase through the downstream mediator Pak1. J. Biol. Chem. 270: 23934-23936.
50. Zheng, Y., R. Cerione, and A. Bender. 1994. Control of the yeast bud-site assembly GTPase Cdc42. J. Biol. Chem. 269:2369-2372.
51. Ziman M., J. M. O'Brien, L. A. Ouellette, W. R. Church, and D. I. Johnson. 1991. Mutational analysis of CDC42Sc, a Saccharomyces cerevisiae gene that encodes a putative GTP-binding protein involved in the control of cell polarity. Mol. Cell. Biol. 11:3537-3544.