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Volumn 57, Issue 12, 1997, Pages 2478-2484

The GTPase and Rho GAP domains of p190, a tumor suppressor protein that binds the M(r) 120,000 Ras GAP, independently function as Anti-Ras tumor suppressors

Author keywords

[No Author keywords available]

Indexed keywords

AMINO TERMINAL SEQUENCE; ARTICLE; CELL TRANSFORMATION; ENZYME ACTIVITY; GENE ACTIVATION; MALIGNANT TRANSFORMATION; NONHUMAN; ONCOGENE RAS; OOCYTE MATURATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION; SIGNAL TRANSDUCTION; TUMOR SUPPRESSOR GENE;

EID: 0030943968     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (56)

References (44)
  • 1
    • 0028464349 scopus 로고
    • Regulation of the Ras signalling network
    • Maruta, H., and Burgess, A. W. Regulation of the Ras signalling network. BioEssays, 16: 486-494, 1994.
    • (1994) BioEssays , vol.16 , pp. 486-494
    • Maruta, H.1    Burgess, A.W.2
  • 3
    • 0030600224 scopus 로고    scopus 로고
    • Controlled over-expression of selected domains of the p85 subunit of PI-3 kinase reverts v-Ha-Ras transformation
    • Zhang, Q. X., and Baldwin, G. Controlled over-expression of selected domains of the p85 subunit of PI-3 kinase reverts v-Ha-Ras transformation. Biochim. Biophys. Acta. 1312: 207-214, 1996.
    • (1996) Biochim. Biophys. Acta. , vol.1312 , pp. 207-214
    • Zhang, Q.X.1    Baldwin, G.2
  • 5
    • 0030022174 scopus 로고    scopus 로고
    • Ral GTPases mediate a distinct downstream signaling pathway from Ras that facilitates cellular transformation
    • Urano, T., Emkey, R., and Feig, L. A. Ral GTPases mediate a distinct downstream signaling pathway from Ras that facilitates cellular transformation. EMBO J., 15: 810-816, 1996.
    • (1996) EMBO J. , vol.15 , pp. 810-816
    • Urano, T.1    Emkey, R.2    Feig, L.A.3
  • 6
    • 0025177324 scopus 로고
    • Phosphorylation of GAP and GAP-associated proteins by transforming and mitogenic tyrosine kinases
    • Ellis, C., Moran, M., McCormick, F., and Pawson, T. Phosphorylation of GAP and GAP-associated proteins by transforming and mitogenic tyrosine kinases. Nature (Lond.), 343: 377-381, 1990.
    • (1990) Nature (Lond.) , vol.343 , pp. 377-381
    • Ellis, C.1    Moran, M.2    McCormick, F.3    Pawson, T.4
  • 7
    • 0031030898 scopus 로고    scopus 로고
    • Tandem SH2 binding sites mediate the Ras GAP-Rho GAP interaction: A conformational mechanism for SH3 domain regulation
    • Hu, K. Q., and Settleman, J. Tandem SH2 binding sites mediate the Ras GAP-Rho GAP interaction: a conformational mechanism for SH3 domain regulation. EMBO J., 16: 473-483, 1997.
    • (1997) EMBO J. , vol.16 , pp. 473-483
    • Hu, K.Q.1    Settleman, J.2
  • 8
    • 0027339729 scopus 로고
    • Identification of the SH3 domain of GAP as an essential sequence for Ras-GAP-mediated signalling
    • Washington DC
    • Duchesne, M., Schweighoffer, F., Parker, F., Clerc, F., Frobert, Y., Thang, M. N., and Tocque, B. Identification of the SH3 domain of GAP as an essential sequence for Ras-GAP-mediated signalling. Science (Washington DC), 259: 525-528, 1993.
    • (1993) Science , vol.259 , pp. 525-528
    • Duchesne, M.1    Schweighoffer, F.2    Parker, F.3    Clerc, F.4    Frobert, Y.5    Thang, M.N.6    Tocque, B.7
  • 9
    • 0008893321 scopus 로고    scopus 로고
    • Mammals II. Downstream of RAS and actin-cytoskeleton
    • H. Maruta and A. W. Burgess (eds.), Heidelberg/Austin: Springer/Landes Bioscience
    • Maruta, H. Mammals II. Downstream of RAS and actin-cytoskeleton. In: H. Maruta and A. W. Burgess (eds.), Regulation of RAS Signaling Network, pp. 139-180. Heidelberg/Austin: Springer/Landes Bioscience, 1996.
    • (1996) Regulation of RAS Signaling Network , pp. 139-180
    • Maruta, H.1
  • 10
    • 0029090228 scopus 로고
    • Two regions with different growth modulating activity in N-terminal half of 120 kDa Ras GAP: SH2/SH3 domain and Gly-Ala-pro-rich stretch
    • Chang, J. S., Kobayashi, M., Wang, D. Z. M., Maruta, H., and Ishiwuta, S. Two regions with different growth modulating activity in N-terminal half of 120 kDa Ras GAP: SH2/SH3 domain and Gly-Ala-pro-rich stretch. Eur. J. Biochem., 232: 691-699, 1995.
    • (1995) Eur. J. Biochem. , vol.232 , pp. 691-699
    • Chang, J.S.1    Kobayashi, M.2    Wang, D.Z.M.3    Maruta, H.4    Ishiwuta, S.5
  • 11
    • 0026740716 scopus 로고
    • Molecular cloning of cDNAs encoding the GAP-associated protein of 190 kDa: Implications for a signalling pathway from Ras to the nucleus
    • Settleman, J., Narashimhan, V., Foster, L. C., and Weinberg, R. A. Molecular cloning of cDNAs encoding the GAP-associated protein of 190 kDa: Implications for a signalling pathway from Ras to the nucleus. Cell, 69: 539-549, 1992.
    • (1992) Cell , vol.69 , pp. 539-549
    • Settleman, J.1    Narashimhan, V.2    Foster, L.C.3    Weinberg, R.A.4
  • 12
    • 0026668762 scopus 로고
    • Association between GTPase activators for Rho and Ras families
    • Settleman, J., Albright, C. F., Foster, L. C., and Weinberg, R. A. Association between GTPase activators for Rho and Ras families. Nature (Lond.), 359: 153-154, 1992.
    • (1992) Nature (Lond.) , vol.359 , pp. 153-154
    • Settleman, J.1    Albright, C.F.2    Foster, L.C.3    Weinberg, R.A.4
  • 14
    • 0027988106 scopus 로고
    • p190 Rho GAP, the major Ras GAP-associated protein, binds GTP directly
    • Foster R., Hu, K. Q., Shaywitz, D. A., and Settleman, J. p190 Rho GAP, the major Ras GAP-associated protein, binds GTP directly. Mol. Cell Biol., 14: 7173-7181, 1994.
    • (1994) Mol. Cell Biol. , vol.14 , pp. 7173-7181
    • Foster, R.1    Hu, K.Q.2    Shaywitz, D.A.3    Settleman, J.4
  • 16
    • 0028892646 scopus 로고
    • Evidence that farnesylase inhibitors suppress Ras transformation by interfering with Rho activity
    • Lebowitz, P. F., Davide, J. P., and Prendergast, G. C. Evidence that farnesylase inhibitors suppress Ras transformation by interfering with Rho activity. Mol. Cell. Biol., 15: 6613-6622, 1995.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6613-6622
    • Lebowitz, P.F.1    Davide, J.P.2    Prendergast, G.C.3
  • 17
    • 0023715225 scopus 로고
    • Inhibition of NIH 3T3 cell proliferation by a mutant Ras protein with preferential affinity for GDP
    • Feig, L. A., and Cooper, G. M. Inhibition of NIH 3T3 cell proliferation by a mutant Ras protein with preferential affinity for GDP. Mol. Cell Biol., 8: 3235-3243, 1988.
    • (1988) Mol. Cell Biol. , vol.8 , pp. 3235-3243
    • Feig, L.A.1    Cooper, G.M.2
  • 18
    • 0028388748 scopus 로고
    • Ras regulatory interactions: Novel targets for anti-cancer intervention?
    • Prendergast, G. C., and Gibbs, J. B. Ras regulatory interactions: novel targets for anti-cancer intervention? BioEssays, 16: 187-191, 1994.
    • (1994) BioEssays , vol.16 , pp. 187-191
    • Prendergast, G.C.1    Gibbs, J.B.2
  • 19
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne, H. R., Sanders, D. A., and McCormick, F. The GTPase superfamily: conserved structure and molecular mechanism. Nature (Lond.), 349: 117-127, 1991.
    • (1991) Nature (Lond.) , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 20
    • 0026017886 scopus 로고
    • The residues of Ras and Rap proteins that determine their GAP specificities
    • Maruta, H., Holden, J., Sizeland, A., and D'Ahaco G. The residues of Ras and Rap proteins that determine their GAP specificities. J. Biol. Chem., 266: 11661-11668, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11661-11668
    • Maruta, H.1    Holden, J.2    Sizeland, A.3    D'Ahaco, G.4
  • 22
    • 0027491616 scopus 로고
    • The GTPase activating NFI fragment of 91 amino acids reverses v-Ha-Ras-induced malignant phenotype
    • Nur-E-Kamal, M. S. A., Varga, M., and Maruta, H. The GTPase activating NFI fragment of 91 amino acids reverses v-Ha-Ras-induced malignant phenotype. J. Biol. Chem., 268: 22331-22338, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22331-22338
    • Nur-E-Kamal, M.S.A.1    Varga, M.2    Maruta, H.3
  • 23
    • 0028168361 scopus 로고
    • An anti-Ras function of neurofibromatosis type 2 gene product (NF2/Merlin)
    • Tikoo, A., Varga, M., Ramesh, V., Gusella, J., and Maruta, H. An anti-Ras function of neurofibromatosis type 2 gene product (NF2/Merlin). J. Biol. Chem., 269: 23387-23390, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23387-23390
    • Tikoo, A.1    Varga, M.2    Ramesh, V.3    Gusella, J.4    Maruta, H.5
  • 24
    • 0021233741 scopus 로고
    • Autophosphorylation of v-Ha-Ras is modulated by amino acid residue 12
    • Gibbs, J. B., Ellis, R. W., and Scolnick, E. M. Autophosphorylation of v-Ha-Ras is modulated by amino acid residue 12. Proc. Natl. Acad. Sci. USA., 81: 2674-2678, 1984.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 2674-2678
    • Gibbs, J.B.1    Ellis, R.W.2    Scolnick, E.M.3
  • 25
    • 0029670841 scopus 로고    scopus 로고
    • Synergy between APC mutation and v-Ha-Ras is sufficient to induce colon carcinomas
    • D'Abaco, G., Whitehead, R., and Burgess, A. W. Synergy between APC mutation and v-Ha-Ras is sufficient to induce colon carcinomas. Mol. Cell Biol., 16: 884-891, 1996.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 884-891
    • D'Abaco, G.1    Whitehead, R.2    Burgess, A.W.3
  • 27
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Bioehem., 72: 248-254, 1976.
    • (1976) Anal. Bioehem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 28
    • 0025647881 scopus 로고
    • v-Ha-Ras transgene mice abrogates the initiationn step in mouse skin tumorigenesis: Effects of phorbol esters and retinoic acid
    • Leder, A., Kuo, A., Cardiff, R. D., Sinn, E., and Leder, P. v-Ha-Ras transgene mice abrogates the initiationn step in mouse skin tumorigenesis: effects of phorbol esters and retinoic acid. Proc. Natl. Acad. Sci. USA, 87: 9178-9182, 1990.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9178-9182
    • Leder, A.1    Kuo, A.2    Cardiff, R.D.3    Sinn, E.4    Leder, P.5
  • 30
    • 0027240628 scopus 로고
    • Tumor-suppressive function of mutated gelsolin in Ras-transformed cells
    • Muellauer, L., Fujita, H., Shizaki, A., and Kuzumaki, N. Tumor-suppressive function of mutated gelsolin in Ras-transformed cells. Oneogene, 8: 2531-2536, 1993.
    • (1993) Oneogene , vol.8 , pp. 2531-2536
    • Muellauer, L.1    Fujita, H.2    Shizaki, A.3    Kuzumaki, N.4
  • 31
    • 0028019830 scopus 로고
    • The minimal fragments of c-Raf-1 and NFI that can suppress v-Ha-Ras-induced malignant phenotype
    • Fridman, M., Tikoo, A., Varga, M., Murphy, A., Nur-E-Karnal, M. S. A., and Maruta, H. The minimal fragments of c-Raf-1 and NFI that can suppress v-Ha-Ras-induced malignant phenotype. J. Biol. Chem., 269: 30105-30108, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30105-30108
    • Fridman, M.1    Tikoo, A.2    Varga, M.3    Murphy, A.4    Nur-E-Karnal, M.S.A.5    Maruta, H.6
  • 32
    • 0029055812 scopus 로고
    • The small GTP-binding proteins Rac 1 and CDC42 regulate the activity of the JNK/SPAK signalling pathway
    • Coso, O. A., Chiariello, M., Yu, J. C., Teramoto, H., Crespo, P., Xu, N., Miki, T., and Gutkind, J. S. The small GTP-binding proteins Rac 1 and CDC42 regulate the activity of the JNK/SPAK signalling pathway. Cell, 81: 1137-1146, 1995.
    • (1995) Cell , vol.81 , pp. 1137-1146
    • Coso, O.A.1    Chiariello, M.2    Yu, J.C.3    Teramoto, H.4    Crespo, P.5    Xu, N.6    Miki, T.7    Gutkind, J.S.8
  • 33
    • 0026425405 scopus 로고
    • Transformation suppressor activity of a Jun transcription factor lacking its activation domain
    • Lloyd, A., Yancheva, N., and Wasylyk, B. Transformation suppressor activity of a Jun transcription factor lacking its activation domain. Nature (Lond.), 352: 635-638, 1991.
    • (1991) Nature (Lond.) , vol.352 , pp. 635-638
    • Lloyd, A.1    Yancheva, N.2    Wasylyk, B.3
  • 34
    • 0028144846 scopus 로고
    • c-Fos transcriptional activity stimulated by H-Ras-activated protein kinase distinct from JNK and ERK
    • Deng, T., and Karin, M. c-Fos transcriptional activity stimulated by H-Ras-activated protein kinase distinct from JNK and ERK. Nature (Lond.), 371: 171-175, 1994.
    • (1994) Nature (Lond.) , vol.371 , pp. 171-175
    • Deng, T.1    Karin, M.2
  • 36
    • 0026778344 scopus 로고
    • GAP SH2-SH3 domains induce gene expression in a Ras-dependent fashion
    • Medema, R. H., De Laat, W. L., Martin, G. A., McCormiek, F., and Bos, J. L. GAP SH2-SH3 domains induce gene expression in a Ras-dependent fashion. Mol. Cell. Biol., 12: 3425-3430, 1992.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3425-3430
    • Medema, R.H.1    De Laat, W.L.2    Martin, G.A.3    McCormiek, F.4    Bos, J.L.5
  • 37
    • 0029015774 scopus 로고
    • The Rho family GTPases RhoA, Rac 1 and CDC42 regulate transcriptional activation by SRF
    • Hill, C. S., Wynne, J., and Treisman, R. The Rho family GTPases RhoA, Rac 1 and CDC42 regulate transcriptional activation by SRF. Cell, 81: 1159-1170, 1995.
    • (1995) Cell , vol.81 , pp. 1159-1170
    • Hill, C.S.1    Wynne, J.2    Treisman, R.3
  • 38
    • 0029117595 scopus 로고
    • Thromin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets
    • Hartwig, J. H., Bokoch, G. M., Carpenter, C. L., Janmey, P. A., Taylor, L. A., Toker, A., and Stossel, T. P. Thromin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets. Cell, 82: 643-653, 1995.
    • (1995) Cell , vol.82 , pp. 643-653
    • Hartwig, J.H.1    Bokoch, G.M.2    Carpenter, C.L.3    Janmey, P.A.4    Taylor, L.A.5    Toker, A.6    Stossel, T.P.7
  • 39
    • 0026654125 scopus 로고
    • The small G protein Rac regulates growth factor-induced membrane ruffling
    • Ridley, A. J., Paterson, H. F., Johnston, C. L., Diekman, D., and Hall, A. The small G protein Rac regulates growth factor-induced membrane ruffling. Cell, 70: 401-410, 1992.
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekman, D.4    Hall, A.5
  • 41
    • 0029070887 scopus 로고
    • Selective activation of the JNK signalling cascade and c-Jun transcriptional activity by the small GTPases Rac and CDC42
    • Minden, A., Lin, A., Claret, F. X., Abo, A., and Karin, M. Selective activation of the JNK signalling cascade and c-Jun transcriptional activity by the small GTPases Rac and CDC42. Cell, 81: 1147-1157, 1995.
    • (1995) Cell , vol.81 , pp. 1147-1157
    • Minden, A.1    Lin, A.2    Claret, F.X.3    Abo, A.4    Karin, M.5
  • 42
    • 0026705661 scopus 로고
    • Suppression of tumorigenicity in transformed cells after transfection with vinculin cDNA
    • Fernandez, J. L. R., Geiger, B., Salomon, D., Sabanay, I., Zoeller, M., and Ben-Ze'ev, A. Suppression of tumorigenicity in transformed cells after transfection with vinculin cDNA. J. Cell Biol., 119: 427-438, 1992.
    • (1992) J. Cell Biol. , vol.119 , pp. 427-438
    • Fernandez, J.L.R.1    Geiger, B.2    Salomon, D.3    Sabanay, I.4    Zoeller, M.5    Ben-Ze'ev, A.6
  • 43
    • 0027506925 scopus 로고
    • Suppression of tumorigenicity in SV40-transformed 3T3 cells transfected with α-actinin
    • Glueck, U., Kwiatkowski, D., and Ben-Ze'ev, A. Suppression of tumorigenicity in SV40-transformed 3T3 cells transfected with α-actinin. Proc. Natl. Acad. Sci. USA, 90: 383-387, 1993.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 383-387
    • Glueck, U.1    Kwiatkowski, D.2    Ben-Ze'ev, A.3
  • 44
    • 0026002048 scopus 로고
    • Molecular cloning and characterization of a factor that binds the human glucocorticoid receptor gene and represses its expression
    • LeClerc, S., Palaniswami, R. Xie, B., and Govindan, M. V. Molecular cloning and characterization of a factor that binds the human glucocorticoid receptor gene and represses its expression. J. Biol. Chem., 266: 17333-17340, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17333-17340
    • LeClerc, S.1    Palaniswami, R.2    Xie, B.3    Govindan, M.V.4


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