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Volumn 290, Issue 25, 2015, Pages 15892-15903

The function of embryonic stem cell-expressed RAS (E-RAS), a unique RAS family member, correlates with its additional motifs and its structural properties

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CELL GROWTH; PROTEINS;

EID: 84940093426     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.640607     Document Type: Article
Times cited : (14)

References (82)
  • 1
    • 0035834388 scopus 로고    scopus 로고
    • The guanine nucleotide-binding switch in three dimensions
    • Vetter, I. R. (2001) The guanine nucleotide-binding switch in three dimensions. Science 294, 1299-1304
    • (2001) Science , vol.294 , pp. 1299-1304
    • Vetter, I.R.1
  • 2
    • 0027732538 scopus 로고
    • Proteins regulating Ras and its relatives
    • Boguski, M. S., and McCormick, F. (1993) Proteins regulating Ras and its relatives. Nature 366, 643-654
    • (1993) Nature , vol.366 , pp. 643-654
    • Boguski, M.S.1    McCormick, F.2
  • 3
    • 0036210840 scopus 로고    scopus 로고
    • The actin filament architecture: Tightly regulated by the cells, manipulated by pathogens. International Titisee Conference on the actin cytoskeleton: From signalling to bacterial pathogenesis
    • Ahmadian, M. R., Wittinghofer, A., and Schmidt, G. (2002) The actin filament architecture: tightly regulated by the cells, manipulated by pathogens. International Titisee Conference on the actin cytoskeleton: from signalling to bacterial pathogenesis. EMBO Rep. 3, 214-218
    • (2002) EMBO Rep. , vol.3 , pp. 214-218
    • Ahmadian, M.R.1    Wittinghofer, A.2    Schmidt, G.3
  • 7
    • 68649121646 scopus 로고    scopus 로고
    • The RASopathies: Developmental syndromes of Ras/MAPK pathway dysregulation
    • Tidyman, W. E., and Rauen, K. A. (2009) The RASopathies: developmental syndromes of Ras/MAPK pathway dysregulation. Curr. Opin. Genet. Dev. 19, 230-236
    • (2009) Curr. Opin. Genet. Dev. , vol.19 , pp. 230-236
    • Tidyman, W.E.1    Rauen, K.A.2
  • 9
    • 84871533576 scopus 로고    scopus 로고
    • Diverging gain-of-function mechanisms of two novel KRAS mutations associated with Noonan and cardio-faciocutaneous syndromes
    • Cirstea, I. C., Gremer, L., Dvorsky, R., Zhang, S. C., Piekorz, R. P., Zenker, M., and Ahmadian, M. R. (2013) Diverging gain-of-function mechanisms of two novel KRAS mutations associated with Noonan and cardio-faciocutaneous syndromes. Hum. Mol. Genet. 22, 262-270
    • (2013) Hum. Mol. Genet. , vol.22 , pp. 262-270
    • Cirstea, I.C.1    Gremer, L.2    Dvorsky, R.3    Zhang, S.C.4    Piekorz, R.P.5    Zenker, M.6    Ahmadian, M.R.7
  • 10
    • 79960038169 scopus 로고    scopus 로고
    • Functional specificity of Ras isoforms: So similar but so different
    • Castellano, E., and Santos, E. (2011) Functional specificity of Ras isoforms: so similar but so different. Genes Cancer 2, 216-231
    • (2011) Genes Cancer , vol.2 , pp. 216-231
    • Castellano, E.1    Santos, E.2
  • 11
    • 77950346287 scopus 로고    scopus 로고
    • H-, N- and Kras cooperatively regulate lymphatic vessel growth by modulating VEGFR3 expression in lymphatic endothelial cells in mice
    • Ichise, T., Yoshida, N., and Ichise, H. (2010) H-, N- and Kras cooperatively regulate lymphatic vessel growth by modulating VEGFR3 expression in lymphatic endothelial cells in mice. Development 137, 1003-1013
    • (2010) Development , vol.137 , pp. 1003-1013
    • Ichise, T.1    Yoshida, N.2    Ichise, H.3
  • 12
    • 35648971073 scopus 로고    scopus 로고
    • Ras proteins: Paradigms for compartmentalised and isoform-specific signalling
    • Omerovic, J., Laude, A. J., and Prior, I. A. (2007) Ras proteins: paradigms for compartmentalised and isoform-specific signalling. Cell. Mol. Life Sci. 64, 2575-2589
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 2575-2589
    • Omerovic, J.1    Laude, A.J.2    Prior, I.A.3
  • 14
    • 0023098381 scopus 로고
    • Differential expression of the ras gene family in mice
    • Leon, J., Guerrero, I., and Pellicer, A. (1987) Differential expression of the ras gene family in mice. Mol. Cell. Biol. 7, 1535-1540
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 1535-1540
    • Leon, J.1    Guerrero, I.2    Pellicer, A.3
  • 17
    • 72449190516 scopus 로고    scopus 로고
    • Nonredundancy within the RAS oncogene family: Insights into mutational disparities in cancer
    • Lau, K. S., and Haigis, K. M. (2009) Nonredundancy within the RAS oncogene family: insights into mutational disparities in cancer. Mol. Cells 28, 315-320
    • (2009) Mol. Cells , vol.28 , pp. 315-320
    • Lau, K.S.1    Haigis, K.M.2
  • 18
    • 0038100185 scopus 로고    scopus 로고
    • Role of ERas in promoting tumour-like properties in mouse embryonic stem cells
    • Takahashi, K., Mitsui, K., and Yamanaka, S. (2003) Role of ERas in promoting tumour-like properties in mouse embryonic stem cells. Nature 423, 541-545
    • (2003) Nature , vol.423 , pp. 541-545
    • Takahashi, K.1    Mitsui, K.2    Yamanaka, S.3
  • 20
    • 77956548624 scopus 로고    scopus 로고
    • Resistance to chemotherapeutic agents and promotion of transforming activity mediated by embryonic stem cell-expressed Ras (ERas) signal in neuroblastoma cells
    • Aoyama, M., Kataoka, H., Kubota, E., Tada, T., and Asai, K. (2010) Resistance to chemotherapeutic agents and promotion of transforming activity mediated by embryonic stem cell-expressed Ras (ERas) signal in neuroblastoma cells. Int. J. Oncol. 37, 1011-1016
    • (2010) Int. J. Oncol. , vol.37 , pp. 1011-1016
    • Aoyama, M.1    Kataoka, H.2    Kubota, E.3    Tada, T.4    Asai, K.5
  • 22
    • 0021170342 scopus 로고
    • The p21 ras C-terminus is required for transformation and membrane association
    • Willumsen, B. M., Christensen, A., Hubbert, N. L., Papageorge, A. G., and Lowy, D. R. (1984) The p21 ras C-terminus is required for transformation and membrane association. Nature 310, 583-586
    • (1984) Nature , vol.310 , pp. 583-586
    • Willumsen, B.M.1    Christensen, A.2    Hubbert, N.L.3    Papageorge, A.G.4    Lowy, D.R.5
  • 24
    • 84898606304 scopus 로고    scopus 로고
    • KRas localizes to the plasma membrane by spatial cycles of solubilization, trapping and vesicular transport
    • Schmick, M., Vartak, N., Papke, B., Kovacevic, M., Truxius, D. C., Rossmannek, L., and Bastiaens, P. I. (2014) KRas localizes to the plasma membrane by spatial cycles of solubilization, trapping and vesicular transport. Cell 157, 459-471
    • (2014) Cell , vol.157 , pp. 459-471
    • Schmick, M.1    Vartak, N.2    Papke, B.3    Kovacevic, M.4    Truxius, D.C.5    Rossmannek, L.6    Bastiaens, P.I.7
  • 26
    • 28844506274 scopus 로고    scopus 로고
    • Role of the phosphoinositide 3-kinase pathway in mouse embryonic stem (ES) cells
    • Takahashi, K., Murakami, M., and Yamanaka, S. (2005) Role of the phosphoinositide 3-kinase pathway in mouse embryonic stem (ES) cells. Biochem. Soc. Trans. 33, 1522-1525
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 1522-1525
    • Takahashi, K.1    Murakami, M.2    Yamanaka, S.3
  • 28
    • 0028973293 scopus 로고
    • Ras CAAX peptidomimetic FTI-277 selectively blocks oncogenic Ras signaling by inducing cytoplasmic accumulation of inactive Ras-Raf complexes
    • Lerner, E. C., Qian, Y., Blaskovich, M. A., Fossum, R. D., Vogt, A., Sun, J., Cox, A. D., Der, C. J., Hamilton, A. D., and Sebti, S. M. (1995) Ras CAAX peptidomimetic FTI-277 selectively blocks oncogenic Ras signaling by inducing cytoplasmic accumulation of inactive Ras-Raf complexes. J. Biol. Chem. 270, 26802-26806
    • (1995) J. Biol. Chem. , vol.270 , pp. 26802-26806
    • Lerner, E.C.1    Qian, Y.2    Blaskovich, M.A.3    Fossum, R.D.4    Vogt, A.5    Sun, J.6    Cox, A.D.7    Der, C.J.8    Hamilton, A.D.9    Sebti, S.M.10
  • 29
    • 0034062812 scopus 로고    scopus 로고
    • H-ras but not K-ras traffics to the plasma membrane through the exocytic pathway
    • Apolloni, A., Prior, I. A., Lindsay, M., Parton, R. G., and Hancock, J. F. (2000) H-ras but not K-ras traffics to the plasma membrane through the exocytic pathway. Mol. Cell. Biol. 20, 2475-2487
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2475-2487
    • Apolloni, A.1    Prior, I.A.2    Lindsay, M.3    Parton, R.G.4    Hancock, J.F.5
  • 30
  • 31
    • 0030932131 scopus 로고    scopus 로고
    • Individual rate constants for the interaction of Ras proteins with GTPase-activating proteins determined by fluorescence spectroscopy
    • Ahmadian, M. R., Hoffmann, U., Goody, R. S., and Wittinghofer, A. (1997) Individual rate constants for the interaction of Ras proteins with GTPase-activating proteins determined by fluorescence spectroscopy. Biochemistry 36, 4535-4541
    • (1997) Biochemistry , vol.36 , pp. 4535-4541
    • Ahmadian, M.R.1    Hoffmann, U.2    Goody, R.S.3    Wittinghofer, A.4
  • 32
    • 0031231083 scopus 로고    scopus 로고
    • Confirmation of the arginine-finger hypothesis for the GAP-stimulated GTP-hydrolysis reaction of Ras
    • Ahmadian, M. R., Stege, P., Scheffzek, K., and Wittinghofer, A. (1997) Confirmation of the arginine-finger hypothesis for the GAP-stimulated GTP-hydrolysis reaction of Ras. Nat. Struct. Biol. 4, 686-689
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 686-689
    • Ahmadian, M.R.1    Stege, P.2    Scheffzek, K.3    Wittinghofer, A.4
  • 33
    • 0032546533 scopus 로고    scopus 로고
    • Kinetic analysis by fluorescence of the interaction between Ras and the catalytic domain of the guanine nucleotide exchange factor Cdc25Mm
    • Lenzen, C., Cool, R. H., Prinz, H., Kuhlmann, J., and Wittinghofer, A. (1998) Kinetic analysis by fluorescence of the interaction between Ras and the catalytic domain of the guanine nucleotide exchange factor Cdc25Mm. Biochemistry 37, 7420-7430
    • (1998) Biochemistry , vol.37 , pp. 7420-7430
    • Lenzen, C.1    Cool, R.H.2    Prinz, H.3    Kuhlmann, J.4    Wittinghofer, A.5
  • 34
    • 56049114699 scopus 로고    scopus 로고
    • Many faces of Ras activation
    • Buday, L., and Downward, J. (2008) Many faces of Ras activation. Biochim. Biophys. Acta 1786, 178-187
    • (2008) Biochim. Biophys. Acta , vol.1786 , pp. 178-187
    • Buday, L.1    Downward, J.2
  • 35
    • 0025010979 scopus 로고
    • The GTPase superfamily: A conserved switch for diverse cell functions
    • Bourne, H. R., Sanders, D. A., and McCormick, F. (1990) The GTPase superfamily: a conserved switch for diverse cell functions. Nature 348, 125-132
    • (1990) Nature , vol.348 , pp. 125-132
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 36
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne, H. R., Sanders, D. A., and McCormick, F. (1991) The GTPase superfamily: conserved structure and molecular mechanism. Nature 349, 117-127
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 37
    • 0025048136 scopus 로고
    • The P-loop - A common motif in ATP- and GTP-binding proteins
    • Saraste, M., Sibbald, P. R., and Wittinghofer, A. (1990) The P-loop-a common motif in ATP- and GTP-binding proteins. Trends Biochem. Sci. 15, 430-434
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 430-434
    • Saraste, M.1    Sibbald, P.R.2    Wittinghofer, A.3
  • 38
    • 0024376173 scopus 로고
    • ras oncogenes in human cancer: A review
    • Bos, J. L. (1989) ras oncogenes in human cancer: a review. Cancer Res. 49, 4682-4689
    • (1989) Cancer Res. , vol.49 , pp. 4682-4689
    • Bos, J.L.1
  • 39
    • 0037308836 scopus 로고    scopus 로고
    • Ras-effector interactions: After one decade
    • Herrmann, C. (2003) Ras-effector interactions: after one decade. Curr. Opin. Struct. Biol. 13, 122-129
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 122-129
    • Herrmann, C.1
  • 40
    • 0030046054 scopus 로고    scopus 로고
    • Biochemical and biological consequences of changing the specificity of p21ras from guanosine to xanthosine nucleotides
    • Schmidt, G., Lenzen, C., Simon, I., Deuter, R., Cool, R. H., Goody, R. S., and Wittinghofer, A. (1996) Biochemical and biological consequences of changing the specificity of p21ras from guanosine to xanthosine nucleotides. Oncogene 12, 87-96
    • (1996) Oncogene , vol.12 , pp. 87-96
    • Schmidt, G.1    Lenzen, C.2    Simon, I.3    Deuter, R.4    Cool, R.H.5    Goody, R.S.6    Wittinghofer, A.7
  • 41
    • 79959393264 scopus 로고    scopus 로고
    • Structure-function relationships of the G domain, a canonical switch motif
    • Wittinghofer, A., and Vetter, I. R. (2011) Structure-function relationships of the G domain, a canonical switch motif. Annu. Rev. Biochem. 80, 943-971
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 943-971
    • Wittinghofer, A.1    Vetter, I.R.2
  • 42
    • 25444450400 scopus 로고    scopus 로고
    • Differential membrane localization of ERas and Rheb, two Ras-related proteins involved in the phosphatidylinositol 3-kinase/mTOR pathway
    • Takahashi, K., Nakagawa, M., Young, S. G., and Yamanaka, S. (2005) Differential membrane localization of ERas and Rheb, two Ras-related proteins involved in the phosphatidylinositol 3-kinase/mTOR pathway. J. Biol. Chem. 280, 32768-32774
    • (2005) J. Biol. Chem. , vol.280 , pp. 32768-32774
    • Takahashi, K.1    Nakagawa, M.2    Young, S.G.3    Yamanaka, S.4
  • 43
    • 0022727887 scopus 로고
    • Expression of p21 proteins in Escherichia coli and stereochemistry of the nucleotide-binding site
    • Tucker, J., Sczakiel, G., Feuerstein, J., John, J., Goody, R. S., and Wittinghofer, A. (1986) Expression of p21 proteins in Escherichia coli and stereochemistry of the nucleotide-binding site. EMBO J. 5, 1351-1358
    • (1986) EMBO J. , vol.5 , pp. 1351-1358
    • Tucker, J.1    Sczakiel, G.2    Feuerstein, J.3    John, J.4    Goody, R.S.5    Wittinghofer, A.6
  • 45
    • 0344885558 scopus 로고    scopus 로고
    • Structural evidence for feedback activation by Ras. GTP of the Ras-specific nucleotide exchange factor SOS
    • Margarit, S. M., Sondermann, H., Hall, B. E., Nagar, B., Hoelz, A., Pirruccello, M., Bar-Sagi, D., and Kuriyan, J. (2003) Structural evidence for feedback activation by Ras. GTP of the Ras-specific nucleotide exchange factor SOS. Cell 112, 685-695
    • (2003) Cell , vol.112 , pp. 685-695
    • Margarit, S.M.1    Sondermann, H.2    Hall, B.E.3    Nagar, B.4    Hoelz, A.5    Pirruccello, M.6    Bar-Sagi, D.7    Kuriyan, J.8
  • 47
    • 77954758621 scopus 로고    scopus 로고
    • What makes Ras an efficient molecular switch: A computational, biophysical, and structural study of Ras-GDP interactions with mutants of Raf
    • Filchtinski, D., Sharabi, O., Rüppel, A., Vetter, I. R., Herrmann, C., and Shifman, J. M. (2010) What makes Ras an efficient molecular switch: a computational, biophysical, and structural study of Ras-GDP interactions with mutants of Raf. J. Mol. Biol. 399, 422-435
    • (2010) J. Mol. Biol. , vol.399 , pp. 422-435
    • Filchtinski, D.1    Sharabi, O.2    Rüppel, A.3    Vetter, I.R.4    Herrmann, C.5    Shifman, J.M.6
  • 50
    • 0031778630 scopus 로고    scopus 로고
    • Structural basis for the interaction of Ras with RalGDS
    • Huang, L., Hofer, F., Martin, G. S., and Kim, S. H. (1998) Structural basis for the interaction of Ras with RalGDS. Nat. Struct. Biol. 5, 422-426
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 422-426
    • Huang, L.1    Hofer, F.2    Martin, G.S.3    Kim, S.H.4
  • 52
    • 84881510335 scopus 로고    scopus 로고
    • Structural basis for the interaction of the adaptor protein grb14 with activated ras
    • Qamra, R., and Hubbard, S. R. (2013) Structural basis for the interaction of the adaptor protein grb14 with activated ras. PLoS One 8, e72473
    • (2013) PLoS One , vol.8
    • Qamra, R.1    Hubbard, S.R.2
  • 53
    • 47949124438 scopus 로고    scopus 로고
    • Novel type of Ras effector interaction established between tumour suppressor NORE1A and Ras switch II
    • Stieglitz, B., Bee, C., Schwarz, D., Yildiz, O., Moshnikova, A., Khokhlatchev, A., and Herrmann, C. (2008) Novel type of Ras effector interaction established between tumour suppressor NORE1A and Ras switch II. EMBO J. 27, 1995-2005
    • (2008) EMBO J. , vol.27 , pp. 1995-2005
    • Stieglitz, B.1    Bee, C.2    Schwarz, D.3    Yildiz, O.4    Moshnikova, A.5    Khokhlatchev, A.6    Herrmann, C.7
  • 54
    • 0032489384 scopus 로고    scopus 로고
    • Identification of Nore1 as a potential Ras effector
    • Vavvas, D., Li, X., Avruch, J., and Zhang, X. F. (1998) Identification of Nore1 as a potential Ras effector. J. Biol. Chem. 273, 5439-5442
    • (1998) J. Biol. Chem. , vol.273 , pp. 5439-5442
    • Vavvas, D.1    Li, X.2    Avruch, J.3    Zhang, X.F.4
  • 56
    • 79960055459 scopus 로고    scopus 로고
    • RAS interaction with PI3K: More than just another effector pathway
    • Castellano, E., and Downward, J. (2011) RAS interaction with PI3K: more than just another effector pathway. Genes Cancer 2, 261-274
    • (2011) Genes Cancer , vol.2 , pp. 261-274
    • Castellano, E.1    Downward, J.2
  • 57
    • 33751315308 scopus 로고    scopus 로고
    • Phospholipase Cε: Linking second messengers and small GTPases
    • Bunney, T. D., and Katan, M. (2006) Phospholipase Cε: linking second messengers and small GTPases. Trends Cell Biol. 16, 640-648
    • (2006) Trends Cell Biol. , vol.16 , pp. 640-648
    • Bunney, T.D.1    Katan, M.2
  • 58
    • 0032508517 scopus 로고    scopus 로고
    • Ras isoforms vary in their ability to activate Raf-1 and phosphoinositide 3-kinase
    • Yan, J., Roy, S., Apolloni, A., Lane, A., and Hancock, J. F. (1998) Ras isoforms vary in their ability to activate Raf-1 and phosphoinositide 3-kinase. J. Biol. Chem. 273, 24052-24056
    • (1998) J. Biol. Chem. , vol.273 , pp. 24052-24056
    • Yan, J.1    Roy, S.2    Apolloni, A.3    Lane, A.4    Hancock, J.F.5
  • 62
    • 0024406286 scopus 로고
    • All ras proteins are polyisoprenylated but only some are palmitoylated
    • Hancock, J. F., Magee, A. I., Childs, J. E., and Marshall, C. J. (1989) All ras proteins are polyisoprenylated but only some are palmitoylated. Cell 57, 1167-1177
    • (1989) Cell , vol.57 , pp. 1167-1177
    • Hancock, J.F.1    Magee, A.I.2    Childs, J.E.3    Marshall, C.J.4
  • 63
    • 33644856168 scopus 로고    scopus 로고
    • Distinct utilization of effectors and biological outcomes resulting from site-specific Ras activation: Ras functions in lipid rafts and Golgi complex are dispensable for proliferation and transformation
    • Matallanas, D., Sanz-Moreno, V., Arozarena, I., Calvo, F., Agudo-Ibáñez, L., Santos, E., Berciano, M. T., and Crespo, P. (2006) Distinct utilization of effectors and biological outcomes resulting from site-specific Ras activation: Ras functions in lipid rafts and Golgi complex are dispensable for proliferation and transformation. Mol. Cell. Biol. 26, 100-116
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 100-116
    • Matallanas, D.1    Sanz-Moreno, V.2    Arozarena, I.3    Calvo, F.4    Agudo-Ibáñez, L.5    Santos, E.6    Berciano, M.T.7    Crespo, P.8
  • 66
  • 67
    • 0032509356 scopus 로고    scopus 로고
    • Separation of "glycosphingolipid signaling domain" from caveolin-containing membrane fraction in mouse melanoma B16 cells and its role in cell adhesion coupled with signaling
    • Iwabuchi, K., Handa, K., and Hakomori, S. (1998) Separation of "glycosphingolipid signaling domain" from caveolin-containing membrane fraction in mouse melanoma B16 cells and its role in cell adhesion coupled with signaling. J. Biol. Chem. 273, 33766-33773
    • (1998) J. Biol. Chem. , vol.273 , pp. 33766-33773
    • Iwabuchi, K.1    Handa, K.2    Hakomori, S.3
  • 68
    • 0037016758 scopus 로고    scopus 로고
    • The linker domain of the Ha-Ras hypervariable region regulates interactions with exchange factors, Raf-1 and phosphoinositide 3-kinase
    • Jaumot, M., Yan, J., Clyde-Smith, J., Sluimer, J., and Hancock, J. F. (2002) The linker domain of the Ha-Ras hypervariable region regulates interactions with exchange factors, Raf-1 and phosphoinositide 3-kinase. J. Biol. Chem. 277, 272-278
    • (2002) J. Biol. Chem. , vol.277 , pp. 272-278
    • Jaumot, M.1    Yan, J.2    Clyde-Smith, J.3    Sluimer, J.4    Hancock, J.F.5
  • 69
    • 0037455589 scopus 로고    scopus 로고
    • Direct visualization of Ras proteins in spatially distinct cell surface microdomains
    • Prior, I. A., Muncke, C., Parton, R. G., and Hancock, J. F. (2003) Direct visualization of Ras proteins in spatially distinct cell surface microdomains. J. Cell Biol. 160, 165-170
    • (2003) J. Cell Biol. , vol.160 , pp. 165-170
    • Prior, I.A.1    Muncke, C.2    Parton, R.G.3    Hancock, J.F.4
  • 70
    • 0034998678 scopus 로고    scopus 로고
    • Compartmentalization of Ras proteins
    • Prior, I. A., and Hancock, J. F. (2001) Compartmentalization of Ras proteins. J. Cell Sci. 114, 1603-1608
    • (2001) J. Cell Sci. , vol.114 , pp. 1603-1608
    • Prior, I.A.1    Hancock, J.F.2
  • 71
    • 3242657115 scopus 로고    scopus 로고
    • Three separable domains regulate GTP-dependent association of H-ras with the plasma membrane
    • Rotblat, B., Prior, I. A., Muncke, C., Parton, R. G., Kloog, Y., Henis, Y. I., and Hancock, J. F. (2004) Three separable domains regulate GTP-dependent association of H-ras with the plasma membrane. Mol. Cell. Biol. 24, 6799-6810
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 6799-6810
    • Rotblat, B.1    Prior, I.A.2    Muncke, C.3    Parton, R.G.4    Kloog, Y.5    Henis, Y.I.6    Hancock, J.F.7
  • 73
    • 0037148505 scopus 로고    scopus 로고
    • Vav3 modulates B cell receptor responses by regulating phosphoinositide 3-kinase activation
    • Inabe, K., Ishiai, M., Scharenberg, A. M., Freshney, N., Downward, J., and Kurosaki, T. (2002) Vav3 modulates B cell receptor responses by regulating phosphoinositide 3-kinase activation. J. Exp. Med. 195, 189-200
    • (2002) J. Exp. Med. , vol.195 , pp. 189-200
    • Inabe, K.1    Ishiai, M.2    Scharenberg, A.M.3    Freshney, N.4    Downward, J.5    Kurosaki, T.6
  • 75
    • 18244390470 scopus 로고    scopus 로고
    • The unique N-terminus of R-ras is required for Rac activation and precise regulation of cell migration
    • Holly, S. P., Larson, M. K., and Parise, L. V. (2005) The unique N-terminus of R-ras is required for Rac activation and precise regulation of cell migration. Mol. Biol. Cell 16, 2458-2469
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2458-2469
    • Holly, S.P.1    Larson, M.K.2    Parise, L.V.3
  • 77
    • 84873676027 scopus 로고    scopus 로고
    • Deciphering the molecular and functional basis of Dbl family proteins: A novel systematic approach toward classification of selective activation of the Rho family proteins
    • Jaiswal, M., Dvorsky, R., and Ahmadian, M. R. (2013) Deciphering the molecular and functional basis of Dbl family proteins: a novel systematic approach toward classification of selective activation of the Rho family proteins. J. Biol. Chem. 288, 4486-4500
    • (2013) J. Biol. Chem. , vol.288 , pp. 4486-4500
    • Jaiswal, M.1    Dvorsky, R.2    Ahmadian, M.R.3
  • 81
    • 33646034613 scopus 로고    scopus 로고
    • A phosphatase holoenzyme comprised of Shoc2/Sur8 and the catalytic subunit of PP1 functions as an M-Ras effector to modulate Raf activity
    • Rodriguez-Viciana, P., Oses-Prieto, J., Burlingame, A., Fried, M., and McCormick, F. (2006) A phosphatase holoenzyme comprised of Shoc2/Sur8 and the catalytic subunit of PP1 functions as an M-Ras effector to modulate Raf activity. Mol. Cell 22, 217-230
    • (2006) Mol. Cell , vol.22 , pp. 217-230
    • Rodriguez-Viciana, P.1    Oses-Prieto, J.2    Burlingame, A.3    Fried, M.4    McCormick, F.5
  • 82
    • 78751487053 scopus 로고    scopus 로고
    • RalGDS family members couple Ras to Ral signalling and that's not all
    • Ferro, E., and Trabalzini, L. (2010) RalGDS family members couple Ras to Ral signalling and that's not all. Cell. Signal. 22, 1804-1810
    • (2010) Cell. Signal. , vol.22 , pp. 1804-1810
    • Ferro, E.1    Trabalzini, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.