메뉴 건너뛰기




Volumn 47, Issue 5, 2006, Pages 883-891

CAAX modification and membrane targeting of Ras

Author keywords

Carboxyl methylation; Farnesylation; Trafficking

Indexed keywords

GERANYLGERANYLTRANSFERASE TYPE I; GERANYLGERANYLTRANSFERASE TYPE-I; GUANINE NUCLEOTIDE DISSOCIATION INHIBITOR; P21(RAS) FARNESYL PROTEIN TRANSFERASE; P21(RAS) FARNESYL-PROTEIN TRANSFERASE; RAS PROTEIN; RHO GUANINE NUCLEOTIDE DISSOCIATION INHIBITORS; TRANSFERASE;

EID: 33646777423     PISSN: 00222275     EISSN: 15397262     Source Type: Journal    
DOI: 10.1194/jlr.R600004-JLR200     Document Type: Review
Times cited : (280)

References (67)
  • 1
    • 33644748133 scopus 로고    scopus 로고
    • Thematic review series: Lipid posttranslational modifications: Structural biology of protein farnesyltransferase and geranylgeranyltransferase type-I
    • Lane, K. T., and L. S. Beese. 2006. Thematic review series: lipid posttranslational modifications: structural biology of protein farnesyltransferase and geranylgeranyltransferase type-I. J. Lipid Res. 47: 681-699.
    • (2006) J. Lipid Res. , vol.47 , pp. 681-699
    • Lane, K.T.1    Beese, L.S.2
  • 2
    • 30844467746 scopus 로고    scopus 로고
    • Thematic review series: Lipid posttranslational modifications. Farnesyl transferase inhibitors
    • Basso, A. D., P. Kirschmeier, and W. R. Bishop. 2006. Thematic review series: lipid posttranslational modifications. Farnesyl transferase inhibitors. J. Lipid Res. 47: 15-31.
    • (2006) J. Lipid Res. , vol.47 , pp. 15-31
    • Basso, A.D.1    Kirschmeier, P.2    Bishop, W.R.3
  • 3
    • 0021170342 scopus 로고
    • The p21 ras C-terminus is required for transformation and membrane association
    • Willumsen, B. M., A. Christensen, N. L. Hubbert, A. G. Papageorge, and D. R. Lowy. 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
  • 4
    • 0025183869 scopus 로고
    • Evidence for an S-farnesylcysteine methyl ester at the carboxyl terminus of the Saccharomyces cerevisiae RAS2 protein
    • Stimmel, J. B., R. J. Deschenes, C. Volker, J. Stock, and S. Clarke. 1990. Evidence for an S-farnesylcysteine methyl ester at the carboxyl terminus of the Saccharomyces cerevisiae RAS2 protein. Biochemistry. 29: 9651-9659.
    • (1990) Biochemistry , vol.29 , pp. 9651-9659
    • Stimmel, J.B.1    Deschenes, R.J.2    Volker, C.3    Stock, J.4    Clarke, S.5
  • 5
    • 0000081175 scopus 로고
    • Posttranslational modification of the Ha-ras oncogene protein: Evidence for a third class of protein carboxyl methyltransferases
    • Clarke, S., J. P. Vogel, R. J. Deschenes, and J. B. Stock. 1988. Posttranslational modification of the Ha-ras oncogene protein: evidence for a third class of protein carboxyl methyltransferases. Proc. Natl. Acad. Sci. USA. 85: 4643-4647.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 4643-4647
    • Clarke, S.1    Vogel, J.P.2    Deschenes, R.J.3    Stock, J.B.4
  • 6
    • 0022657845 scopus 로고
    • Direct identification of palmitic acid as the lipid attached to p21ras
    • Buss, J. E., and B. M. Sefton. 1986. Direct identification of palmitic acid as the lipid attached to p21ras. Mol. Cell. Biol. 6: 116-122.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 116-122
    • Buss, J.E.1    Sefton, B.M.2
  • 7
    • 0024406286 scopus 로고
    • All ras proteins are polyisoprenylated but only some are palmitoylated
    • Hancock, J. F., A. I. Magee, J. E. Childs, and C. J. Marshall. 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
  • 8
    • 0030909336 scopus 로고    scopus 로고
    • Modulation of Ras and a-factor function by carboxyl-terminal proteolysis
    • Boyartchuk, V. L., M. N. Ashby, and J. Rine. 1997. Modulation of Ras and a-factor function by carboxyl-terminal proteolysis. Science. 275: 1796-1800.
    • (1997) Science , vol.275 , pp. 1796-1800
    • Boyartchuk, V.L.1    Ashby, M.N.2    Rine, J.3
  • 9
    • 0025764049 scopus 로고
    • The Saccharomyces cerevisiae STE14 gene encodes a methyltransferase that modulates C-terminal methylation of a-factor and RAS proteins
    • Hrycyna, C. A., S. K. Sapperstein, S. Clarke, and S. Michaelis. 1991. The Saccharomyces cerevisiae STE14 gene encodes a methyltransferase that modulates C-terminal methylation of a-factor and RAS proteins. EMBO J. 10: 1699-1709.
    • (1991) EMBO J. , vol.10 , pp. 1699-1709
    • Hrycyna, C.A.1    Sapperstein, S.K.2    Clarke, S.3    Michaelis, S.4
  • 11
    • 0022388682 scopus 로고
    • Methyl-esterified proteins in a mammalian cell line
    • Chelsky, D., B. Ruskin, and D. E. Koshland. 1985. Methyl-esterified proteins in a mammalian cell line. Biochemistry. 24: 6651-6658.
    • (1985) Biochemistry , vol.24 , pp. 6651-6658
    • Chelsky, D.1    Ruskin, B.2    Koshland, D.E.3
  • 15
    • 0037174987 scopus 로고    scopus 로고
    • Identification of a Ras palmitoyltransferase in Saccharomyces cerevisiae
    • Lobo, S., W. K. Greentree, M. E. Linder, and R. J. Deschenes. 2002. Identification of a Ras palmitoyltransferase in Saccharomyces cerevisiae. J. Biol. Chem. 277: 41268-41273.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41268-41273
    • Lobo, S.1    Greentree, W.K.2    Linder, M.E.3    Deschenes, R.J.4
  • 16
    • 24744466287 scopus 로고    scopus 로고
    • DHHC9 and GCP16 constitute a human protein fatty acyltransferase with specificity for H- And N-Ras
    • Swarthout, J. T., S. Lobo, L. Farh, M. R. Croke, W. K. Greentree, R. J. Deschenes, and M. E. Linder. 2005. DHHC9 and GCP16 constitute a human protein fatty acyltransferase with specificity for H- and N-Ras. J. Biol. Chem. 280: 31141-31148.
    • (2005) J. Biol. Chem. , vol.280 , pp. 31141-31148
    • Swarthout, J.T.1    Lobo, S.2    Farh, L.3    Croke, M.R.4    Greentree, W.K.5    Deschenes, R.J.6    Linder, M.E.7
  • 18
    • 0036732940 scopus 로고    scopus 로고
    • Membrane trafficking of heterotrimeric G proteins via the endoplasmic reticulum and Golgi
    • Michaelson, D., I. Ahearn, M. Bergo, S. Young, and M. Philips. 2002. Membrane trafficking of heterotrimeric G proteins via the endoplasmic reticulum and Golgi. Mol. Biol. Cell. 13: 3294-3302.
    • (2002) Mol. Biol. Cell. , vol.13 , pp. 3294-3302
    • Michaelson, D.1    Ahearn, I.2    Bergo, M.3    Young, S.4    Philips, M.5
  • 19
    • 0033621812 scopus 로고    scopus 로고
    • Interaction with Gbetagamma is required for membrane targeting and palmitoylation of Galpha(s) and Galpha(q)
    • Evanko, D. S., M. M. Thiyagarajan, and P. B. Wedegaertner. 2000. Interaction with Gbetagamma is required for membrane targeting and palmitoylation of Galpha(s) and Galpha(q). J. Biol. Chem. 275: 1327-1336.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1327-1336
    • Evanko, D.S.1    Thiyagarajan, M.M.2    Wedegaertner, P.B.3
  • 20
    • 0031858844 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae prenylcysteine carboxyl methyltransferase Ste14p is in the endoplasmic reticulum membrane
    • Romano, J. D., W. K. Schmidt, and S. Michaelis. 1998. The Saccharomyces cerevisiae prenylcysteine carboxyl methyltransferase Ste14p is in the endoplasmic reticulum membrane. Mol. Biol. Cell. 9: 2231-2247.
    • (1998) Mol. Biol. Cell. , vol.9 , pp. 2231-2247
    • Romano, J.D.1    Schmidt, W.K.2    Michaelis, S.3
  • 21
    • 0032530150 scopus 로고    scopus 로고
    • Endoplasmic reticulum membrane localization of Rce1p and Ste24p, yeast proteases involved in carboxyl-terminal CAAX protein processing and amino-terminal a-factor cleavage
    • Schmidt, W. K., A. Tam, K. Fujimura-Kamada, and S. Michaelis. 1998. Endoplasmic reticulum membrane localization of Rce1p and Ste24p, yeast proteases involved in carboxyl-terminal CAAX protein processing and amino-terminal a-factor cleavage. Proc. Natl. Acad. Sci. USA. 95: 11175-11180.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11175-11180
    • Schmidt, W.K.1    Tam, A.2    Fujimura-Kamada, K.3    Michaelis, S.4
  • 23
    • 0034062812 scopus 로고    scopus 로고
    • H-ras but not K-ras traffics to the plasma membrane through the exocytic pathway
    • Apolloni, A., I. A. Prior, M. Lindsay, R. G. Parton, and J. F. Hancock. 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
  • 24
    • 0041689887 scopus 로고    scopus 로고
    • Palmitoylation and plasma membrane localization of Ras2p by a nonclassical trafficking pathway in Saccharomyces cerevisiae
    • Dong, X., D. A. Mitchell, S. Lobo, L. Zhao, D. J. Bartels, and R. J. Deschenes. 2003. Palmitoylation and plasma membrane localization of Ras2p by a nonclassical trafficking pathway in Saccharomyces cerevisiae. Mol. Cell. Biol. 23: 6574-6584.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 6574-6584
    • Dong, X.1    Mitchell, D.A.2    Lobo, S.3    Zhao, L.4    Bartels, D.J.5    Deschenes, R.J.6
  • 25
    • 0028196986 scopus 로고
    • Fluorimetric evaluation of the affinities of isoprenylated peptides for lipid bilayers
    • Silvius, J. R., and F. l'Heureux. 1994. Fluorimetric evaluation of the affinities of isoprenylated peptides for lipid bilayers. Biochemistry. 33: 3014-3022.
    • (1994) Biochemistry , vol.33 , pp. 3014-3022
    • Silvius, J.R.1    L'Heureux, F.2
  • 27
    • 0035825193 scopus 로고    scopus 로고
    • Differential localization of Rho GTPases in live cells. Regulation by hypervariable regions and RhoGDI binding
    • Michaelson, D., J. Silletti, G. Murphy, P. D'Eustachio, M. Rush, and M. R. Philips. 2001. Differential localization of Rho GTPases in live cells. Regulation by hypervariable regions and RhoGDI binding. J. Cell Biol. 152: 111-126.
    • (2001) J. Cell Biol. , vol.152 , pp. 111-126
    • Michaelson, D.1    Silletti, J.2    Murphy, G.3    D'Eustachio, P.4    Rush, M.5    Philips, M.R.6
  • 28
    • 33646773289 scopus 로고    scopus 로고
    • Intracellular targeting of Rho family GTPases: Implications of localization on function
    • M. Symon, editor. Kluwer Academic/Plenum Publishers, New York
    • Michaelson, D., M. Rush, and M. R. Philips. 2003. Intracellular targeting of Rho family GTPases: implications of localization on function. In M. Symon, editor. Rho GTPases. Kluwer Academic/Plenum Publishers, New York. 17-31.
    • (2003) Rho GTPases , pp. 17-31
    • Michaelson, D.1    Rush, M.2    Philips, M.R.3
  • 29
    • 0034603198 scopus 로고    scopus 로고
    • Structure of the Rho family GTP-binding protein Cdc42 in complex with the multifunctional regulator RhoGDI
    • Hoffman, G. R., N. Nassar, and R. A. Cerione. 2000. Structure of the Rho family GTP-binding protein Cdc42 in complex with the multifunctional regulator RhoGDI. Cell. 100: 345-356.
    • (2000) Cell , vol.100 , pp. 345-356
    • Hoffman, G.R.1    Nassar, N.2    Cerione, R.A.3
  • 30
    • 0024465343 scopus 로고
    • Post-translational processing of p21ras is two-step and involves carboxyl-methylation and carboxyl-terminal proteolysis
    • Gutierrez, L., A. I. Magee, C. J. Marshall, and J. F. Hancock. 1989. Post-translational processing of p21ras is two-step and involves carboxyl-methylation and carboxyl-terminal proteolysis. EMBO J. 8: 1093-1098.
    • (1989) EMBO J. , vol.8 , pp. 1093-1098
    • Gutierrez, L.1    Magee, A.I.2    Marshall, C.J.3    Hancock, J.F.4
  • 31
    • 0037177881 scopus 로고    scopus 로고
    • The delta subunit of retinal rod cGMP phosphodiesterase regulates the membrane association of Ras and Rap GTPases
    • Nancy, V., I. Callebaut, A. El Marjou, and J. de Gunzburg. 2002. The delta subunit of retinal rod cGMP phosphodiesterase regulates the membrane association of Ras and Rap GTPases. J. Biol. Chem. 277: 15076-15084.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15076-15084
    • Nancy, V.1    Callebaut, I.2    El Marjou, A.3    De Gunzburg, J.4
  • 32
    • 0035958898 scopus 로고    scopus 로고
    • Prenylated Rab acceptor protein is a receptor for prenylated small GTPases
    • Figueroa, C., J. Taylor, and A. B. Vojtek. 2001. Prenylated Rab acceptor protein is a receptor for prenylated small GTPases. J. Biol. Chem. 276: 28219-28225.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28219-28225
    • Figueroa, C.1    Taylor, J.2    Vojtek, A.B.3
  • 33
    • 0035829731 scopus 로고    scopus 로고
    • Galectin-1 binds oncogenic H-Ras to mediate Ras membrane anhorage and cell transformation
    • Paz, A., R. Haklai, G. Elad-Sfadia, E. Ballan, and Y. Kloog. 2001. Galectin-1 binds oncogenic H-Ras to mediate Ras membrane anhorage and cell transformation. Oncogene. 20: 7486-7493.
    • (2001) Oncogene , vol.20 , pp. 7486-7493
    • Paz, A.1    Haklai, R.2    Elad-Sfadia, G.3    Ballan, E.4    Kloog, Y.5
  • 34
    • 0037455589 scopus 로고    scopus 로고
    • Direct visualization of Ras proteins in spatially distinct cell surface microdomains
    • Prior, I. A., C. Muncke, R. G. Parton, and J. F. Hancock. 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
  • 35
    • 22144479017 scopus 로고    scopus 로고
    • Ras plasma membrane signalling platforms
    • Hancock, J. F., and R. G. Parton. 2005. Ras plasma membrane signalling platforms. Biochem. J. 389: 1-11.
    • (2005) Biochem. J. , vol.389 , pp. 1-11
    • Hancock, J.F.1    Parton, R.G.2
  • 36
    • 0035067187 scopus 로고    scopus 로고
    • GTP-dependent segregation of H-ras from lipid rafts is required for biological activity
    • Prior, I. A., A. Harding, J. Yan, J. Sluimer, R. G. Parton, and J. F. Hancock. 2001. GTP-dependent segregation of H-ras from lipid rafts is required for biological activity. Nat. Cell Biol. 3: 368-375.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 368-375
    • Prior, I.A.1    Harding, A.2    Yan, J.3    Sluimer, J.4    Parton, R.G.5    Hancock, J.F.6
  • 38
    • 0028915903 scopus 로고
    • Depalmitoylation of CAAX motif proteins. Protein structural determinants of palmitate turnover rate
    • Lu, J. Y., and S. L. Hofmann. 1995. Depalmitoylation of CAAX motif proteins. Protein structural determinants of palmitate turnover rate. J. Biol. Chem. 270: 7251-7256.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7251-7256
    • Lu, J.Y.1    Hofmann, S.L.2
  • 39
    • 0038143229 scopus 로고    scopus 로고
    • Distinct rates of palmitate turnover on membrane-bound cellular and oncogenic H-ras
    • Baker, T. L., H. Zheng, J. Walker, J. L. Coloff, and J. E. Buss. 2003. Distinct rates of palmitate turnover on membrane-bound cellular and oncogenic H-ras. J. Biol. Chem. 278: 19292-19300.
    • (2003) J. Biol. Chem. , vol.278 , pp. 19292-19300
    • Baker, T.L.1    Zheng, H.2    Walker, J.3    Coloff, J.L.4    Buss, J.E.5
  • 46
    • 0029058605 scopus 로고
    • The myristoyl-electrostatic switch: A modulator of reversible protein-membrane interactions
    • McLaughlin, S., and A. Aderem. 1995. The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions. Trends Biochem. Sci. 20: 272-276.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 272-276
    • McLaughlin, S.1    Aderem, A.2
  • 47
    • 30044431691 scopus 로고    scopus 로고
    • K-ras4B and prenylated proteins lacking "second signals" associate dynamically with cellular membranes
    • Silvius, J. R., P. Bhagatji, R. Leventis, and D. Terrone. 2006. K-ras4B and prenylated proteins lacking "second signals" associate dynamically with cellular membranes. Mol. Biol. Cell. 17: 192-202.
    • (2006) Mol. Biol. Cell. , vol.17 , pp. 192-202
    • Silvius, J.R.1    Bhagatji, P.2    Leventis, R.3    Terrone, D.4
  • 48
    • 0029842109 scopus 로고    scopus 로고
    • Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP
    • Choi, J., J. Chen, S. L. Schreiber, and J. Clardy. 1996. Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP. Science. 273: 239-242.
    • (1996) Science. , vol.273 , pp. 239-242
    • Choi, J.1    Chen, J.2    Schreiber, S.L.3    Clardy, J.4
  • 50
    • 0036301339 scopus 로고    scopus 로고
    • Prenylcysteine carboxylmethyltransferase is essential for the earliest stages of liver development in mice
    • Lin, X., J. Jung, D. Kang, B. Xu, K. S. Zaret, and H. Zoghbi. 2002. Prenylcysteine carboxylmethyltransferase is essential for the earliest stages of liver development in mice. Gastroenterology. 123: 345-351.
    • (2002) Gastroenterology , vol.123 , pp. 345-351
    • Lin, X.1    Jung, J.2    Kang, D.3    Xu, B.4    Zaret, K.S.5    Zoghbi, H.6
  • 52
    • 0033605596 scopus 로고    scopus 로고
    • Disruption of the mouse Rce1 gene results in defective Ras processing and mislocalization of Ras within cells
    • Kim, E., P. Ambroziak, J. C. Otto, B. Taylor, M. Ashby, K. Shannon, P. J. Casey, and S. G. Young. 1999. Disruption of the mouse Rce1 gene results in defective Ras processing and mislocalization of Ras within cells. J. Biol. Chem. 274: 8383-8390.
    • (1999) J. Biol. Chem. , vol.274 , pp. 8383-8390
    • Kim, E.1    Ambroziak, P.2    Otto, J.C.3    Taylor, B.4    Ashby, M.5    Shannon, K.6    Casey, P.J.7    Young, S.G.8
  • 54
    • 0027983602 scopus 로고
    • Effects of carboxyl methylation of photoreceptor G protein gamma-subunit in visual transduction
    • Fukada, Y., T. Matsuda, K. Kokame, T. Takao, Y. Shimonishi, T. Akino, and T. Yoshizawa. 1994. Effects of carboxyl methylation of photoreceptor G protein gamma-subunit in visual transduction. J. Biol. Chem. 269: 5163-5170.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5163-5170
    • Fukada, Y.1    Matsuda, T.2    Kokame, K.3    Takao, T.4    Shimonishi, Y.5    Akino, T.6    Yoshizawa, T.7
  • 55
    • 0029940468 scopus 로고    scopus 로고
    • The role of G protein methylation in the function of a geranylgeranylated beta gamma isoform
    • Parish, C. A., A. V. Smrcka, and R. R. Rando. 1996. The role of G protein methylation in the function of a geranylgeranylated beta gamma isoform. Biochemistry. 35: 7499-7505.
    • (1996) Biochemistry , vol.35 , pp. 7499-7505
    • Parish, C.A.1    Smrcka, A.V.2    Rando, R.R.3
  • 56
    • 0027932723 scopus 로고
    • Functional significance of G protein carboxymethylation
    • Parish, C. A., and R. R. Rando. 1994. Functional significance of G protein carboxymethylation. Biochemistry. 33: 9986-9991.
    • (1994) Biochemistry , vol.33 , pp. 9986-9991
    • Parish, C.A.1    Rando, R.R.2
  • 59
    • 1842609782 scopus 로고    scopus 로고
    • Ras activation in Jurkat T cells following low-grade stimulation of the T-cell receptor is specific to N-Ras and occurs only on the Golgi
    • Pérez de Castro, I., T. Bivona, M. Philips, and A. Pellicer. 2004. Ras activation in Jurkat T cells following low-grade stimulation of the T-cell receptor is specific to N-Ras and occurs only on the Golgi. Mol. Cell. Biol. 24: 3485-3496.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 3485-3496
    • Pérez De Castro, I.1    Bivona, T.2    Philips, M.3    Pellicer, A.4
  • 60
    • 0042858184 scopus 로고    scopus 로고
    • Exchange factors of the RasGRP family mediate Ras activation in the Golgi
    • Caloca, M. J., J. L. Zugaza, and X. R. Bustelo. 2003. Exchange factors of the RasGRP family mediate Ras activation in the Golgi. J. Biol. Chem. 278: 33465-33473.
    • (2003) J. Biol. Chem. , vol.278 , pp. 33465-33473
    • Caloca, M.J.1    Zugaza, J.L.2    Bustelo, X.R.3
  • 62
    • 33644856168 scopus 로고    scopus 로고
    • Distinct utilization of effectors and biological outcomes resulting from sitespecific Ras activation: Ras functions in lipid rafts and Golgi complex are dispensable for proliferation and transformation
    • Matallanas, D., V. Sanz-Moreno, I. Arozarena, F. Calvo, L. Agudo-Ibanez, E. Santos, M. T. Berciano, and P. Crespo. 2006. Distinct utilization of effectors and biological outcomes resulting from sitespecific 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-Ibanez, L.5    Santos, E.6    Berciano, M.T.7    Crespo, P.8
  • 64
    • 0347320784 scopus 로고    scopus 로고
    • Geranylgeranyltransferase I inhibitor GGTI-2154 induces breast carcinoma apoptosis and tumor regression in H-Ras transgenic mice
    • Sun, J., J. Ohkanda, D. Coppola, H. Yin, M. Kothare, B. Busciglio, A. D. Hamilton, and S. M. Sebti. 2003. Geranylgeranyltransferase I inhibitor GGTI-2154 induces breast carcinoma apoptosis and tumor regression in H-Ras transgenic mice. Cancer Res. 63: 8922-8929.
    • (2003) Cancer Res. , vol.63 , pp. 8922-8929
    • Sun, J.1    Ohkanda, J.2    Coppola, D.3    Yin, H.4    Kothare, M.5    Busciglio, B.6    Hamilton, A.D.7    Sebti, S.M.8
  • 65
    • 18344394166 scopus 로고    scopus 로고
    • Post-prenylation-processing enzymes as new targets in oncogenesis
    • Winter-Vann,A.M., and P. J.Casey. 2005. Post-prenylation-processing enzymes as new targets in oncogenesis. Nat. Rev. Cancer. 5: 405-412.
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 405-412
    • Winter-Vann, A.M.1    Casey, P.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.