메뉴 건너뛰기




Volumn 65, Issue 2, 2005, Pages 507-515

The COOH-terminal end of R-Ras alters the motility and morphology of breast epithelial cells through Rho/Rho-kinase

Author keywords

[No Author keywords available]

Indexed keywords

4 (1 AMINOETHYL) N (4 PYRIDYL)CYCLOHEXANECARBOXAMIDE; CARBOXYLIC ACID; COLLAGEN TYPE 1; MYOSIN LIGHT CHAIN; PAXILLIN; PROTEIN CDC42; RAC1 PROTEIN; RAS PROTEIN; RHO KINASE; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 12544252253     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (34)

References (41)
  • 1
    • 0023390847 scopus 로고
    • Heterologous expression and characterization of the human R-Ras gene product
    • Lowe DG Goeddel DV. Heterologous expression and characterization of the human R-Ras gene product. Mol Cell Biol 1981;7:2845-56.
    • (1981) Mol Cell Biol , vol.7 , pp. 2845-2856
    • Lowe, D.G.1    Goeddel, D.V.2
  • 2
    • 0027470176 scopus 로고
    • Different structural organization of Ras and Rho effector domains
    • Self AJ, Paterson HF, Hall A. Different structural organization of Ras and Rho effector domains. Oncogene 1993;8:655-61.
    • (1993) Oncogene , vol.8 , pp. 655-661
    • Self, A.J.1    Paterson, H.F.2    Hall, A.3
  • 3
    • 0027465064 scopus 로고
    • Epidermal growth factor regulates the exchange rate of guanine nucleotides on p21Ras on fibroblasts
    • Buday L, Downward J. Epidermal growth factor regulates the exchange rate of guanine nucleotides on p21Ras on fibroblasts. Mol Cell Biol 1993;13:1903-10.
    • (1993) Mol Cell Biol , vol.13 , pp. 1903-1910
    • Buday, L.1    Downward, J.2
  • 4
    • 0028144704 scopus 로고
    • R-Ras interacts with RasGAP, neurofibromin and c-Raf but does not regulate cell growth or differentiation
    • Rey I, Taylor HP, Van Erp EH, Hall A. R-Ras interacts with RasGAP, neurofibromin and c-Raf but does not regulate cell growth or differentiation. Oncogene 1994;9:685-92.
    • (1994) Oncogene , vol.9 , pp. 685-692
    • Rey, I.1    Taylor, H.P.2    Van Erp, E.H.3    Hall, A.4
  • 5
    • 0028577298 scopus 로고
    • Identification of the guanine nucleotide dissociation stimulator for Ra1 as a putative effector molecule of R-ras, H-ras, K-ras, and Rap
    • Spaargaren M, Bischoff JR. Identification of the guanine nucleotide dissociation stimulator for Ra1 as a putative effector molecule of R-ras, H-ras, K-ras, and Rap. Proc Natl Acad Sci U S A 1994;91:12609-13.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 12609-12613
    • Spaargaren, M.1    Bischoff, J.R.2
  • 6
    • 0032524389 scopus 로고    scopus 로고
    • RasGRP, a Ras guanyl nucleotide-releasing protein with calcium- and diacylglycerol-binding motifs
    • Ebinu JO, Bottoroff DA, Chan EY, Stang SL, Dunn RJ, Stone JC. RasGRP, a Ras guanyl nucleotide-releasing protein with calcium- and diacylglycerol-binding motifs. Science 1998;280:1082-6.
    • (1998) Science , vol.280 , pp. 1082-1086
    • Ebinu, J.O.1    Bottoroff, D.A.2    Chan, E.Y.3    Stang, S.L.4    Dunn, R.J.5    Stone, J.C.6
  • 7
    • 0028113884 scopus 로고
    • R-Ras induces malignant, but not morphologic, transformation of NIH3T3 cells
    • Cox AD, Brtva TR, Lowe DG, Der CJ. R-Ras induces malignant, but not morphologic, transformation of NIH3T3 cells. Oncogene 1994;9:3281-8.
    • (1994) Oncogene , vol.9 , pp. 3281-3288
    • Cox, A.D.1    Brtva, T.R.2    Lowe, D.G.3    Der, C.J.4
  • 8
    • 0028136185 scopus 로고
    • Oncogenic activation of human R-Ras by point mutations, analogous to those of prototype H-Ras
    • Saez R, Chan AM, Miki T, Aaronson SA. Oncogenic activation of human R-Ras by point mutations, analogous to those of prototype H-Ras. Oncogene 1994;9:2977-82.
    • (1994) Oncogene , vol.9 , pp. 2977-2982
    • Saez, R.1    Chan, A.M.2    Miki, T.3    Aaronson, S.A.4
  • 10
    • 0032979447 scopus 로고    scopus 로고
    • The small GTP-binding protein R-Ras can influence integrin activation by antagonizing a Ras/Raf-initiated integrin suppression pathway
    • Sethi T, Ginsberg MH, Downward J, Hughes PE. The small GTP-binding protein R-Ras can influence integrin activation by antagonizing a Ras/Raf-initiated integrin suppression pathway. Mol Biol Cell 1999;10:1799-809.
    • (1999) Mol Biol Cell , vol.10 , pp. 1799-1809
    • Sethi, T.1    Ginsberg, M.H.2    Downward, J.3    Hughes, P.E.4
  • 11
    • 0034641865 scopus 로고    scopus 로고
    • The effector loop and prenylation site of R-Ras are involved in the regulation of integrin function
    • Oertli B, Han J, Marte BM, et al. The effector loop and prenylation site of R-Ras are involved in the regulation of integrin function. Oncogene 2000;19:4961-9.
    • (2000) Oncogene , vol.19 , pp. 4961-4969
    • Oertli, B.1    Han, J.2    Marte, B.M.3
  • 12
    • 0034681424 scopus 로고    scopus 로고
    • R-Ras contains a proline-rich site that binds to SH3 domains and is required for integrin activation by R-Ras
    • Wang B, Zou JX, Ek-Rylander B, Ruoslahti E. R-Ras contains a proline-rich site that binds to SH3 domains and is required for integrin activation by R-Ras. J Biol Chem 2000;275:5222-7.
    • (2000) J Biol Chem , vol.275 , pp. 5222-5227
    • Wang, B.1    Zou, J.X.2    Ek-Rylander, B.3    Ruoslahti, E.4
  • 13
    • 2442661711 scopus 로고    scopus 로고
    • Rho is involved in superoxide formation during phagocytosis of opsonized zymosans
    • Kim JS, Biebold BA, Kim JI, Kim J, Lee JY, Park JB. Rho is involved in superoxide formation during phagocytosis of opsonized zymosans. J Biol Chem 2004;279:21589-97.
    • (2004) J Biol Chem , vol.279 , pp. 21589-21597
    • Kim, J.S.1    Biebold, B.A.2    Kim, J.I.3    Kim, J.4    Lee, J.Y.5    Park, J.B.6
  • 15
    • 0029894080 scopus 로고    scopus 로고
    • Determination of functional domains in the C subunit of the CCAAT-binding factor (CBF) necessary for formation of a CBF-DNA complex: CBF-B interacts simultaneously with both the CBF-A and CBF-C subunits to form a heterotrimeric CBF molecule
    • Kim IS, Sinha S, Crombrugghe B, Maity SN. Determination of functional domains in the C subunit of the CCAAT-binding factor (CBF) necessary for formation of a CBF-DNA complex: CBF-B interacts simultaneously with both the CBF-A and CBF-C subunits to form a heterotrimeric CBF molecule. Mol Cell Biol 1996;6:4003-13.
    • (1996) Mol Cell Biol , vol.6 , pp. 4003-4013
    • Kim, I.S.1    Sinha, S.2    Crombrugghe, B.3    Maity, S.N.4
  • 16
    • 0037474267 scopus 로고    scopus 로고
    • Oncogenic Ras leads to Rho activation by activating the mitogen activated protein kinase pathway and decreasing Rho-GTPase activating protein activity
    • Chen JC, Zhuang S, Nguyen TH, Boss GR, Pilz RB. Oncogenic Ras leads to Rho activation by activating the mitogen activated protein kinase pathway and decreasing Rho-GTPase activating protein activity. J Biol Chem 2003;278:2807-18.
    • (2003) J Biol Chem , vol.278 , pp. 2807-2818
    • Chen, J.C.1    Zhuang, S.2    Nguyen, T.H.3    Boss, G.R.4    Pilz, R.B.5
  • 17
    • 0036443970 scopus 로고    scopus 로고
    • Isoprenylation is necessary for the full invasive potential of RhoA overexpression in human melanoma cells
    • Collisson EA, Carranza DC, Chen IY, Kolodney MS. Isoprenylation is necessary for the full invasive potential of RhoA overexpression in human melanoma cells. J Invest Dermatol 2002;110:1172-6.
    • (2002) J Invest Dermatol , vol.110 , pp. 1172-1176
    • Collisson, E.A.1    Carranza, D.C.2    Chen, I.Y.3    Kolodney, M.S.4
  • 18
    • 0032977036 scopus 로고    scopus 로고
    • Rho as a mediator of G protein-coupled receptor signaling
    • Seasholtz TM, Majumdar M, Brown JH. Rho as a mediator of G protein-coupled receptor signaling. Mol Pharmacol 1999;55:949-6.
    • (1999) Mol Pharmacol , vol.55 , pp. 949-956
    • Seasholtz, T.M.1    Majumdar, M.2    Brown, J.H.3
  • 19
    • 0029786313 scopus 로고    scopus 로고
    • Phosphorylation and activation of myosin by Rho-associated kinase (Rho-kinase)
    • Amano M, Ito M, Kimura K, et al. Phosphorylation and activation of myosin by Rho-associated kinase (Rho-kinase). J Biol Chem 1996;271:20246-9.
    • (1996) J Biol Chem , vol.271 , pp. 20246-20249
    • Amano, M.1    Ito, M.2    Kimura, K.3
  • 20
    • 0034739854 scopus 로고    scopus 로고
    • Activated R-Ras, Rac1. PI3kinases and PKC each restore cell spreading inhibited by isolated integrin β1 cytoplasmic domains
    • Berrier AL, Mastrangelo AM, Downward J, Ginsberg M, LaFlamme SE. Activated R-Ras, Rac1. PI3kinases and PKC each restore cell spreading inhibited by isolated integrin β1 cytoplasmic domains. J Cell Biol 2000;151:1549-60.
    • (2000) J Cell Biol , vol.151 , pp. 1549-1560
    • Berrier, A.L.1    Mastrangelo, A.M.2    Downward, J.3    Ginsberg, M.4    LaFlamme, S.E.5
  • 22
    • 0141613755 scopus 로고    scopus 로고
    • The C-terminal end of R-Ras contains a focal adhesion targeting signal
    • Furuhjelm J, Peranen J. The C-terminal end of R-Ras contains a focal adhesion targeting signal. J Cell Sci 2003;116:3729-38.
    • (2003) J Cell Sci , vol.116 , pp. 3729-3738
    • Furuhjelm, J.1    Peranen, J.2
  • 23
    • 0032772015 scopus 로고    scopus 로고
    • Differential roles of Akt, Rac, and Ral in R-Ras-mediated cellular transformation, adhesion, and survival
    • Osada M, Tolkacheva T, Li W, et al. Differential roles of Akt, Rac, and Ral in R-Ras-mediated cellular transformation, adhesion, and survival. Mol Cell Biol 1999;19:6333-44.
    • (1999) Mol Cell Biol , vol.19 , pp. 6333-6344
    • Osada, M.1    Tolkacheva, T.2    Li, W.3
  • 24
    • 0034715923 scopus 로고    scopus 로고
    • Focal adhesion; a nexus for intracellular signaling and cytoskeletal dynamics
    • Sastry SK, Burridge K. Focal adhesion; a nexus for intracellular signaling and cytoskeletal dynamics. Exp Cell Res 2000;261:25-36.
    • (2000) Exp Cell Res , vol.261 , pp. 25-36
    • Sastry, S.K.1    Burridge, K.2
  • 25
    • 0033594123 scopus 로고    scopus 로고
    • Rho GTPases control polarity, protrusion and adhesion during cell movement
    • Nobes CD, Hall A. Rho GTPases control polarity, protrusion and adhesion during cell movement. J Cell Biol 1999;144:1235-44.
    • (1999) J Cell Biol , vol.144 , pp. 1235-1244
    • Nobes, C.D.1    Hall, A.2
  • 26
    • 0345731237 scopus 로고    scopus 로고
    • Cell migration: Rho GTPases lead the way
    • Raftopoulou M, Hall A. Cell migration: Rho GTPases lead the way. Dev Biol 2004;265:23-32.
    • (2004) Dev Biol , vol.265 , pp. 23-32
    • Raftopoulou, M.1    Hall, A.2
  • 27
    • 0030968580 scopus 로고    scopus 로고
    • Rho GTPases and signaling networks
    • Van Aelst L, D'Souza-Schorey C. Rho GTPases and signaling networks. Genes Dev 1997;11:2295-322.
    • (1997) Genes Dev , vol.11 , pp. 2295-2322
    • Van Aelst, L.1    D'Souza-Schorey, C.2
  • 28
    • 0035152391 scopus 로고    scopus 로고
    • Integrin mediated adhesion regulates cell and membrane protrusion through the Rho family of GTPases
    • Cox EA, Sastry SK, Huttenlocher A. Integrin mediated adhesion regulates cell and membrane protrusion through the Rho family of GTPases. Mol Biol Cell 2001;12:265-77.
    • (2001) Mol Biol Cell , vol.12 , pp. 265-277
    • Cox, E.A.1    Sastry, S.K.2    Huttenlocher, A.3
  • 29
    • 0035158377 scopus 로고    scopus 로고
    • RhoA inactivation by p190RhoGAP regulated cell spreading and migration by promoting membranes protrusion and polarity
    • Aruthur WT, Burridge K. RhoA inactivation by p190RhoGAP regulated cell spreading and migration by promoting membranes protrusion and polarity. Mol Biol Cell 2001;12:2711-20.
    • (2001) Mol Biol Cell , vol.12 , pp. 2711-2720
    • Aruthur, W.T.1    Burridge, K.2
  • 30
    • 0032498528 scopus 로고    scopus 로고
    • Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association
    • Matsui T, Maeda M, Doi Y, et al. Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association. J Cell Biol 1998;140:647-57.
    • (1998) J Cell Biol , vol.140 , pp. 647-657
    • Matsui, T.1    Maeda, M.2    Doi, Y.3
  • 31
    • 0032550225 scopus 로고    scopus 로고
    • Association of the myosin-binding sub-unit of myosin phosphatase and moesin: Dual regulation of moesin phosphorylation by Rho-associated kinase and myosin phosphatase
    • Fukata Y, Kimura K, Oshiro N, Saya H, Matsuura Y, Kaibuchi K. Association of the myosin-binding sub-unit of myosin phosphatase and moesin: dual regulation of moesin phosphorylation by Rho-associated kinase and myosin phosphatase. J Cell Biol 1998;141:409-18.
    • (1998) J Cell Biol , vol.141 , pp. 409-418
    • Fukata, Y.1    Kimura, K.2    Oshiro, N.3    Saya, H.4    Matsuura, Y.5    Kaibuchi, K.6
  • 32
    • 0032489531 scopus 로고    scopus 로고
    • Regulation of the association of adducin with actin filaments by Rho-associated kinase (Rho-kinase) and myosin phosphatase
    • Kimura K, Fukata Y, Matsuoka Y, et al. Regulation of the association of adducin with actin filaments by Rho-associated kinase (Rho-kinase) and myosin phosphatase. J Biol Chem 1998;273:5542-8.
    • (1998) J Biol Chem , vol.273 , pp. 5542-5548
    • Kimura, K.1    Fukata, Y.2    Matsuoka, Y.3
  • 33
    • 0842288222 scopus 로고    scopus 로고
    • Distinct roles of MLCK and ROCK in the regulation of membrane protrusions and focal adhesion dynamics during cell migration of fibroblasts
    • Totsukawa G, Wu Y, Sasaki Y, et al. Distinct roles of MLCK and ROCK in the regulation of membrane protrusions and focal adhesion dynamics during cell migration of fibroblasts. J Cell Biol 2004;164:427-39.
    • (2004) J Cell Biol , vol.164 , pp. 427-439
    • Totsukawa, G.1    Wu, Y.2    Sasaki, Y.3
  • 34
    • 0034698841 scopus 로고    scopus 로고
    • Distinct roles of ROCK (Rho-kinase) and MLCK in spatial regulation of MLC phosphorylation for assembly of stress fibers and focal adhesions in 3T3 fibroblasts
    • Totsukawa G, Yamakita Y, Yamashiro S, Hartshorne DJ, Sasaki Y, Matsumura F. Distinct roles of ROCK (Rho-kinase) and MLCK in spatial regulation of MLC phosphorylation for assembly of stress fibers and focal adhesions in 3T3 fibroblasts. J Cell Biol 2000;150:797-806.
    • (2000) J Cell Biol , vol.150 , pp. 797-806
    • Totsukawa, G.1    Yamakita, Y.2    Yamashiro, S.3    Hartshorne, D.J.4    Sasaki, Y.5    Matsumura, F.6
  • 35
    • 0033620657 scopus 로고    scopus 로고
    • R-Ras signals through specific integrin α cytoplasmic domains to promote migration and invasion of breast epithelial cells
    • Keely PJ, Rusyn EV, Cox AD, Parise LV. R-Ras signals through specific integrin α cytoplasmic domains to promote migration and invasion of breast epithelial cells. J Cell Biol 1999;145:1077-88.
    • (1999) J Cell Biol , vol.145 , pp. 1077-1088
    • Keely, P.J.1    Rusyn, E.V.2    Cox, A.D.3    Parise, L.V.4
  • 36
    • 0034708221 scopus 로고    scopus 로고
    • Positive regulation of skeletal myogenesis by R-Ras
    • Suzuki J, Kaziro Y, Koide H. Positive regulation of skeletal myogenesis by R-Ras. Oncogene 2000;19:1138-45.
    • (2000) Oncogene , vol.19 , pp. 1138-1145
    • Suzuki, J.1    Kaziro, Y.2    Koide, H.3
  • 38
    • 0037469079 scopus 로고    scopus 로고
    • Ras superfamily monomeric G proteins in carcinoma cell motility
    • Oxford G, Theodorescu D. Ras superfamily monomeric G proteins in carcinoma cell motility. Cancer Lett 2003;189:117-28.
    • (2003) Cancer Lett , vol.189 , pp. 117-128
    • Oxford, G.1    Theodorescu, D.2
  • 39
    • 0029820264 scopus 로고    scopus 로고
    • Modulation of cell migration by integrin-mediated cytoskeletal linkages and ligand-binding affinity
    • Huttenlocher A, Ginsberg MH, Horwitz AF. Modulation of cell migration by integrin-mediated cytoskeletal linkages and ligand-binding affinity. J Cell Biol 1996;134:1551-62.
    • (1996) J Cell Biol , vol.134 , pp. 1551-1562
    • Huttenlocher, A.1    Ginsberg, M.H.2    Horwitz, A.F.3
  • 40
    • 0036327732 scopus 로고    scopus 로고
    • Suppression of integrin activation by activated Ras or Raf does not correlate with bulk activation of ERK MAP kinase
    • Hughes PE, Oertli B, Hansen M, Chou FL, Willumsen BM, Ginsberg MH. Suppression of integrin activation by activated Ras or Raf does not correlate with bulk activation of ERK MAP kinase. Mol Biol Cell 2002;13:2256-65.
    • (2002) Mol Biol Cell , vol.13 , pp. 2256-2265
    • Hughes, P.E.1    Oertli, B.2    Hansen, M.3    Chou, F.L.4    Willumsen, B.M.5    Ginsberg, M.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.