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Volumn 295, Issue 2, 2004, Pages 488-496

Thy-1 regulates fibroblast focal adhesions, cytoskeletal organization and migration through modulation of p190 RhoGAP and Rho GTPase activity

Author keywords

Adhesion; Fibroblast; Migration; p190 RhoGAP; Rho GTPase; Src kinase; Thy 1

Indexed keywords

GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; PROTEIN TYROSINE KINASE; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; THY 1 ANTIGEN;

EID: 1842861664     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2004.01.026     Document Type: Article
Times cited : (90)

References (46)
  • 1
    • 0024690462 scopus 로고
    • Characterization of two major populations of lung fibroblasts: Distinguishing morphology and discordant display of Thy 1 and class II MHC
    • Phipps R.P., Penney D.P., Keng P., Quill H., Paxhia A., Derdak S., Felch M.E. Characterization of two major populations of lung fibroblasts: distinguishing morphology and discordant display of Thy 1 and class II MHC. Am. J. Respir. Cell Mol. Biol. 1:1989;65-74.
    • (1989) Am. J. Respir. Cell Mol. Biol. , vol.1 , pp. 65-74
    • Phipps, R.P.1    Penney, D.P.2    Keng, P.3    Quill, H.4    Paxhia, A.5    Derdak, S.6    Felch, M.E.7
  • 4
    • 0029966632 scopus 로고    scopus 로고
    • Interleukin-4 and interferon-gamma discordantly regulate collagen biosynthesis by functionally distinct lung fibroblast subsets
    • Sempowski G.D., Derdak S., Phipps R.P. Interleukin-4 and interferon-gamma discordantly regulate collagen biosynthesis by functionally distinct lung fibroblast subsets. J. Cell. Physiol. 167:1996;290-296.
    • (1996) J. Cell. Physiol. , vol.167 , pp. 290-296
    • Sempowski, G.D.1    Derdak, S.2    Phipps, R.P.3
  • 5
    • 0034917543 scopus 로고    scopus 로고
    • Differential expression, surface binding, and response to connective tissue growth factor in lung fibroblast subpopulations
    • Hagood J.S., Lasky J.A., Nesbitt J.E., Segarini P. Differential expression, surface binding, and response to connective tissue growth factor in lung fibroblast subpopulations. Chest. 120:2001;S64-S66.
    • (2001) Chest , vol.120
    • Hagood, J.S.1    Lasky, J.A.2    Nesbitt, J.E.3    Segarini, P.4
  • 6
    • 0032801131 scopus 로고    scopus 로고
    • Differential expression of platelet-derived growth factor-alpha receptor by Thy-1(-) and Thy-1(+) lung fibroblasts
    • Hagood J.S., Miller P.J., Lasky J.A., Tousson A., Guo B., Fuller G.M., McIntosh J.C. Differential expression of platelet-derived growth factor-alpha receptor by Thy-1(-) and Thy-1(+) lung fibroblasts. Am. J. Physiol. 277:1999;L218-L224.
    • (1999) Am. J. Physiol. , vol.277
    • Hagood, J.S.1    Miller, P.J.2    Lasky, J.A.3    Tousson, A.4    Guo, B.5    Fuller, G.M.6    McIntosh, J.C.7
  • 7
    • 0026553053 scopus 로고
    • Morphologic and functional characteristics of subpopulations of murine lung fibroblasts grown in vitro
    • Penney D.P., Keng P.C., Derdak S., Phipps R.P. Morphologic and functional characteristics of subpopulations of murine lung fibroblasts grown in vitro. Anat. Rec. 232:1992;432-443.
    • (1992) Anat. Rec. , vol.232 , pp. 432-443
    • Penney, D.P.1    Keng, P.C.2    Derdak, S.3    Phipps, R.P.4
  • 9
    • 0018139183 scopus 로고
    • Differential expression of Rous Sarcoma virus-specific transformation parameters in enucleated cells
    • Beug H., Claviez M., Jockusch B.M., Graf T. Differential expression of Rous Sarcoma virus-specific transformation parameters in enucleated cells. Cell. 14:1978;843-856.
    • (1978) Cell , vol.14 , pp. 843-856
    • Beug, H.1    Claviez, M.2    Jockusch, B.M.3    Graf, T.4
  • 10
    • 0030482560 scopus 로고    scopus 로고
    • Translocation of Src kinase to the cell periphery is mediated by the actin cytoskeleton under the control of the Rho family of small G proteins
    • Fincham V.J., Unlu M., Brunton V.G., Pitts J.D., Wyke J.A., Frame M.C. Translocation of Src kinase to the cell periphery is mediated by the actin cytoskeleton under the control of the Rho family of small G proteins. J. Cell Biol. 135:1996;1551-1564.
    • (1996) J. Cell Biol. , vol.135 , pp. 1551-1564
    • Fincham, V.J.1    Unlu, M.2    Brunton, V.G.3    Pitts, J.D.4    Wyke, J.A.5    Frame, M.C.6
  • 11
    • 0028988989 scopus 로고
    • V-Src-induced degradation of focal adhesion kinase during morphological transformation of chicken embryo fibroblasts
    • Fincham V.J., Wyke J.A., Frame M.C. v-Src-induced degradation of focal adhesion kinase during morphological transformation of chicken embryo fibroblasts. Oncogene. 10:1995;2247-2252.
    • (1995) Oncogene , vol.10 , pp. 2247-2252
    • Fincham, V.J.1    Wyke, J.A.2    Frame, M.C.3
  • 12
    • 0035158377 scopus 로고    scopus 로고
    • RhoA inactivation by p190RhoGAP regulates cell spreading and migration by promoting membrane protrusion and polarity
    • Arthur W.T., Burridge K. RhoA inactivation by p190RhoGAP regulates cell spreading and migration by promoting membrane protrusion and polarity. Mol. Biol. Cell. 12:2001;2711-2720.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2711-2720
    • Arthur, W.T.1    Burridge, K.2
  • 13
    • 0035071323 scopus 로고    scopus 로고
    • P190 RhoGAP is the principal Src substrate in brain and regulates axon outgrowth, guidance and fasciculation
    • Brouns M.R., Matheson S.F., Settleman J. p190 RhoGAP is the principal Src substrate in brain and regulates axon outgrowth, guidance and fasciculation. Nat. Cell Biol. 3:2001;361-367.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 361-367
    • Brouns, M.R.1    Matheson, S.F.2    Settleman, J.3
  • 14
    • 0022039722 scopus 로고
    • Coupling of cytoskeleton functions for fibroblast locomotion
    • Couchman J.R., Lenn M., Rees D.A. Coupling of cytoskeleton functions for fibroblast locomotion. Eur. J. Cell Biol. 36:1985;182-194.
    • (1985) Eur. J. Cell Biol. , vol.36 , pp. 182-194
    • Couchman, J.R.1    Lenn, M.2    Rees, D.A.3
  • 15
    • 0030045346 scopus 로고    scopus 로고
    • Cell migration: A physically integrated molecular process
    • Lauffenburger D.A., Horwitz A.F. Cell migration: a physically integrated molecular process. Cell. 84:1996;359-369.
    • (1996) Cell , vol.84 , pp. 359-369
    • Lauffenburger, D.A.1    Horwitz, A.F.2
  • 18
    • 0033178168 scopus 로고    scopus 로고
    • Thy-1/CD3 coengagement promotes TCR signaling and enhances particularly tyrosine phosphorylation of the raft molecule LAT
    • Leyton L., Quest A.F., Bron C. Thy-1/CD3 coengagement promotes TCR signaling and enhances particularly tyrosine phosphorylation of the raft molecule LAT. Mol. Immunol. 36:1999;755-768.
    • (1999) Mol. Immunol. , vol.36 , pp. 755-768
    • Leyton, L.1    Quest, A.F.2    Bron, C.3
  • 19
    • 0028360654 scopus 로고
    • The mode of anchorage to the cell surface determines both the function and the membrane location of Thy-1 glycoprotein
    • Tiveron M.C., Nosten-Bertrand M., Jani H., Garnett D., Hirst E.M., Grosveld F., Morris R.J. The mode of anchorage to the cell surface determines both the function and the membrane location of Thy-1 glycoprotein. J. Cell Sci. 107:1994;1783-1796.
    • (1994) J. Cell Sci. , vol.107 , pp. 1783-1796
    • Tiveron, M.C.1    Nosten-Bertrand, M.2    Jani, H.3    Garnett, D.4    Hirst, E.M.5    Grosveld, F.6    Morris, R.J.7
  • 20
    • 1842414894 scopus 로고    scopus 로고
    • Src family-selective tyrosine kinase inhibitor, PP1, inhibits both Fc epsilonRI- and Thy-1-mediated activation of rat basophilic leukemia cells
    • Amoui M., Draber P., Draberova L. Src family-selective tyrosine kinase inhibitor, PP1, inhibits both Fc epsilonRI- and Thy-1-mediated activation of rat basophilic leukemia cells. Eur. J. Immunol. 27:1997;1881-1886.
    • (1997) Eur. J. Immunol. , vol.27 , pp. 1881-1886
    • Amoui, M.1    Draber, P.2    Draberova, L.3
  • 21
    • 0029007251 scopus 로고
    • Differential requirement for protein tyrosine kinase Fyn in the functional activation of antigen-specific T lymphocyte clones through the TCR or Thy-1
    • Lancki D.W., Qian D., Fields P., Gajewski T., Fitch F.W. Differential requirement for protein tyrosine kinase Fyn in the functional activation of antigen-specific T lymphocyte clones through the TCR or Thy-1. J. Immunol. 154:1995;4363-4370.
    • (1995) J. Immunol. , vol.154 , pp. 4363-4370
    • Lancki, D.W.1    Qian, D.2    Fields, P.3    Gajewski, T.4    Fitch, F.W.5
  • 22
    • 0035132591 scopus 로고    scopus 로고
    • Differential sensitivity to acute cholesterol lowering of activation mediated via the high-affinity IgE receptor and Thy-1 glycoprotein
    • Surviladze Z., Draberova L., Kovarova M., Boubelik M., Draber P. Differential sensitivity to acute cholesterol lowering of activation mediated via the high-affinity IgE receptor and Thy-1 glycoprotein. Eur. J. Immunol. 31:2001;1-10.
    • (2001) Eur. J. Immunol. , vol.31 , pp. 1-10
    • Surviladze, Z.1    Draberova, L.2    Kovarova, M.3    Boubelik, M.4    Draber, P.5
  • 24
    • 0033081753 scopus 로고    scopus 로고
    • Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton
    • Ren X.D., Kiosses W.B., Schwartz M.A. Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton. EMBO J. 18:1999;578-585.
    • (1999) EMBO J. , vol.18 , pp. 578-585
    • Ren, X.D.1    Kiosses, W.B.2    Schwartz, M.A.3
  • 26
    • 0026078630 scopus 로고
    • Thy-1 supports adhesion of mouse thymocytes to thymic epithelial cells through a Ca2(+)-independent mechanism
    • He H.T., Naquet P., Caillol D., Pierres M. Thy-1 supports adhesion of mouse thymocytes to thymic epithelial cells through a Ca2(+)-independent mechanism. J. Exp. Med. 173:1991;515-518.
    • (1991) J. Exp. Med. , vol.173 , pp. 515-518
    • He, H.T.1    Naquet, P.2    Caillol, D.3    Pierres, M.4
  • 27
    • 0025873983 scopus 로고
    • Effect of ras-activation on the expression of glycosyl- phosphatidylinositol-anchored proteins on the plasma membrane
    • Bamezai A., Rock K.L. Effect of ras-activation on the expression of glycosyl-phosphatidylinositol-anchored proteins on the plasma membrane. Oncogene. 6:1991;1445-1451.
    • (1991) Oncogene , vol.6 , pp. 1445-1451
    • Bamezai, A.1    Rock, K.L.2
  • 28
    • 0026085477 scopus 로고
    • Thy-1 as a negative growth regulator in ras-transformed mouse fibroblasts
    • Sugimoto Y., Ikawa Y., Nakauchi H. Thy-1 as a negative growth regulator in ras-transformed mouse fibroblasts. Cancer Res. 51:1991;99-104.
    • (1991) Cancer Res. , vol.51 , pp. 99-104
    • Sugimoto, Y.1    Ikawa, Y.2    Nakauchi, H.3
  • 30
    • 0035171631 scopus 로고    scopus 로고
    • Glycosylphosphatidyl inositol-anchored proteins and fyn kinase assemble in noncaveolar plasma membrane microdomains defined by reggie-1 and-2
    • Stuermer C.A., Lang D.M., Kirsch F., Wiechers M., Deininger S.O., Plattner H. Glycosylphosphatidyl inositol-anchored proteins and fyn kinase assemble in noncaveolar plasma membrane microdomains defined by reggie-1 and-2. Mol. Biol. Cell. 12:2001;3031-3045.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3031-3045
    • Stuermer, C.A.1    Lang, D.M.2    Kirsch, F.3    Wiechers, M.4    Deininger, S.O.5    Plattner, H.6
  • 31
    • 0021341026 scopus 로고
    • T cell-activating properties of an anti-Thy-1 monoclonal antibody. Possible analogy to OKT3/Leu-4
    • Gunter K.C., Malek T.R., Shevach E.M. T cell-activating properties of an anti-Thy-1 monoclonal antibody. Possible analogy to OKT3/Leu-4. J. Exp. Med. 159:1984;716-730.
    • (1984) J. Exp. Med. , vol.159 , pp. 716-730
    • Gunter, K.C.1    Malek, T.R.2    Shevach, E.M.3
  • 32
    • 0026352248 scopus 로고
    • GPI-anchored cell-surface molecules complexed to protein tyrosine kinases
    • Stefanova I., Horejsi V., Ansotegui I.J., Knapp W., Stockinger H. GPI-anchored cell-surface molecules complexed to protein tyrosine kinases. Science. 254:1991;1016-1019.
    • (1991) Science , vol.254 , pp. 1016-1019
    • Stefanova, I.1    Horejsi, V.2    Ansotegui, I.J.3    Knapp, W.4    Stockinger, H.5
  • 33
    • 0026457327 scopus 로고
    • Signal transduction through decay-accelerating factor. Interaction of glycosyl-phosphatidylinositol anchor and protein tyrosine kinases p56lck and p59fyn 1
    • Shenoy-Scaria A.M., Kwong J., Fujita T., Olszowy M.W., Shaw A.S., Lublin D.M. Signal transduction through decay-accelerating factor. Interaction of glycosyl-phosphatidylinositol anchor and protein tyrosine kinases p56lck and p59fyn 1. J. Immunol. 149:1992;3535-3541.
    • (1992) J. Immunol. , vol.149 , pp. 3535-3541
    • Shenoy-Scaria, A.M.1    Kwong, J.2    Fujita, T.3    Olszowy, M.W.4    Shaw, A.S.5    Lublin, D.M.6
  • 34
    • 0025823714 scopus 로고
    • Association of the CD59 and CD55 cell surface glycoproteins with other membrane molecules
    • Stefanova I., Horejsi V. Association of the CD59 and CD55 cell surface glycoproteins with other membrane molecules. J. Immunol. 147:1991;1587-1592.
    • (1991) J. Immunol. , vol.147 , pp. 1587-1592
    • Stefanova, I.1    Horejsi, V.2
  • 35
    • 0035150791 scopus 로고    scopus 로고
    • Thy-1 associated Pp85-90 is a potential docking site for Sh2 domain-containing signal transduction molecules
    • Durrheim G.A., Garnett D., Dennehy K.M., Beyers A.D. Thy-1 associated Pp85-90 is a potential docking site for Sh2 domain-containing signal transduction molecules. Cell Biol. Int. 25:2001;33-42.
    • (2001) Cell Biol. Int. , vol.25 , pp. 33-42
    • Durrheim, G.A.1    Garnett, D.2    Dennehy, K.M.3    Beyers, A.D.4
  • 36
    • 0036543312 scopus 로고    scopus 로고
    • Rho proteins, mental retardation and the cellular basis of cognition
    • Ramakers G.J. Rho proteins, mental retardation and the cellular basis of cognition. Trends Neurosci. 25:2002;191-199.
    • (2002) Trends Neurosci. , vol.25 , pp. 191-199
    • Ramakers, G.J.1
  • 38
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley A.J., Hall A. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell. 70:1992;389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 39
    • 0032959561 scopus 로고    scopus 로고
    • Regulation of p190 Rho-GAP by v-Src is linked to cytoskeletal disruption during transformation
    • Fincham V.J., Chudleigh A., Frame M.C. Regulation of p190 Rho-GAP by v-Src is linked to cytoskeletal disruption during transformation. J. Cell Sci. 112(Pt. 6):1999;947-956.
    • (1999) J. Cell Sci. , vol.112 , Issue.PT. 6 , pp. 947-956
    • Fincham, V.J.1    Chudleigh, A.2    Frame, M.C.3
  • 40
    • 0035018025 scopus 로고    scopus 로고
    • Phosphorylation of p190 on Tyr1105 by c-Src is necessary but not sufficient for EGF-induced actin disassembly in C3H10T1/2 fibroblasts
    • Haskell M.D., Nickles A.L., Agati J.M., Su L., Dukes B.D., Parsons S.J. Phosphorylation of p190 on Tyr1105 by c-Src is necessary but not sufficient for EGF-induced actin disassembly in C3H10T1/2 fibroblasts. J. Cell Sci. 114:2001;1699-1708.
    • (2001) J. Cell Sci. , vol.114 , pp. 1699-1708
    • Haskell, M.D.1    Nickles, A.L.2    Agati, J.M.3    Su, L.4    Dukes, B.D.5    Parsons, S.J.6
  • 41
    • 0029029889 scopus 로고
    • Two SH2 domains of p120 Ras GTPase-activating protein bind synergistically to tyrosine phosphorylated p190 Rho GTPase-activating protein
    • Bryant S.S., Briggs S., Smithgall T.E., Martin G.A., McCormick F., Chang J.H., Parsons S.J., Jove R. Two SH2 domains of p120 Ras GTPase-activating protein bind synergistically to tyrosine phosphorylated p190 Rho GTPase-activating protein. J. Biol. Chem. 270:1995;17947-17952.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17947-17952
    • Bryant, S.S.1    Briggs, S.2    Smithgall, T.E.3    Martin, G.A.4    McCormick, F.5    Chang, J.H.6    Parsons, S.J.7    Jove, R.8
  • 42
    • 0031030898 scopus 로고    scopus 로고
    • Tandem SH2 binding sites mediate the RasGAP-RhoGAP interaction: A conformational mechanism for SH3 domain regulation
    • Hu K.Q., Settleman J. Tandem SH2 binding sites mediate the RasGAP-RhoGAP interaction: a conformational mechanism for SH3 domain regulation. EMBO J. 16:1997;473-483.
    • (1997) EMBO J. , vol.16 , pp. 473-483
    • Hu, K.Q.1    Settleman, J.2
  • 44
    • 0034659526 scopus 로고    scopus 로고
    • Integrin engagement suppresses RhoA activity via a c-Src-dependent mechanism
    • Arthur W.T., Petch L.A., Burridge K. Integrin engagement suppresses RhoA activity via a c-Src-dependent mechanism. Curr. Biol. 10:2000;719-722.
    • (2000) Curr. Biol. , vol.10 , pp. 719-722
    • Arthur, W.T.1    Petch, L.A.2    Burridge, K.3
  • 45
    • 0032374079 scopus 로고    scopus 로고
    • Signaling of de-adhesion in cellular regulation and motility
    • Greenwood J.A., Murphy-Ullrich J.E. Signaling of de-adhesion in cellular regulation and motility. Microsc. Res. Tech. 43:1998;420-432.
    • (1998) Microsc. Res. Tech. , vol.43 , pp. 420-432
    • Greenwood, J.A.1    Murphy-Ullrich, J.E.2
  • 46
    • 0034858207 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of p190 RhoGAP by Fyn regulates oligodendrocyte differentiation
    • Wolf R.M., Wilkes J.J., Chao M.V., Resh M.D. Tyrosine phosphorylation of p190 RhoGAP by Fyn regulates oligodendrocyte differentiation. J. Neurobiol. 49:2001;62-78.
    • (2001) J. Neurobiol. , vol.49 , pp. 62-78
    • Wolf, R.M.1    Wilkes, J.J.2    Chao, M.V.3    Resh, M.D.4


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