메뉴 건너뛰기




Volumn 2, Issue 9, 2000, Pages 637-644

Inhibition of RhoA by p120 catenin

Author keywords

[No Author keywords available]

Indexed keywords

CATENIN; GUANOSINE TRIPHOSPHATASE; PROTEIN P120; RHO FACTOR;

EID: 0001468710     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/35023588     Document Type: Article
Times cited : (396)

References (39)
  • 1
    • 0029160437 scopus 로고
    • Morphogenetic roles of classic cadherins
    • Takeichi, M. Morphogenetic roles of classic cadherins. Curr. Opin. Cell Biol. 7, 619-627 (1995).
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 619-627
    • Takeichi, M.1
  • 2
    • 0031894062 scopus 로고    scopus 로고
    • The morphogenetic role of cadherin cell adhesion molecules in human cancer: A thematic review
    • Yap, A. S. The morphogenetic role of cadherin cell adhesion molecules in human cancer: a thematic review. Cancer Invest. 16, 252-261 (1998).
    • (1998) Cancer Invest. , vol.16 , pp. 252-261
    • Yap, A.S.1
  • 3
    • 0025765115 scopus 로고
    • E-cadherin-mediated cell-cell adhesion prevents invasiveness of human carcinoma cells
    • Frixen, U. H. et al. E-cadherin-mediated cell-cell adhesion prevents invasiveness of human carcinoma cells. J. Cell Biol. 113, 173-185 (1991).
    • (1991) J. Cell Biol. , vol.113 , pp. 173-185
    • Frixen, U.H.1
  • 4
    • 0032510494 scopus 로고    scopus 로고
    • A causal role for E-cadherin in the transition from adenoma to carcinoma
    • Perl, A. K., Wilgenbus, P., Dahl, U., Semb, H. & Christofori, G. A causal role for E-cadherin in the transition from adenoma to carcinoma. Nature 392, 190-193 (1998).
    • (1998) Nature , vol.392 , pp. 190-193
    • Perl, A.K.1    Wilgenbus, P.2    Dahl, U.3    Semb, H.4    Christofori, G.5
  • 5
    • 0025818032 scopus 로고
    • Genetic manipulation of E-cadherin expression by epithelial tumor cells reveals an invasion suppressor role
    • Vleminckx, K., Vakaet, L., Jr., Mareel, M., Fiers, W. & van Roy, F. Genetic manipulation of E-cadherin expression by epithelial tumor cells reveals an invasion suppressor role. Cell 66, 107-119 (1991).
    • (1991) Cell , vol.66 , pp. 107-119
    • Vleminckx, K.1    Vakaet L., Jr.2    Mareel, M.3    Fiers, W.4    Van Roy, F.5
  • 6
    • 0034010129 scopus 로고    scopus 로고
    • The p120 catenin family: Complex roles in adhesion, signalling and cancer
    • Anastasiadis, P. Z. & Reynolds, A. B. The p120 catenin family: complex roles in adhesion, signalling and cancer. J. Cell Sci. 113, 1319-1334 (2000).
    • (2000) J. Cell Sci. , vol.113 , pp. 1319-1334
    • Anastasiadis, P.Z.1    Reynolds, A.B.2
  • 7
    • 0028961293 scopus 로고
    • Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibres, lamellipodia, and filopodia
    • Nobes, C. C. & Hall, A. Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibres, lamellipodia, and filopodia. Cell 81, 53-62 (1995).
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.C.1    Hall, A.2
  • 8
    • 0030968177 scopus 로고    scopus 로고
    • The small GTPases Rho and Rac are required for the establishment of cadherin-dependent cell-cell contacts
    • Braga, V. M., Machesky, L. M., Hall, A. & Hotchin, N. A. The small GTPases Rho and Rac are required for the establishment of cadherin-dependent cell-cell contacts. J. Cell Biol. 137, 1421-1431 (1997).
    • (1997) J. Cell Biol. , vol.137 , pp. 1421-1431
    • Braga, V.M.1    Machesky, L.M.2    Hall, A.3    Hotchin, N.A.4
  • 9
    • 0030718609 scopus 로고    scopus 로고
    • Regulation of cell-cell adhesion by rac and rho small G proteins in MDCK cells
    • Takaishi, K., Sasaki, T., Kotani, H., Nishioka, H. & Takai, Y. Regulation of cell-cell adhesion by rac and rho small G proteins in MDCK cells. J. Cell Biol. 139, 1047-1059 (1997).
    • (1997) J. Cell Biol. , vol.139 , pp. 1047-1059
    • Takaishi, K.1    Sasaki, T.2    Kotani, H.3    Nishioka, H.4    Takai, Y.5
  • 10
    • 0032514214 scopus 로고    scopus 로고
    • Effects of regulated expression of mutant RhoA and Rac1 small GTPases on the development of epithelial (MDCK) cell polarity
    • Jou, T.S. & Nelson, W.J. Effects of regulated expression of mutant RhoA and Rac1 small GTPases on the development of epithelial (MDCK) cell polarity. J. Cell Biol. 142, 85-100 (1998).
    • (1998) J. Cell Biol. , vol.142 , pp. 85-100
    • Jou, T.S.1    Nelson, W.J.2
  • 11
    • 0032859045 scopus 로고    scopus 로고
    • Regulation of cadherin-mediated cell-cell adhesion by the Rho family GTPases
    • Kaibuchi, K., Kuroda, S., Fukata, M. & Nakagawa, M. Regulation of cadherin-mediated cell-cell adhesion by the Rho family GTPases. Curr. Opin. Cell Biol. 11, 591-596 (1999).
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 591-596
    • Kaibuchi, K.1    Kuroda, S.2    Fukata, M.3    Nakagawa, M.4
  • 12
    • 0029665589 scopus 로고    scopus 로고
    • cas binds classical cadherins and induces an unusual morphological phenotype in NIH3T3 fibroblasts
    • cas binds classical cadherins and induces an unusual morphological phenotype in NIH3T3 fibroblasts. Exp. Cell Res. 225, 328-337 (1996).
    • (1996) Exp. Cell Res. , vol.225 , pp. 328-337
    • Reynolds, A.B.1    Daniel, J.M.2    Mo, Y.Y.3    Wu, J.4    Zhang, Z.5
  • 13
    • 0033581010 scopus 로고    scopus 로고
    • Morphological changes and detachment of adherent cells induced by p122, a GTPase-activating protein for Rho
    • Sekimata, M., Kabuyama, Y., Emori, Y. & Homma, Y. Morphological changes and detachment of adherent cells induced by p122, a GTPase-activating protein for Rho. J. Biol. Chem. 274, 17757-17762 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 17757-17762
    • Sekimata, M.1    Kabuyama, Y.2    Emori, Y.3    Homma, Y.4
  • 14
    • 0033018626 scopus 로고    scopus 로고
    • Activation of RhoA by lysophosphatidic acid and Galpha12/13 subunits in neuronal cells: Induction of neurite retraction
    • Kranenburg, O. et al. Activation of RhoA by lysophosphatidic acid and Galpha12/13 subunits in neuronal cells: induction of neurite retraction. Mol. Biol. Cell 10, 1851-1857 (1999).
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1851-1857
    • Kranenburg, O.1
  • 15
    • 0029995797 scopus 로고    scopus 로고
    • Rho-stimulated contractility drives the formation of stress fibres and focal adhesions
    • Chrzanowska-Wodnicka, M. & Burridge, K. Rho-stimulated contractility drives the formation of stress fibres and focal adhesions. J. Cell Biol. 133, 1403-1415 (1996).
    • (1996) J. Cell Biol. , vol.133 , pp. 1403-1415
    • Chrzanowska-Wodnicka, M.1    Burridge, K.2
  • 16
    • 0032429270 scopus 로고    scopus 로고
    • Signalling mechanisms and molecular characteristics of G protein-coupled receptors for lysophosphatidic acid and sphingosine 1-phosphate
    • An, S., Goetzl, E. J. & Lee, H. Signalling mechanisms and molecular characteristics of G protein-coupled receptors for lysophosphatidic acid and sphingosine 1-phosphate. J. Cell Biochem. Suppl. 31, 147-157 (1998).
    • (1998) J. Cell Biochem. Suppl. , vol.31 , pp. 147-157
    • An, S.1    Goetzl, E.J.2    Lee, H.3
  • 17
    • 0032575667 scopus 로고    scopus 로고
    • cAMP-induced morphological changes are counteracted by the activated RhoA small GTPase and the Rho kinase ROKalpha
    • Dong, J. M., Leung, T., Manser, E. & Lim, L. cAMP-induced morphological changes are counteracted by the activated RhoA small GTPase and the Rho kinase ROKalpha. J. Biol. Chem. 273, 22554-22562 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 22554-22562
    • Dong, J.M.1    Leung, T.2    Manser, E.3    Lim, L.4
  • 18
    • 0032534510 scopus 로고    scopus 로고
    • Regulation of astrocyte morphology by RhoA and lysophosphatidic acid
    • Ramakers, G. J. A. & Moolenaar, W. H. Regulation of astrocyte morphology by RhoA and lysophosphatidic acid. Exp. Cell Res. 245, 252-262 (1998).
    • (1998) Exp. Cell Res. , vol.245 , pp. 252-262
    • Ramakers, G.J.A.1    Moolenaar, W.H.2
  • 19
    • 0029952315 scopus 로고    scopus 로고
    • The multidomain protein Trio binds the LAR transmembrane tyrosine phosphatase, contains a protein kinase domain, and has separate rac-specific and rho-specific guanine nucleotide exchange factor domains
    • Debant, A. et al. The multidomain protein Trio binds the LAR transmembrane tyrosine phosphatase, contains a protein kinase domain, and has separate rac-specific and rho-specific guanine nucleotide exchange factor domains. Proc. Natl Acad. Sci. USA 93, 5466-5471 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 5466-5471
    • Debant, A.1
  • 20
    • 0032576997 scopus 로고    scopus 로고
    • The Rho small G protein family-Rho GDI system as a temporal and spatial determinant for cytoskeletal control
    • Sasaki, T. & Takai, Y. The Rho small G protein family-Rho GDI system as a temporal and spatial determinant for cytoskeletal control. Biochem. Biophys. Res. Commun. 245, 641-645 (1998).
    • (1998) Biochem. Biophys. Res. Commun. , vol.245 , pp. 641-645
    • Sasaki, T.1    Takai, Y.2
  • 21
    • 0033058184 scopus 로고    scopus 로고
    • Rho guanine dissociation inhibitors: Pivotal molecules in cellular signalling
    • Olofsson, B. Rho guanine dissociation inhibitors: pivotal molecules in cellular signalling. Cell Signal. 11, 545-554 (1999).
    • (1999) Cell Signal , vol.11 , pp. 545-554
    • Olofsson, B.1
  • 23
    • 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, 578-585 (1999).
    • (1999) EMBO J. , vol.18 , pp. 578-585
    • Ren, X.D.1    Kiosses, W.B.2    Schwartz, M.A.3
  • 24
    • 0034627769 scopus 로고    scopus 로고
    • Selective uncoupling of p120(ctn) from E-cadherin disrupts strong adhesion
    • Thoreson, M. A. et al. Selective uncoupling of p120(ctn) from E-cadherin disrupts strong adhesion. J. Cell Biol. 148, 189-202 (2000).
    • (2000) J. Cell Biol. , vol.148 , pp. 189-202
    • Thoreson, M.A.1
  • 25
    • 0029795488 scopus 로고    scopus 로고
    • Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: Possible involvement of phosphatidylinositol turnover and Rho-dependent signalling pathway
    • Hirao, M. et al. Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signalling pathway. J. Cell Biol. 135, 37-51 (1996).
    • (1996) J. Cell Biol. , vol.135 , pp. 37-51
    • Hirao, M.1
  • 26
    • 0030961752 scopus 로고    scopus 로고
    • Rho regulates association of both the ERM family and vinculin with the plasma membrane in MDCK cells
    • Kotani, H., Takaishi, K., Sasaki, T. & Takai, Y. Rho regulates association of both the ERM family and vinculin with the plasma membrane in MDCK cells. Oncogene 14, 1705-1713 (1997).
    • (1997) Oncogene , vol.14 , pp. 1705-1713
    • Kotani, H.1    Takaishi, K.2    Sasaki, T.3    Takai, Y.4
  • 27
    • 0032104205 scopus 로고    scopus 로고
    • Molecular cloning of the human p120ctn catenin gene (CTNND1): Expression of multiple alternatively spliced isoforms
    • Keirsebilck, A. et al. Molecular cloning of the human p120ctn catenin gene (CTNND1): expression of multiple alternatively spliced isoforms. Genomics 50, 129-146 (1998).
    • (1998) Genomics , vol.50 , pp. 129-146
    • Keirsebilck, A.1
  • 28
    • 0029116143 scopus 로고
    • Tyrosine phosphorylation regulates the adhesions of ras-transformed breast epithelia
    • Kinch, M. S., Clark, G. J., Der, C. J. & Burridge, K. Tyrosine phosphorylation regulates the adhesions of ras-transformed breast epithelia. J. Cell Biol. 130, 461-471 (1995).
    • (1995) J. Cell Biol. , vol.130 , pp. 461-471
    • Kinch, M.S.1    Clark, G.J.2    Der, C.J.3    Burridge, K.4
  • 29
    • 0032526941 scopus 로고    scopus 로고
    • Tyrosine phosphorylation and src family kinases control keratinocyte cell-cell adhesion
    • Calautti, E. et al. Tyrosine phosphorylation and src family kinases control keratinocyte cell-cell adhesion. J. Cell Biol. 141, 1449-1465 (1998).
    • (1998) J. Cell Biol. , vol.141 , pp. 1449-1465
    • Calautti, E.1
  • 30
    • 0032555935 scopus 로고    scopus 로고
    • The membrane-proximal region of the E-cadherin cytoplasmic domain prevents dimerization and negatively regulates adhesion activity
    • Ozawa, M. & Kemler, R. The membrane-proximal region of the E-cadherin cytoplasmic domain prevents dimerization and negatively regulates adhesion activity. J. Cell Biol. 142, 1605-1613 (1998).
    • (1998) J. Cell Biol. , vol.142 , pp. 1605-1613
    • Ozawa, M.1    Kemler, R.2
  • 31
    • 0033519239 scopus 로고    scopus 로고
    • p120(ctn) acts as an inhibitory regulator of cadherin function in colon carcinoma cells
    • Aono, S., Nakagawa, S., Reynolds, A. B. & Takeichi, M. p120(ctn) acts as an inhibitory regulator of cadherin function in colon carcinoma cells. J. Cell Biol. 145, 551-562 (1999).
    • (1999) J. Cell Biol. , vol.145 , pp. 551-562
    • Aono, S.1    Nakagawa, S.2    Reynolds, A.B.3    Takeichi, M.4
  • 32
    • 0028247080 scopus 로고
    • Perturbation of cell adhesion and microvilli formation by antisense oligonucleotides to ERM family members
    • Takeuchi, K. et al. Perturbation of cell adhesion and microvilli formation by antisense oligonucleotides to ERM family members. J. Cell Biol. 125, 1371-1384 (1994).
    • (1994) J. Cell Biol. , vol.125 , pp. 1371-1384
    • Takeuchi, K.1
  • 33
    • 0030872949 scopus 로고    scopus 로고
    • Rho- and rac-dependent assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: An essential role for ezrin/radixin/moesin proteins
    • Mackay, D. J., Esch, F., Furthmayr, H. & Hall, A. Rho- and rac-dependent assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: an essential role for ezrin/radixin/moesin proteins. J. Cell Biol. 138, 927-938 (1997).
    • (1997) J. Cell Biol. , vol.138 , pp. 927-938
    • Mackay, D.J.1    Esch, F.2    Furthmayr, H.3    Hall, A.4
  • 34
    • 0030760544 scopus 로고    scopus 로고
    • Cell confluence regulates tyrosine phosphorylation of adherens junction components in endothelial cells
    • Lampugnani, M. G. et al. Cell confluence regulates tyrosine phosphorylation of adherens junction components in endothelial cells. J. Cell Sci. 110, 2065-2077 (1997).
    • (1997) J. Cell Sci. , vol.110 , pp. 2065-2077
    • Lampugnani, M.G.1
  • 35
    • 0028019276 scopus 로고
    • Identification of a new catenin: The tyrosine kinase substrate p120cas associates with E-cadherin complexes
    • Reynolds, A. B. et al. Identification of a new catenin: the tyrosine kinase substrate p120cas associates with E-cadherin complexes. Mol. Cell. Biol. 14, 8333-8342 (1994).
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 8333-8342
    • Reynolds, A.B.1
  • 36
    • 0031832299 scopus 로고    scopus 로고
    • Production and characterization of monoclonal antibodies to the catenin p120ctn
    • Wu, J., Mariner, D. J., Thoreson, M. A. & Reynolds, A. B. Production and characterization of monoclonal antibodies to the catenin p120ctn. Hybridoma 17, 175-183 (1998).
    • (1998) Hybridoma , vol.17 , pp. 175-183
    • Wu, J.1    Mariner, D.J.2    Thoreson, M.A.3    Reynolds, A.B.4
  • 37
    • 0033613927 scopus 로고    scopus 로고
    • A built-in arginine finger triggers the self-stimulatory GTPase-activating activity of rho family GTPases
    • Zhang, B., Zhang, Y., Collins, C.C., Johnson, D. I. & Zheng, Y. A built-in arginine finger triggers the self-stimulatory GTPase-activating activity of rho family GTPases. J. Biol. Chem. 274, 2609-2612 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 2609-2612
    • Zhang, B.1    Zhang, Y.2    Collins, C.C.3    Johnson, D.I.4    Zheng, Y.5
  • 38
    • 0031468438 scopus 로고    scopus 로고
    • Structural determinants required for the interaction between Rho GTPase and the GTPase-activating domain of p190
    • Li, R., Zhang, B. & Zheng, Y. Structural determinants required for the interaction between Rho GTPase and the GTPase-activating domain of p190. J. Biol Chem. 272, 32830-32835 (1997).
    • (1997) J. Biol Chem. , vol.272 , pp. 32830-32835
    • Li, R.1    Zhang, B.2    Zheng, Y.3
  • 39
    • 0031040253 scopus 로고    scopus 로고
    • Residues of the Rho family GTPases Rho and Cdc42 that specify sensitivity to Dbl-like guanine nucleotide exchange factors
    • Li, R. & Zheng, Y. Residues of the Rho family GTPases Rho and Cdc42 that specify sensitivity to Dbl-like guanine nucleotide exchange factors. J. Biol. Chem. 272, 4671-4679 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 4671-4679
    • Li, R.1    Zheng, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.