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Volumn 126, Issue 15, 2013, Pages 3271-3277

TEM4 is a junctional Rho GEF required for cell-cell adhesion, monolayer integrity and barrier function

Author keywords

Catenin; Cell adhesion; Cell junction; Guanine nucleotide exchange factor; RhoA; TEM4

Indexed keywords

ACTIN; CADHERIN; CATENIN; CYTOSKELETON PROTEIN; GUANINE NUCLEOTIDE EXCHANGE FACTOR; RHO FACTOR; SHORT HAIRPIN RNA; TUMOR ENDOTHELIAL MARKER 4 PROTEIN; UNCLASSIFIED DRUG;

EID: 84883350938     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.123869     Document Type: Article
Times cited : (34)

References (28)
  • 1
    • 17844402719 scopus 로고    scopus 로고
    • Binding of GEF-H1 to the tight junction-associated adaptor cingulin results in inhibition of Rho signaling and G1/S phase transition.
    • Aijaz, S., D'Atri, F., Citi, S., Balda, M. S. and Matter, K. (2005). Binding of GEF-H1 to the tight junction-associated adaptor cingulin results in inhibition of Rho signaling and G1/S phase transition. Dev. Cell 8, 777-786.
    • (2005) Dev. Cell , vol.8 , pp. 777-786
    • Aijaz, S.1    D'Atri, F.2    Citi, S.3    Balda, M.S.4    Matter, K.5
  • 3
    • 79955508089 scopus 로고    scopus 로고
    • Dynamics of adherens junctions in epithelial establishment, maintenance, and remodeling.
    • Baum, B. and Georgiou, M. (2011). Dynamics of adherens junctions in epithelial establishment, maintenance, and remodeling. J. Cell Biol. 192, 907-917.
    • (2011) J. Cell Biol. , vol.192 , pp. 907-917
    • Baum, B.1    Georgiou, M.2
  • 4
    • 0037416129 scopus 로고    scopus 로고
    • Identification of a tight junction-associated guanine nucleotide exchange factor that activates Rho and regulates paracellular permeability.
    • Benais-Pont, G., Punn, A., Flores-Maldonado, C., Eckert, J., Raposo, G., Fleming, T. P., Cereijido, M., Balda, M. S. and Matter, K. (2003). Identification of a tight junction-associated guanine nucleotide exchange factor that activates Rho and regulates paracellular permeability. J. Cell Biol. 160, 729-740.
    • (2003) J. Cell Biol. , vol.160 , pp. 729-740
    • Benais-Pont, G.1    Punn, A.2    Flores-Maldonado, C.3    Eckert, J.4    Raposo, G.5    Fleming, T.P.6    Cereijido, M.7    Balda, M.S.8    Matter, K.9
  • 5
    • 34247615185 scopus 로고    scopus 로고
    • GEF-H1 modulates localized RhoA activation during cytokinesis under the control of mitotic kinases.
    • Birkenfeld, J., Nalbant, P., Bohl, B. P., Pertz, O., Hahn, K. M. and Bokoch, G. M. (2007). GEF-H1 modulates localized RhoA activation during cytokinesis under the control of mitotic kinases. Dev. Cell 12, 699-712.
    • (2007) Dev. Cell , vol.12 , pp. 699-712
    • Birkenfeld, J.1    Nalbant, P.2    Bohl, B.P.3    Pertz, O.4    Hahn, K.M.5    Bokoch, G.M.6
  • 6
    • 57149101313 scopus 로고    scopus 로고
    • Identification of ARHGEF17, DENND2D, FGFR3, and RB1 mutations in melanoma by inhibition of nonsense-mediated mRNA decay.
    • Bloethner, S., Mould, A., Stark, M. and Hayward, N. K. (2008). Identification of ARHGEF17, DENND2D, FGFR3, and RB1 mutations in melanoma by inhibition of nonsense-mediated mRNA decay. Genes Chromosomes Cancer 47, 1076-1085.
    • (2008) Genes Chromosomes Cancer , vol.47 , pp. 1076-1085
    • Bloethner, S.1    Mould, A.2    Stark, M.3    Hayward, N.K.4
  • 7
    • 48249098842 scopus 로고    scopus 로고
    • GEF-H1 couples nocodazole-induced microtubule disassembly to cell contractility via RhoA.
    • Chang, Y. C., Nalbant, P., Birkenfeld, J., Chang, Z. F. and Bokoch, G. M. (2008). GEF-H1 couples nocodazole-induced microtubule disassembly to cell contractility via RhoA. Mol. Biol. Cell 19, 2147-2153.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2147-2153
    • Chang, Y.C.1    Nalbant, P.2    Birkenfeld, J.3    Chang, Z.F.4    Bokoch, G.M.5
  • 8
    • 0029995797 scopus 로고    scopus 로고
    • Rho-stimulated contractility drives the formation of stress fibers and focal adhesions.
    • Chrzanowska-Wodnicka, M. and Burridge, K. (1996). Rho-stimulated contractility drives the formation of stress fibers and focal adhesions. J. Cell Biol. 133, 1403-1415.
    • (1996) J. Cell Biol. , vol.133 , pp. 1403-1415
    • Chrzanowska-Wodnicka, M.1    Burridge, K.2
  • 9
    • 0042841777 scopus 로고    scopus 로고
    • Lumen formation: in vivo versus in vitro observations.
    • Egginton, S. and Gerritsen, M. (2003). Lumen formation: in vivo versus in vitro observations. Microcirculation 10, 45-61.
    • (2003) Microcirculation , vol.10 , pp. 45-61
    • Egginton, S.1    Gerritsen, M.2
  • 10
    • 0037069690 scopus 로고    scopus 로고
    • Rho GTPases in cell biology.
    • Etienne-Manneville, S. and Hall, A. (2002). Rho GTPases in cell biology. Nature 420, 629-635.
    • (2002) Nature , vol.420 , pp. 629-635
    • Etienne-Manneville, S.1    Hall, A.2
  • 11
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton.
    • Hall, A. (1998). Rho GTPases and the actin cytoskeleton. Science 279, 509-514.
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 13
    • 33748443594 scopus 로고    scopus 로고
    • Regulation of cell-cell junctions by the cytoskeleton.
    • Mége, R. M., Gavard, J. and Lambert, M. (2006). Regulation of cell-cell junctions by the cytoskeleton. Curr. Opin. Cell Biol. 18, 541-548.
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 541-548
    • Mége, R.M.1    Gavard, J.2    Lambert, M.3
  • 14
    • 84864243965 scopus 로고    scopus 로고
    • Identification of a novel actin-binding domain within the Rho guanine nucleotide exchange factor TEM4
    • Mitin, N., Rossman, K. L. and Der, C. J. (2012). Identification of a novel actin-binding domain within the Rho guanine nucleotide exchange factor TEM4. PLoS ONE 7, e41876.
    • (2012) PLoS ONE , vol.7 , pp. 41876
    • Mitin, N.1    Rossman, K.L.2    Der, C.J.3
  • 15
    • 80155186757 scopus 로고    scopus 로고
    • Lulu2 regulates the circumferential actomyosin tensile system in epithelial cells through p114RhoGEF.
    • Nakajima, H. and Tanoue, T. (2011). Lulu2 regulates the circumferential actomyosin tensile system in epithelial cells through p114RhoGEF. J. Cell Biol. 195, 245-261.
    • (2011) J. Cell Biol. , vol.195 , pp. 245-261
    • Nakajima, H.1    Tanoue, T.2
  • 16
    • 0029791373 scopus 로고    scopus 로고
    • The small GTPase Rho: cellular functions and signal transduction.
    • Narumiya, S. (1996). The small GTPase Rho: cellular functions and signal transduction. J. Biochem. 120, 215-228.
    • (1996) J. Biochem. , vol.120 , pp. 215-228
    • Narumiya, S.1
  • 18
    • 84874789491 scopus 로고    scopus 로고
    • Phosphorylation-mediated 14-3-3 protein binding regulates the function of the rho-specific guanine nucleotide exchange factor (RhoGEF) Syx.
    • Ngok, S. P., Geyer, R., Kourtidis, A., Storz, P. and Anastasiadis, P. Z. (2013). Phosphorylation-mediated 14-3-3 protein binding regulates the function of the rho-specific guanine nucleotide exchange factor (RhoGEF) Syx. J. Biol. Chem. 288, 6640-6650.
    • (2013) J. Biol. Chem. , vol.288 , pp. 6640-6650
    • Ngok, S.P.1    Geyer, R.2    Kourtidis, A.3    Storz, P.4    Anastasiadis, P.Z.5
  • 19
    • 0028961293 scopus 로고
    • Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia.
    • Nobes, C. D. and Hall, A. (1995). Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81, 53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 21
    • 0032567341 scopus 로고    scopus 로고
    • Cloning and characterization of GEF-H1, a microtubule-associated guanine nucleotide exchange factor for Rac and Rho GTPases.
    • Ren, Y., Li, R., Zheng, Y. and Busch, H. (1998). Cloning and characterization of GEF-H1, a microtubule-associated guanine nucleotide exchange factor for Rac and Rho GTPases. J. Biol. Chem. 273, 34954-34960.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34954-34960
    • Ren, Y.1    Li, R.2    Zheng, Y.3    Busch, H.4
  • 22
    • 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. and Hall, A. (1992). The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70, 389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 23
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling.
    • Ridley, A. J., Paterson, H. F., Johnston, C. L., Diekmann, D. and Hall, A. (1992). The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell 70, 401-410.
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 24
    • 13444252631 scopus 로고    scopus 로고
    • GEF means go: turning on RHO GTPases with guanine nucleotide-exchange factors.
    • Rossman, K. L., Der, C. J. and Sondek, J. (2005). GEF means go: turning on RHO GTPases with guanine nucleotide-exchange factors. Nat. Rev. Mol. Cell Biol. 6, 167-180.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 167-180
    • Rossman, K.L.1    Der, C.J.2    Sondek, J.3
  • 25
    • 0037106342 scopus 로고    scopus 로고
    • A mammalian Rho-specific guanine-nucleotide exchange factor (p164-RhoGEF) without a pleckstrin homology domain.
    • Rümenapp, U., Freichel-Blomquist, A., Wittinghofer, B., Jakobs, K. H. and Wieland, T. (2002). A mammalian Rho-specific guanine-nucleotide exchange factor (p164-RhoGEF) without a pleckstrin homology domain. Biochem. J. 366, 721-728.
    • (2002) Biochem. J. , vol.366 , pp. 721-728
    • Rümenapp, U.1    Freichel-Blomquist, A.2    Wittinghofer, B.3    Jakobs, K.H.4    Wieland, T.5
  • 27
    • 79551612886 scopus 로고    scopus 로고
    • Spatially restricted activation of RhoA signalling at epithelial junctions by p114RhoGEF drives junction formation and morphogenesis.
    • Terry, S. J., Zihni, C., Elbediwy, A., Vitiello, E., Leefa Chong San, I. V., Balda, M. S. and Matter, K. (2011). Spatially restricted activation of RhoA signalling at epithelial junctions by p114RhoGEF drives junction formation and morphogenesis. Nat. Cell Biol. 13, 159-166.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 159-166
    • Terry, S.J.1    Zihni, C.2    Elbediwy, A.3    Vitiello, E.4    Leefa Chong San, I.V.5    Balda, M.S.6    Matter, K.7
  • 28
    • 0025023525 scopus 로고
    • Steps in the morphogenesis of a polarized epithelium. I. Uncoupling the roles of cell-cell and cell-substratum contact in establishing plasma membrane polarity in multicellular epithelial (MDCK) cysts
    • Wang, A. Z., Ojakian, G. K. and Nelson, W. J. (1990). Steps in the morphogenesis of a polarized epithelium. I. Uncoupling the roles of cell-cell and cell-substratum contact in establishing plasma membrane polarity in multicellular epithelial (MDCK) cysts. J. Cell Sci. 95, 137-151.
    • (1990) J. Cell Sci. , vol.95 , pp. 137-151
    • Wang, A.Z.1    Ojakian, G.K.2    Nelson, W.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.