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Volumn 27, Issue 5, 2013, Pages 545-559

FHOD1 is needed for directed forces and adhesion maturation during cell spreading and migration

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; FHOD1 PROTEIN; INTEGRIN; PROTEIN; PROTEIN TYROSINE KINASE; RHO KINASE; UNCLASSIFIED DRUG;

EID: 84892159494     PISSN: 15345807     EISSN: 18781551     Source Type: Journal    
DOI: 10.1016/j.devcel.2013.11.003     Document Type: Article
Times cited : (89)

References (55)
  • 1
    • 52449089651 scopus 로고    scopus 로고
    • Comparative dynamics of retrograde actin flow and focal adhesions: formation of nascent adhesions triggers transition from fast to slow flow
    • Alexandrova A.Y., Arnold K., Schaub S., Vasiliev J.M., Meister J.J., Bershadsky A.D., Verkhovsky A.B. Comparative dynamics of retrograde actin flow and focal adhesions: formation of nascent adhesions triggers transition from fast to slow flow. PLoS ONE 2008, 3:e3234.
    • (2008) PLoS ONE , vol.3
    • Alexandrova, A.Y.1    Arnold, K.2    Schaub, S.3    Vasiliev, J.M.4    Meister, J.J.5    Bershadsky, A.D.6    Verkhovsky, A.B.7
  • 2
    • 0027436135 scopus 로고
    • Binding of the Src SH2 domain to phosphopeptides is determined by residues in both the SH2 domain and the phosphopeptides
    • Bibbins K.B., Boeuf H., Varmus H.E. Binding of the Src SH2 domain to phosphopeptides is determined by residues in both the SH2 domain and the phosphopeptides. Mol. Cell. Biol. 1993, 13:7278-7287.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7278-7287
    • Bibbins, K.B.1    Boeuf, H.2    Varmus, H.E.3
  • 4
    • 77949834455 scopus 로고    scopus 로고
    • A nucleator arms race: cellular control of actin assembly
    • Campellone K.G., Welch M.D. A nucleator arms race: cellular control of actin assembly. Nat. Rev. Mol. Cell Biol. 2010, 11:237-251.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 237-251
    • Campellone, K.G.1    Welch, M.D.2
  • 5
    • 0036205320 scopus 로고    scopus 로고
    • SRC catalytic but not scaffolding function is needed for integrin-regulated tyrosine phosphorylation, cell migration, and cell spreading
    • Cary L.A., Klinghoffer R.A., Sachsenmaier C., Cooper J.A. SRC catalytic but not scaffolding function is needed for integrin-regulated tyrosine phosphorylation, cell migration, and cell spreading. Mol. Cell. Biol. 2002, 22:2427-2440.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2427-2440
    • Cary, L.A.1    Klinghoffer, R.A.2    Sachsenmaier, C.3    Cooper, J.A.4
  • 6
    • 51049104617 scopus 로고    scopus 로고
    • Actin and alpha-actinin orchestrate the assembly and maturation of nascent adhesions in a myosin II motor-independent manner
    • Choi C.K., Vicente-Manzanares M., Zareno J., Whitmore L.A., Mogilner A., Horwitz A.R. Actin and alpha-actinin orchestrate the assembly and maturation of nascent adhesions in a myosin II motor-independent manner. Nat. Cell Biol. 2008, 10:1039-1050.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1039-1050
    • Choi, C.K.1    Vicente-Manzanares, M.2    Zareno, J.3    Whitmore, L.A.4    Mogilner, A.5    Horwitz, A.R.6
  • 7
    • 0030994017 scopus 로고    scopus 로고
    • Extracellular matrix rigidity causes strengthening of integrin-cytoskeleton linkages
    • Choquet D., Felsenfeld D.P., Sheetz M.P. Extracellular matrix rigidity causes strengthening of integrin-cytoskeleton linkages. Cell 1997, 88:39-48.
    • (1997) Cell , vol.88 , pp. 39-48
    • Choquet, D.1    Felsenfeld, D.P.2    Sheetz, M.P.3
  • 8
    • 84878982264 scopus 로고    scopus 로고
    • Tension modulates actin filament polymerization mediated by formin and profilin
    • Courtemanche N., Lee J.Y., Pollard T.D., Greene E.C. Tension modulates actin filament polymerization mediated by formin and profilin. Proc. Natl. Acad. Sci. USA 2013, 110:9752-9757.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 9752-9757
    • Courtemanche, N.1    Lee, J.Y.2    Pollard, T.D.3    Greene, E.C.4
  • 17
    • 33749037156 scopus 로고    scopus 로고
    • The ARP2/3 complex: an actin nucleator comes of age
    • Goley E.D., Welch M.D. The ARP2/3 complex: an actin nucleator comes of age. Nat. Rev. Mol. Cell Biol. 2006, 7:713-726.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 713-726
    • Goley, E.D.1    Welch, M.D.2
  • 18
    • 34248154652 scopus 로고    scopus 로고
    • Mechanism and function of formins in the control of actin assembly
    • Goode B.L., Eck M.J. Mechanism and function of formins in the control of actin assembly. Annu. Rev. Biochem. 2007, 76:593-627.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 593-627
    • Goode, B.L.1    Eck, M.J.2
  • 19
    • 35648943165 scopus 로고    scopus 로고
    • MDia2 regulates actin and focal adhesion dynamics and organization in the lamella for efficient epithelial cell migration
    • Gupton S.L., Eisenmann K., Alberts A.S., Waterman-Storer C.M. mDia2 regulates actin and focal adhesion dynamics and organization in the lamella for efficient epithelial cell migration. J.Cell Sci. 2007, 120:3475-3487.
    • (2007) J.Cell Sci. , vol.120 , pp. 3475-3487
    • Gupton, S.L.1    Eisenmann, K.2    Alberts, A.S.3    Waterman-Storer, C.M.4
  • 22
    • 66849101632 scopus 로고    scopus 로고
    • Adhesion signaling - crosstalk between integrins, Src and Rho
    • Huveneers S., Danen E.H. Adhesion signaling - crosstalk between integrins, Src and Rho. J.Cell Sci. 2009, 122:1059-1069.
    • (2009) J.Cell Sci. , vol.122 , pp. 1059-1069
    • Huveneers, S.1    Danen, E.H.2
  • 23
    • 78650078032 scopus 로고    scopus 로고
    • Formin follows function: a muscle-specific isoform of FHOD3 is regulated by CK2 phosphorylation and promotes myofibril maintenance
    • Iskratsch T., Lange S., Dwyer J., Kho A.L., dos Remedios C., Ehler E. Formin follows function: a muscle-specific isoform of FHOD3 is regulated by CK2 phosphorylation and promotes myofibril maintenance. J.Cell Biol. 2010, 191:1159-1172.
    • (2010) J.Cell Biol. , vol.191 , pp. 1159-1172
    • Iskratsch, T.1    Lange, S.2    Dwyer, J.3    Kho, A.L.4    dos Remedios, C.5    Ehler, E.6
  • 25
    • 84878722228 scopus 로고    scopus 로고
    • Formin mDia1 senses and generates mechanical forces on actin filaments
    • Jégou A., Carlier M.F., Romet-Lemonne G. Formin mDia1 senses and generates mechanical forces on actin filaments. Nat. Commun. 2013, 4:1883.
    • (2013) Nat. Commun. , vol.4 , pp. 1883
    • Jégou, A.1    Carlier, M.F.2    Romet-Lemonne, G.3
  • 26
    • 24044465136 scopus 로고    scopus 로고
    • Novel Src homology 3 domain-binding motifs identified from proteomic screen of a Pro-rich region
    • Jia C.Y., Nie J., Wu C., Li C., Li S.S. Novel Src homology 3 domain-binding motifs identified from proteomic screen of a Pro-rich region. Mol. Cell. Proteomics 2005, 4:1155-1166.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1155-1166
    • Jia, C.Y.1    Nie, J.2    Wu, C.3    Li, C.4    Li, S.S.5
  • 27
    • 0041461882 scopus 로고    scopus 로고
    • Two-piconewton slip bond between fibronectin and the cytoskeleton depends on talin
    • Jiang G., Giannone G., Critchley D.R., Fukumoto E., Sheetz M.P. Two-piconewton slip bond between fibronectin and the cytoskeleton depends on talin. Nature 2003, 424:334-337.
    • (2003) Nature , vol.424 , pp. 334-337
    • Jiang, G.1    Giannone, G.2    Critchley, D.R.3    Fukumoto, E.4    Sheetz, M.P.5
  • 28
    • 0032561342 scopus 로고    scopus 로고
    • Interaction of Bnr1p with a novel Src homology 3 domain-containing Hof1p. Implication in cytokinesis in Saccharomyces cerevisiae
    • Kamei T., Tanaka K., Hihara T., Umikawa M., Imamura H., Kikyo M., Ozaki K., Takai Y. Interaction of Bnr1p with a novel Src homology 3 domain-containing Hof1p. Implication in cytokinesis in Saccharomyces cerevisiae. J.Biol. Chem. 1998, 273:28341-28345.
    • (1998) J.Biol. Chem. , vol.273 , pp. 28341-28345
    • Kamei, T.1    Tanaka, K.2    Hihara, T.3    Umikawa, M.4    Imamura, H.5    Kikyo, M.6    Ozaki, K.7    Takai, Y.8
  • 29
    • 0033522510 scopus 로고    scopus 로고
    • Src family kinases are required for integrin but not PDGFR signal transduction
    • Klinghoffer R.A., Sachsenmaier C., Cooper J.A., Soriano P. Src family kinases are required for integrin but not PDGFR signal transduction. EMBO J. 1999, 18:2459-2471.
    • (1999) EMBO J. , vol.18 , pp. 2459-2471
    • Klinghoffer, R.A.1    Sachsenmaier, C.2    Cooper, J.A.3    Soriano, P.4
  • 31
    • 33744772918 scopus 로고    scopus 로고
    • Fibronectin rigidity response through Fyn and p130Cas recruitment to the leading edge
    • Kostic A., Sheetz M.P. Fibronectin rigidity response through Fyn and p130Cas recruitment to the leading edge. Mol. Biol. Cell 2006, 17:2684-2695.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2684-2695
    • Kostic, A.1    Sheetz, M.P.2
  • 33
    • 0029786988 scopus 로고    scopus 로고
    • Knockouts of Src-family kinases: stiff bones, wimpy Tcells, and bad memories
    • Lowell C.A., Soriano P. Knockouts of Src-family kinases: stiff bones, wimpy Tcells, and bad memories. Genes Dev. 1996, 10:1845-1857.
    • (1996) Genes Dev. , vol.10 , pp. 1845-1857
    • Lowell, C.A.1    Soriano, P.2
  • 34
    • 77649271537 scopus 로고    scopus 로고
    • The role of formins in filopodia formation
    • Mellor H. The role of formins in filopodia formation. Biochim. Biophys. Acta 2010, 1803:191-200.
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 191-200
    • Mellor, H.1
  • 36
    • 0035958959 scopus 로고    scopus 로고
    • Processive phosphorylation of p130Cas by Src depends on SH3-polyproline interactions
    • Pellicena P., Miller W.T. Processive phosphorylation of p130Cas by Src depends on SH3-polyproline interactions. J.Biol. Chem. 2001, 276:28190-28196.
    • (2001) J.Biol. Chem. , vol.276 , pp. 28190-28196
    • Pellicena, P.1    Miller, W.T.2
  • 37
    • 0032547071 scopus 로고    scopus 로고
    • Enhanced phosphorylation of Src family kinase substrates containing SH2 domain binding sites
    • Pellicena P., Stowell K.R., Miller W.T. Enhanced phosphorylation of Src family kinase substrates containing SH2 domain binding sites. J.Biol. Chem. 1998, 273:15325-15328.
    • (1998) J.Biol. Chem. , vol.273 , pp. 15325-15328
    • Pellicena, P.1    Stowell, K.R.2    Miller, W.T.3
  • 38
    • 70349171810 scopus 로고    scopus 로고
    • The formin-homology protein SmDia interacts with the Src kinase SmTK and the GTPase SmRho1 in the gonads of Schistosoma mansoni
    • Quack T., Knobloch J., Beckmann S., Vicogne J., Dissous C., Grevelding C.G. The formin-homology protein SmDia interacts with the Src kinase SmTK and the GTPase SmRho1 in the gonads of Schistosoma mansoni. PLoS ONE 2009, 4:e6998.
    • (2009) PLoS ONE , vol.4
    • Quack, T.1    Knobloch, J.2    Beckmann, S.3    Vicogne, J.4    Dissous, C.5    Grevelding, C.G.6
  • 40
    • 0038024241 scopus 로고    scopus 로고
    • Rocks: multifunctional kinases in cell behaviour
    • Riento K., Ridley A.J. Rocks: multifunctional kinases in cell behaviour. Nat. Rev. Mol. Cell Biol. 2003, 4:446-456.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 446-456
    • Riento, K.1    Ridley, A.J.2
  • 41
    • 84869102195 scopus 로고    scopus 로고
    • Finding the weakest link: exploring integrin-mediated mechanical molecular pathways
    • Roca-Cusachs P., Iskratsch T., Sheetz M.P. Finding the weakest link: exploring integrin-mediated mechanical molecular pathways. J.Cell Sci. 2012, 125:3025-3038.
    • (2012) J.Cell Sci. , vol.125 , pp. 3025-3038
    • Roca-Cusachs, P.1    Iskratsch, T.2    Sheetz, M.P.3
  • 43
    • 13544256790 scopus 로고    scopus 로고
    • Src protein-tyrosine kinase structure and regulation
    • Roskoski R. Src protein-tyrosine kinase structure and regulation. Biochem. Biophys. Res. Commun. 2004, 324:1155-1164.
    • (2004) Biochem. Biophys. Res. Commun. , vol.324 , pp. 1155-1164
    • Roskoski, R.1
  • 45
    • 50849103669 scopus 로고    scopus 로고
    • The human formin FHOD1 contains a bipartite structure of FH3 and GTPase-binding domains required for activation
    • Schulte A., Stolp B., Schönichen A., Pylypenko O., Rak A., Fackler O.T., Geyer M. The human formin FHOD1 contains a bipartite structure of FH3 and GTPase-binding domains required for activation. Structure 2008, 16:1313-1323.
    • (2008) Structure , vol.16 , pp. 1313-1323
    • Schulte, A.1    Stolp, B.2    Schönichen, A.3    Pylypenko, O.4    Rak, A.5    Fackler, O.T.6    Geyer, M.7
  • 48
    • 0033620689 scopus 로고    scopus 로고
    • Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia
    • Svitkina T.M., Borisy G.G. Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia. J.Cell Biol. 1999, 145:1009-1026.
    • (1999) J.Cell Biol. , vol.145 , pp. 1009-1026
    • Svitkina, T.M.1    Borisy, G.G.2
  • 49
    • 39449085061 scopus 로고    scopus 로고
    • The mammalian formin FHOD1 is activated through phosphorylation by ROCK and mediates thrombin-induced stress fibre formation in endothelial cells
    • Takeya R., Taniguchi K., Narumiya S., Sumimoto H. The mammalian formin FHOD1 is activated through phosphorylation by ROCK and mediates thrombin-induced stress fibre formation in endothelial cells. EMBO J. 2008, 27:618-628.
    • (2008) EMBO J. , vol.27 , pp. 618-628
    • Takeya, R.1    Taniguchi, K.2    Narumiya, S.3    Sumimoto, H.4
  • 50
    • 80051599187 scopus 로고    scopus 로고
    • G-protein coupled and ITAM receptor regulation of the formin FHOD1 through Rho kinase in platelets
    • Thomas S.G., Calaminus S.D., Machesky L.M., Alberts A.S., Watson S.P. G-protein coupled and ITAM receptor regulation of the formin FHOD1 through Rho kinase in platelets. J.Thromb. Haemost. 2011, 9:1648-1651.
    • (2011) J.Thromb. Haemost. , vol.9 , pp. 1648-1651
    • Thomas, S.G.1    Calaminus, S.D.2    Machesky, L.M.3    Alberts, A.S.4    Watson, S.P.5
  • 51
    • 0037437150 scopus 로고    scopus 로고
    • RPTP-alpha acts as a transducer of mechanical force on alphav/beta3-integrin-cytoskeleton linkages
    • von Wichert G., Jiang G., Kostic A., De Vos K., Sap J., Sheetz M.P. RPTP-alpha acts as a transducer of mechanical force on alphav/beta3-integrin-cytoskeleton linkages. J.Cell Biol. 2003, 161:143-153.
    • (2003) J.Cell Biol. , vol.161 , pp. 143-153
    • von Wichert, G.1    Jiang, G.2    Kostic, A.3    De Vos, K.4    Sap, J.5    Sheetz, M.P.6
  • 52
    • 0033160196 scopus 로고    scopus 로고
    • Cooperation between mDia1 and ROCK in Rho-induced actin reorganization
    • Watanabe N., Kato T., Fujita A., Ishizaki T., Narumiya S. Cooperation between mDia1 and ROCK in Rho-induced actin reorganization. Nat. Cell Biol. 1999, 1:136-143.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 136-143
    • Watanabe, N.1    Kato, T.2    Fujita, A.3    Ishizaki, T.4    Narumiya, S.5
  • 55
    • 84855500059 scopus 로고    scopus 로고
    • Early integrin binding to Arg-Gly-Asp peptide activates actin polymerization and contractile movement that stimulates outward translocation
    • Yu C.H., Law J.B., Suryana M., Low H.Y., Sheetz M.P. Early integrin binding to Arg-Gly-Asp peptide activates actin polymerization and contractile movement that stimulates outward translocation. Proc. Natl. Acad. Sci. USA 2011, 108:20585-20590.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 20585-20590
    • Yu, C.H.1    Law, J.B.2    Suryana, M.3    Low, H.Y.4    Sheetz, M.P.5


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