메뉴 건너뛰기




Volumn 126, Issue 8, 2013, Pages 1891-1901

FHOD1 is a combined actin filament capping and bundling factor that selectively associates with actin arcs and stress fibers

Author keywords

Actin arcs; Actin bundling; FHOD1; Retrograde flow; Stress fibers

Indexed keywords

ACTIN; F ACTIN; FH1 FH2 DOMAIN CONTAINING PROTEIN 1; PEPTIDES AND PROTEINS; TROPOMYOSIN; UNCLASSIFIED DRUG;

EID: 84877968641     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.126706     Document Type: Article
Times cited : (72)

References (49)
  • 1
    • 0035951824 scopus 로고    scopus 로고
    • Identification of a carboxyl-terminal diaphanous-related formin homology protein autoregulatory domain
    • Alberts, A. S. (2001). Identification of a carboxyl-terminal diaphanous-related formin homology protein autoregulatory domain. J. Biol. Chem. 276, 2824-2830.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2824-2830
    • Alberts, A.S.1
  • 3
    • 84861708449 scopus 로고    scopus 로고
    • Rocket launcher mechanism of collaborative actin assembly defined by single-molecule imaging
    • Breitsprecher, D., Jaiswal, R., Bombardier, J. P., Gould, C. J., Gelles, J. and Goode, B. L. (2012). Rocket launcher mechanism of collaborative actin assembly defined by single-molecule imaging. Science 336, 1164-1168.
    • (2012) Science , vol.336 , pp. 1164-1168
    • Breitsprecher, D.1    Jaiswal, R.2    Bombardier, J.P.3    Gould, C.J.4    Gelles, J.5    Goode, B.L.6
  • 5
    • 72949110575 scopus 로고    scopus 로고
    • Unleashing formins to remodel the actin and microtubule cytoskeletons
    • Chesarone, M. A., DuPage, A. G. and Goode, B. L. (2010). Unleashing formins to remodel the actin and microtubule cytoskeletons. Nat. Rev. Mol. Cell Biol. 11, 62-74.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 62-74
    • Chesarone, M.A.1    DuPage, A.G.2    Goode, B.L.3
  • 6
    • 0030864069 scopus 로고    scopus 로고
    • Identification of novel graded polarity actin filament bundles in locomoting heart fibroblasts: implications for the generation of motile force
    • Cramer, L. P., Siebert, M. and Mitchison, T. J. (1997). Identification of novel graded polarity actin filament bundles in locomoting heart fibroblasts: implications for the generation of motile force. J. Cell Biol. 136, 1287-1305.
    • (1997) J. Cell Biol. , vol.136 , pp. 1287-1305
    • Cramer, L.P.1    Siebert, M.2    Mitchison, T.J.3
  • 7
    • 80054709439 scopus 로고    scopus 로고
    • Structure, dynamics, lipid binding, and physiological relevance of the putative GTPase-binding domain of Dictyostelium formin C
    • Dames, S. A., Junemann, A., Sass, H. J., Schönichen, A., Stopschinski, B. E., Grzesiek, S., Faix, J. and Geyer, M. (2011). Structure, dynamics, lipid binding, and physiological relevance of the putative GTPase-binding domain of Dictyostelium formin C. J. Biol. Chem. 286, 36907-36920.
    • (2011) J. Biol. Chem. , vol.286 , pp. 36907-36920
    • Dames, S.A.1    Junemann, A.2    Sass, H.J.3    Schönichen, A.4    Stopschinski, B.E.5    Grzesiek, S.6    Faix, J.7    Geyer, M.8
  • 8
    • 33745027397 scopus 로고    scopus 로고
    • Quantitative fluorescent speckle microscopy of cytoskeleton dynamics
    • Danuser, G. and Waterman-Storer, C. M. (2006). Quantitative fluorescent speckle microscopy of cytoskeleton dynamics. Annu. Rev. Biophys. Biomol. Struct. 35, 361- 387.
    • (2006) Annu. Rev. Biophys. Biomol. Struct. , vol.35 , pp. 361-387
    • Danuser, G.1    Waterman-Storer, C.M.2
  • 10
    • 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. and Waterman-Storer, C. M. (2007). mDia2 regulates actin and focal adhesion dynamics and organization in the lamella for efficient epithelial cell migration. J. Cell Sci. 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
  • 12
    • 33646867122 scopus 로고    scopus 로고
    • Mechanistic differences in actin bundling activity of two mammalian formins, FRL1 and mDia2
    • Harris, E. S., Rouiller, I., Hanein, D. and Higgs, H. N. (2006). Mechanistic differences in actin bundling activity of two mammalian formins, FRL1 and mDia2. J. Biol. Chem. 281, 14383-14392.
    • (2006) J. Biol. Chem. , vol.281 , pp. 14383-14392
    • Harris, E.S.1    Rouiller, I.2    Hanein, D.3    Higgs, H.N.4
  • 13
    • 0027134875 scopus 로고
    • The actin monomers in the ternary gelsolin: 2 actin complex are in an antiparallel orientation
    • Hesterkamp, T., Weeds, A. G. and Mannherz, H. G. (1993). The actin monomers in the ternary gelsolin: 2 actin complex are in an antiparallel orientation. Eur. J. Biochem. 218, 507-513.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 507-513
    • Hesterkamp, T.1    Weeds, A.G.2    Mannherz, H.G.3
  • 15
    • 33646386142 scopus 로고    scopus 로고
    • Stress fibers are generated by two distinct actin assembly mechanisms in motile cells
    • Hotulainen, P. and Lappalainen, P. (2006). Stress fibers are generated by two distinct actin assembly mechanisms in motile cells. J. Cell Biol. 173, 383-394.
    • (2006) J. Cell Biol. , vol.173 , pp. 383-394
    • Hotulainen, P.1    Lappalainen, P.2
  • 16
    • 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. and Ehler, E. (2010). Formin follows function: a muscle-specific isoform of FHOD3 is regulated by CK2 phosphorylation and promotes myofibril maintenance. J. Cell Biol. 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
  • 18
    • 0018162170 scopus 로고
    • p-NN9-phenylenebismaleimide, a specific crosslinking agent for F-actin
    • Knight, P. and Offer, G. (1978). p-NN9-phenylenebismaleimide, a specific crosslinking agent for F-actin. Biochem. J. 175, 1023-1032.
    • (1978) Biochem. J. , vol.175 , pp. 1023-1032
    • Knight, P.1    Offer, G.2
  • 19
    • 6944220067 scopus 로고    scopus 로고
    • Insertional assembly of actin filament barbed ends in association with formins produces piconewton forces
    • USA
    • Kovar, D. R. and Pollard, T. D. (2004). Insertional assembly of actin filament barbed ends in association with formins produces piconewton forces. Proc. Natl. Acad. Sci. USA 101, 14725-14730.
    • (2004) Proc. Natl. Acad. Sci. , vol.101 , pp. 14725-14730
    • Kovar, D.R.1    Pollard, T.D.2
  • 20
    • 81255134470 scopus 로고    scopus 로고
    • Integrin adhesion and force coupling are independently regulated by localized PtdIns(4,5)2 synthesis
    • Legate, K. R., Takahashi, S., Bonakdar, N., Fabry, B., Boettiger, D., Zent, R. and Fässler, R. (2011). Integrin adhesion and force coupling are independently regulated by localized PtdIns(4,5)2 synthesis. EMBO J. 30, 4539-4553.
    • (2011) EMBO J. , vol.30 , pp. 4539-4553
    • Legate, K.R.1    Takahashi, S.2    Bonakdar, N.3    Fabry, B.4    Boettiger, D.5    Zent, R.6    Fässler, R.7
  • 21
    • 0043202969 scopus 로고    scopus 로고
    • The mouse Formin mDia1 is a potent actin nucleation factor regulated by autoinhibition
    • Li, F. and Higgs, H. N. (2003). The mouse Formin mDia1 is a potent actin nucleation factor regulated by autoinhibition. Curr. Biol. 13, 1335-1340.
    • (2003) Curr. Biol. , vol.13 , pp. 1335-1340
    • Li, F.1    Higgs, H.N.2
  • 22
    • 33846642485 scopus 로고    scopus 로고
    • Mapping the ADF/cofilin binding site on monomeric actin by competitive cross-linking and peptide array: evidence for a second binding site on monomeric actin
    • Mannherz, H. G., Ballweber, E., Galla, M., Villard, S., Granier, C., Steegborn, C., Schmidtmann, A., Jaquet, K., Pope, B. and Weeds, A. G. (2007). Mapping the ADF/cofilin binding site on monomeric actin by competitive cross-linking and peptide array: evidence for a second binding site on monomeric actin. J. Mol. Biol. 366, 745-755.
    • (2007) J. Mol. Biol. , vol.366 , pp. 745-755
    • Mannherz, H.G.1    Ballweber, E.2    Galla, M.3    Villard, S.4    Granier, C.5    Steegborn, C.6    Schmidtmann, A.7    Jaquet, K.8    Pope, B.9    Weeds, A.G.10
  • 23
    • 84865098229 scopus 로고    scopus 로고
    • Z-line formins promote contractile lattice growth and maintenance in striated muscles of C
    • Mi-Mi, L., Votra, S., Kemphues, K., Bretscher, A. and Pruyne, D. (2012). Z-line formins promote contractile lattice growth and maintenance in striated muscles of C. elegans. J. Cell Biol. 198, 87-102.
    • (2012) elegans. J. Cell Biol. , vol.198 , pp. 87-102
    • Mi-Mi, L.1    Votra, S.2    Kemphues, K.3    Bretscher, A.4    Pruyne, D.5
  • 24
    • 33845700946 scopus 로고    scopus 로고
    • Actin turnover-dependent fast dissociation of capping protein in the dendritic nucleation actin network: evidence of frequent filament severing
    • Miyoshi, T., Tsuji, T., Higashida, C., Hertzog, M., Fujita, A., Narumiya, S., Scita, G. and Watanabe, N. (2006). Actin turnover-dependent fast dissociation of capping protein in the dendritic nucleation actin network: evidence of frequent filament severing. J. Cell Biol. 175, 947-955.
    • (2006) J. Cell Biol. , vol.175 , pp. 947-955
    • Miyoshi, T.1    Tsuji, T.2    Higashida, C.3    Hertzog, M.4    Fujita, A.5    Narumiya, S.6    Scita, G.7    Watanabe, N.8
  • 25
    • 23044510466 scopus 로고    scopus 로고
    • Differential activities and regulation of Saccharomyces cerevisiae formin proteins Bni1 and Bnr1 by Bud6
    • Moseley, J. B. and Goode, B. L. (2005). Differential activities and regulation of Saccharomyces cerevisiae formin proteins Bni1 and Bnr1 by Bud6. J. Biol. Chem. 280, 28023-28033.
    • (2005) J. Biol. Chem. , vol.280 , pp. 28023-28033
    • Moseley, J.B.1    Goode, B.L.2
  • 26
    • 0742305302 scopus 로고    scopus 로고
    • A conserved mechanism for Bni1- and mDia1-induced actin assembly and dual regulation of Bni1 by Bud6 and profilin
    • Moseley, J. B., Sagot, I., Manning, A. L., Xu, Y., Eck, M. J., Pellman, D. and Goode, B. L. (2004). A conserved mechanism for Bni1- and mDia1-induced actin assembly and dual regulation of Bni1 by Bud6 and profilin. Mol. Biol. Cell 15, 896-907.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 896-907
    • Moseley, J.B.1    Sagot, I.2    Manning, A.L.3    Xu, Y.4    Eck, M.J.5    Pellman, D.6    Goode, B.L.7
  • 27
    • 2342662152 scopus 로고    scopus 로고
    • Negative Staining and Image Classification - Powerful Tools in Modern Electron Microscopy
    • Ohi, M., Li, Y., Cheng, Y. and Walz, T. (2004). Negative Staining and Image Classification - Powerful Tools in Modern Electron Microscopy. Biol. Proced. Online 6, 23-34.
    • (2004) Biol. Proced. Online , vol.6 , pp. 23-34
    • Ohi, M.1    Li, Y.2    Cheng, Y.3    Walz, T.4
  • 29
    • 80855133531 scopus 로고    scopus 로고
    • Membrane binding of the N-terminal ubiquitin-like domain of kindlin-2 is crucial for its regulation of integrin activation
    • Perera, H. D., Ma, Y. Q., Yang, J., Hirbawi, J., Plow, E. F. and Qin, J. (2011). Membrane binding of the N-terminal ubiquitin-like domain of kindlin-2 is crucial for its regulation of integrin activation. Structure 19, 1664-1671.
    • (2011) Structure , vol.19 , pp. 1664-1671
    • Perera, H.D.1    Ma, Y.Q.2    Yang, J.3    Hirbawi, J.4    Plow, E.F.5    Qin, J.6
  • 30
    • 35349021033 scopus 로고    scopus 로고
    • Regulatory interactions between two actin nucleators, Spire and Cappuccino
    • Quinlan, M. E., Hilgert, S., Bedrossian, A., Mullins, R. D. and Kerkhoff, E. (2007). Regulatory interactions between two actin nucleators, Spire and Cappuccino. J. Cell Biol. 179, 117-128.
    • (2007) J. Cell Biol. , vol.179 , pp. 117-128
    • Quinlan, M.E.1    Hilgert, S.2    Bedrossian, A.3    Mullins, R.D.4    Kerkhoff, E.5
  • 31
    • 79959677602 scopus 로고    scopus 로고
    • Life at the leading edge
    • Ridley, A. J. (2011). Life at the leading edge. Cell 145, 1012-1022.
    • (2011) Cell , vol.145 , pp. 1012-1022
    • Ridley, A.J.1
  • 32
    • 7044224754 scopus 로고    scopus 로고
    • Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis
    • Romero, S., Le Clainche, C., Didry, D., Egile, C., Pantaloni, D. and Carlier, M. F. (2004). Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis. Cell 119, 419-429.
    • (2004) Cell , vol.119 , pp. 419-429
    • Romero, S.1    Le Clainche, C.2    Didry, D.3    Egile, C.4    Pantaloni, D.5    Carlier, M.F.6
  • 33
    • 77649273530 scopus 로고    scopus 로고
    • Fifteen formins for an actin filament: a molecular view on the regulation of human formins
    • Schönichen, A. and Geyer, M. (2010). Fifteen formins for an actin filament: a molecular view on the regulation of human formins. Biochim. Biophys. Acta 1803, 152-163.
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 152-163
    • Schönichen, A.1    Geyer, M.2
  • 34
    • 33646185063 scopus 로고    scopus 로고
    • Biochemical characterization of the diaphanous autoregulatory interaction in the formin homology protein FHOD1
    • Schönichen, A., Alexander, M., Gasteier, J. E., Cuesta, F. E., Fackler, O. T. and Geyer, M. (2006). Biochemical characterization of the diaphanous autoregulatory interaction in the formin homology protein FHOD1. J. Biol. Chem. 281, 5084-5093.
    • (2006) J. Biol. Chem. , vol.281 , pp. 5084-5093
    • Schönichen, A.1    Alexander, M.2    Gasteier, J.E.3    Cuesta, F.E.4    Fackler, O.T.5    Geyer, M.6
  • 35
    • 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. and Geyer, M. (2008). The human formin FHOD1 contains a bipartite structure of FH3 and GTPase-binding domains required for activation. Structure 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
  • 37
    • 62849125813 scopus 로고    scopus 로고
    • The initial steps of myofibril assembly: integrins pave the way
    • Sparrow, J. C. and Schöck, F. (2009). The initial steps of myofibril assembly: integrins pave the way. Nat. Rev. Mol. Cell Biol. 10, 293-298.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 293-298
    • Sparrow, J.C.1    Schöck, F.2
  • 39
    • 0345328684 scopus 로고    scopus 로고
    • Fhos, a mammalian formin, directly binds to Factin via a region N-terminal to the FH1 domain and forms a homotypic complex via the FH2 domain to promote actin fiber formation
    • Takeya, R. and Sumimoto, H. (2003). Fhos, a mammalian formin, directly binds to Factin via a region N-terminal to the FH1 domain and forms a homotypic complex via the FH2 domain to promote actin fiber formation. J. Cell Sci. 116, 4567-4575.
    • (2003) J. Cell Sci. , vol.116 , pp. 4567-4575
    • Takeya, R.1    Sumimoto, H.2
  • 40
    • 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. and Sumimoto, H. (2008). The mammalian formin FHOD1 is activated through phosphorylation by ROCK and mediates thrombin-induced stress fibre formation in endothelial cells. EMBO J. 27, 618-628.
    • (2008) EMBO J. , vol.27 , pp. 618-628
    • Takeya, R.1    Taniguchi, K.2    Narumiya, S.3    Sumimoto, H.4
  • 44
    • 84870875953 scopus 로고    scopus 로고
    • Structure of the formin-interaction domain of the actin nucleation-promoting factor Bud6
    • USA
    • Tu, D., Graziano, B. R., Park, E., Zheng, W., Li, Y., Goode, B. L. and Eck, M. J. (2012). Structure of the formin-interaction domain of the actin nucleation-promoting factor Bud6. Proc. Natl. Acad. Sci. USA 109, E3424-E3433.
    • (2012) Proc. Natl. Acad. Sci. , vol.109
    • Tu, D.1    Graziano, B.R.2    Park, E.3    Zheng, W.4    Li, Y.5    Goode, B.L.6    Eck, M.J.7
  • 45
    • 0037039770 scopus 로고    scopus 로고
    • Single-molecule speckle analysis of actin filament turnover in lamellipodia
    • Watanabe, N. and Mitchison, T. J. (2002). Single-molecule speckle analysis of actin filament turnover in lamellipodia. Science 295, 1083-1086.
    • (2002) Science , vol.295 , pp. 1083-1086
    • Watanabe, N.1    Mitchison, T.J.2
  • 46
    • 0033160196 scopus 로고    scopus 로고
    • Cooperation between mDia1 and ROCK in Rho-induced actin reorganization
    • Watanabe, N., Kato, T., Fujita, A., Ishizaki, T. and Narumiya, S. (1999). Cooperation between mDia1 and ROCK in Rho-induced actin reorganization. Nat. Cell Biol. 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
  • 47
    • 0035824618 scopus 로고    scopus 로고
    • The formin/diaphanous-related protein, FHOS, interacts with Rac1 and activates transcription from the serum response element
    • Westendorf, J. J. (2001). The formin/diaphanous-related protein, FHOS, interacts with Rac1 and activates transcription from the serum response element. J. Biol. Chem. 276, 46453-46459.
    • (2001) J. Biol. Chem. , vol.276 , pp. 46453-46459
    • Westendorf, J.J.1
  • 48
    • 0035040645 scopus 로고    scopus 로고
    • Rho and Rac but not Cdc42 regulate endothelial cell permeability
    • Wójciak-Stothard, B., Potempa, S., Eichholtz, T. and Ridley, A. J. (2001). Rho and Rac but not Cdc42 regulate endothelial cell permeability. J. Cell Sci. 114, 1343-1355.
    • (2001) J. Cell Sci. , vol.114 , pp. 1343-1355
    • Wójciak-Stothard, B.1    Potempa, S.2    Eichholtz, T.3    Ridley, A.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.