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Volumn 116, Issue 22, 2003, Pages 4567-4575

Fhos, a mammalian formin, directly binds to F-actin via a region N-terminal to the FH1 domain and forms a homotypic complex via the FH2 domain to promote actin fiber formation

Author keywords

Actin; Diaphanous proteins; Fhos; Formin proteins; Rac; Stress fiber

Indexed keywords

ACTIN; CELL PROTEIN; F ACTIN; PROTEIN FHOS; UNCLASSIFIED DRUG;

EID: 0345328684     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.00769     Document Type: Article
Times cited : (50)

References (42)
  • 1
    • 0034105436 scopus 로고    scopus 로고
    • Functional analysis of the Drosophila diaphanous FH protein in early embryonic development
    • Afshar, K., Stuart, B. and Wasserman, S. A. (2000). Functional analysis of the Drosophila diaphanous FH protein in early embryonic development. Development 127, 1887-1897.
    • (2000) Development , vol.127 , pp. 1887-1897
    • Afshar, K.1    Stuart, B.2    Wasserman, S.A.3
  • 3
    • 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
  • 4
    • 0034687247 scopus 로고    scopus 로고
    • Cellular regulation of actin network assembly
    • Amann, K. J. and Pollard, T. D. (2000). Cellular regulation of actin network assembly. Curr. Biol. 10, R728-R730.
    • (2000) Curr. Biol. , vol.10
    • Amann, K.J.1    Pollard, T.D.2
  • 5
    • 0032007313 scopus 로고    scopus 로고
    • In vivo functions of actin-binding proteins
    • Ayscough, K. R. (1998). In vivo functions of actin-binding proteins. Curr. Opin. Cell Biol. 10, 102-111.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 102-111
    • Ayscough, K.R.1
  • 6
    • 0030910308 scopus 로고    scopus 로고
    • FBP WW domains and the Ab1 SH3 domain bind to a specific class of proline-rich ligands
    • Bedford, M. T., Chan, D. C. and Leder, P. (1997). FBP WW domains and the Ab1 SH3 domain bind to a specific class of proline-rich ligands. EMBO J. 16, 2376-2383.
    • (1997) EMBO J. , vol.16 , pp. 2376-2383
    • Bedford, M.T.1    Chan, D.C.2    Leder, P.3
  • 7
    • 0021691325 scopus 로고
    • Isolation and some properties of macrophage alpha-actinin: Evidence that it is not an actin gelling protein
    • Bennett, J. P., Zaner, K. S. and Stossel, T. P. (1984). Isolation and some properties of macrophage alpha-actinin: evidence that it is not an actin gelling protein. Biochemistry 23, 5081-5086.
    • (1984) Biochemistry , vol.23 , pp. 5081-5086
    • Bennett, J.P.1    Zaner, K.S.2    Stossel, T.P.3
  • 8
    • 0029981652 scopus 로고    scopus 로고
    • Formin binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains
    • Chan, D. C., Bedford, M. T. and Leder, P. (1996). Formin binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains. EMBO J. 15, 1045-1054.
    • (1996) EMBO J. , vol.15 , pp. 1045-1054
    • Chan, D.C.1    Bedford, M.T.2    Leder, P.3
  • 9
    • 0030958087 scopus 로고    scopus 로고
    • cdc12p, a protein required for cytokinesis in fission yeast, is a component of the cell division ring and interacts with profilin
    • Chang, F., Drubin, D. and Nurse, P. (1997). cdc12p, a protein required for cytokinesis in fission yeast, is a component of the cell division ring and interacts with profilin. J. Cell Biol. 137, 169-182.
    • (1997) J. Cell Biol. , vol.137 , pp. 169-182
    • Chang, F.1    Drubin, D.2    Nurse, P.3
  • 11
    • 0028973402 scopus 로고
    • Cappuccino, a Drosophila maternal effect gene required for polarity of the egg and embryo, is related to the vertebrate limb deformity locus
    • Emmons, S., Phan, H., Calley, J., Chen, W., James, B. and Manseau, L. (1995). Cappuccino, a Drosophila maternal effect gene required for polarity of the egg and embryo, is related to the vertebrate limb deformity locus. Genes Dev. 9, 2482-2494.
    • (1995) Genes Dev. , vol.9 , pp. 2482-2494
    • Emmons, S.1    Phan, H.2    Calley, J.3    Chen, W.4    James, B.5    Manseau, L.6
  • 13
    • 0036144567 scopus 로고    scopus 로고
    • Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast
    • Evangelista, M., Pruyne, D., Amberg, D. C., Boone, C. and Bretscher, A. (2002). Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast. Nat. Cell Biol. 4, 32-41.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 32-41
    • Evangelista, M.1    Pruyne, D.2    Amberg, D.C.3    Boone, C.4    Bretscher, A.5
  • 14
    • 0035975991 scopus 로고    scopus 로고
    • Roles of the fission yeast formin for3p in cell polarity, actin cable formation and symmetric cell division
    • Feierbach, B. and Chang, F. (2001). Roles of the fission yeast formin for3p in cell polarity, actin cable formation and symmetric cell division. Curr. Biol. 11, 1656-1665.
    • (2001) Curr. Biol. , vol.11 , pp. 1656-1665
    • Feierbach, B.1    Chang, F.2
  • 15
    • 0031194074 scopus 로고    scopus 로고
    • Actin cytoskeleton: Are FH proteins local organizers?
    • Frazier, J. A. and Field, C. M. (1997). Actin cytoskeleton: are FH proteins local organizers? Curr. Biol. 7, R414-R417.
    • (1997) Curr. Biol. , vol.7
    • Frazier, J.A.1    Field, C.M.2
  • 16
    • 0035966322 scopus 로고    scopus 로고
    • Wnt/Frizzled activation of Rho regulates vertebrate gastrulation and requires a novel Formin homology protein Daam1
    • Habas, R., Kato, Y. and He, X. (2001). Wnt/Frizzled activation of Rho regulates vertebrate gastrulation and requires a novel Formin homology protein Daam1. Cell 107, 843-854.
    • (2001) Cell , vol.107 , pp. 843-854
    • Habas, R.1    Kato, Y.2    He, X.3
  • 17
    • 0030927327 scopus 로고    scopus 로고
    • Bni1p and Bnr1p: Downstream targets of the Rho family small G-proteins which interact with protilin and regulate actin cytoskeleton in Saccharomyces cerevisiae
    • Imamura, H., Tanaka, K., Hihara, T., Umikawa, M., Kamei, T., Takahashi, K., Sasaki, T. and Takai, Y. (1997). Bni1p and Bnr1p: downstream targets of the Rho family small G-proteins which interact with protilin and regulate actin cytoskeleton in Saccharomyces cerevisiae. EMBO J. 16, 2745-2755.
    • (1997) EMBO J. , vol.16 , pp. 2745-2755
    • Imamura, H.1    Tanaka, K.2    Hihara, T.3    Umikawa, M.4    Kamei, T.5    Takahashi, K.6    Sasaki, T.7    Takai, Y.8
  • 18
    • 0030615004 scopus 로고    scopus 로고
    • p160ROCK, a Rho-associated coiled-coil forming protein kinase, works downstream of Rho and induces focal adhesions
    • Ishizaki, T., Naito, M., Fujisawa, K., Maekawa, M., Watanabe, N., Saito, Y. and Narumiya, S. (1997). p160ROCK, a Rho-associated coiled-coil forming protein kinase, works downstream of Rho and induces focal adhesions. FEBS Lett. 404, 118-124.
    • (1997) FEBS Lett. , vol.404 , pp. 118-124
    • Ishizaki, T.1    Naito, M.2    Fujisawa, K.3    Maekawa, M.4    Watanabe, N.5    Saito, Y.6    Narumiya, S.7
  • 20
    • 0035910054 scopus 로고    scopus 로고
    • Creating a niche in the cytoskeleton: Actin reorganization by a protein kinase
    • Janmey, P. A. (2001). Creating a niche in the cytoskeleton: Actin reorganization by a protein kinase. Proc. Natl. Acad. Sci. USA 98, 14745-14747.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14745-14747
    • Janmey, P.A.1
  • 21
    • 0032561342 scopus 로고    scopus 로고
    • Interaction of Bnr1p with a novel Src homology 3 domam-containing Hof1p. Implication in cytokinesis in Saccharomyces cerevisiae
    • Kamei, T., Tanaka, K., Hihara, T., Umikawa, M., Imamura, H., Kikyo, M., Ozaki, K. and Takai, Y. (1998). Interaction of Bnr1p with a novel Src homology 3 domam-containing Hof1p. Implication in cytokinesis in Saccharomyces cerevisiae. J. Biol. Chem. 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
  • 22
    • 0035081810 scopus 로고    scopus 로고
    • Localization of a mammalian homolog of diaphanous, mDia1, to the mitotic spindle in HeLa cells
    • Kato, T., Watanabe, N., Morishima, Y., Fujita, A., Ishizaki, T. and Narumiya, S. (2001). Localization of a mammalian homolog of diaphanous, mDia1, to the mitotic spindle in HeLa cells. J. Cell Sci. 114, 775-784.
    • (2001) J. Cell Sci. , vol.114 , pp. 775-784
    • Kato, T.1    Watanabe, N.2    Morishima, Y.3    Fujita, A.4    Ishizaki, T.5    Narumiya, S.6
  • 23
    • 0031610808 scopus 로고    scopus 로고
    • F-actin blot overlays
    • Luna, E. J. (1998). F-actin blot overlays. Methods Enzymol. 298, 32-42.
    • (1998) Methods Enzymol. , vol.298 , pp. 32-42
    • Luna, E.J.1
  • 24
    • 0030908297 scopus 로고    scopus 로고
    • The I/LWEQ module: A conserved sequence that signifies F-actin binding in functionally diverse proteins from yeast to mammals
    • McCann, R. O. and Craig, S. W. (1997). The I/LWEQ module: a conserved sequence that signifies F-actin binding in functionally diverse proteins from yeast to mammals. Proc. Natl. Acad. Sci. USA 94, 5679-5684.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5679-5684
    • McCann, R.O.1    Craig, S.W.2
  • 25
    • 0032784388 scopus 로고    scopus 로고
    • Distinct actions and cooperative roles of ROCK and mDia in Rho small G protein-induced reorganization of the actin cytoskeleton in Madin-Darby canine kidney cells
    • Nakano, K., Takaishi, K., Kodama, A., Mammoto, A., Shiozaki, H., Monden, M. and Takai, Y. (1999). Distinct actions and cooperative roles of ROCK and mDia in Rho small G protein-induced reorganization of the actin cytoskeleton in Madin-Darby canine kidney cells. Mol. Biol. Cell 10, 2481-2491.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2481-2491
    • Nakano, K.1    Takaishi, K.2    Kodama, A.3    Mammoto, A.4    Shiozaki, H.5    Monden, M.6    Takai, Y.7
  • 26
    • 0035070099 scopus 로고    scopus 로고
    • Human homologues of the Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C
    • Noda, Y., Takeya, R., Ohno, S., Naito, S., Ito, T. and Sumimoto, H. (2001) Human homologues of the Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C. Genes Cells 6, 107-119.
    • (2001) Genes Cells , vol.6 , pp. 107-119
    • Noda, Y.1    Takeya, R.2    Ohno, S.3    Naito, S.4    Ito, T.5    Sumimoto, H.6
  • 27
    • 0037026486 scopus 로고    scopus 로고
    • Actin dynamics in the contractile ring during cytokinesis in fission yeast
    • Pelham, R. J. and Chang, E. (2002). Actin dynamics in the contractile ring during cytokinesis in fission yeast. Nature 419, 82-86.
    • (2002) Nature , vol.419 , pp. 82-86
    • Pelham, R.J.1    Chang, E.2
  • 28
    • 0032101410 scopus 로고    scopus 로고
    • FH3, a domain found in formins, targets the fission yeast formin Fus 1 to the projection tip during conjugation
    • Petersen, J., Nielsen, O., Egel, R. and Hagan, I. M. (1998). FH3, a domain found in formins, targets the fission yeast formin Fus 1 to the projection tip during conjugation. J. Cell Biol. 141, 1217-1228.
    • (1998) J. Cell Biol. , vol.141 , pp. 1217-1228
    • Petersen, J.1    Nielsen, O.2    Egel, R.3    Hagan, I.M.4
  • 29
  • 30
    • 0032005974 scopus 로고    scopus 로고
    • The modular structure of actin-regulatory proteins
    • Puius, Y. A., Mahoney, N. M. and Almo, S. C. (1998). The modular structure of actin-regulatory proteins. Curr. Opin. Cell Biol. 10, 23-34.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 23-34
    • Puius, Y.A.1    Mahoney, N.M.2    Almo, S.C.3
  • 31
    • 0036141585 scopus 로고    scopus 로고
    • Yeast formins regulate cell polarity by controlling the assembly of actin cables
    • Sagot, I., Klee, S. K. and Pellman, D. (2002a). Yeast formins regulate cell polarity by controlling the assembly of actin cables. Nat. Cell Biol. 4, 42-50.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 42-50
    • Sagot, I.1    Klee, S.K.2    Pellman, D.3
  • 33
    • 0037039402 scopus 로고    scopus 로고
    • Cell polarity: Following formin function
    • Sawin, K. E. (2002). Cell polarity: following formin function. Curr. Biol. 12, R6-R8.
    • (2002) Curr. Biol. , vol.12
    • Sawin, K.E.1
  • 34
    • 0028241533 scopus 로고
    • Activation of Raf as a result of recruitment to the plasma membrane
    • Stokoe, D., Macdonald, S. G., Cadwallader, K., Symons, M. and Hancock, J. F. (1994). Activation of Raf as a result of recruitment to the plasma membrane. Science 264, 1463-1467.
    • (1994) Science , vol.264 , pp. 1463-1467
    • Stokoe, D.1    Macdonald, S.G.2    Cadwallader, K.3    Symons, M.4    Hancock, J.F.5
  • 35
    • 0034614350 scopus 로고    scopus 로고
    • Interaction of the PDZ domain of human PICK1 with class 1 ADP-ribosylation factors
    • Takeya, R., Takeshige, K. and Sumimoto, H. (2000). Interaction of the PDZ domain of human PICK1 with class 1 ADP-ribosylation factors. Biochem. Biophys. Res. Commun. 267, 149-155.
    • (2000) Biochem. Biophys. Res. Commun. , vol.267 , pp. 149-155
    • Takeya, R.1    Takeshige, K.2    Sumimoto, H.3
  • 36
  • 37
    • 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
  • 38
    • 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
  • 39
    • 0033620658 scopus 로고    scopus 로고
    • Identification and characterization of a protein containing formin homology (FH1/FH2) domains
    • Westendorf, J. J., Mernaugh, R. and Hiebert, S. W. (1999). Identification and characterization of a protein containing formin homology (FH1/FH2) domains. Gene 232, 173-182.
    • (1999) Gene , vol.232 , pp. 173-182
    • Westendorf, J.J.1    Mernaugh, R.2    Hiebert, S.W.3
  • 40
    • 0025007616 scopus 로고
    • 'Formins': Proteins deduced from the alternative transcripts of the limb deformity gene
    • Woychik, R. P., Maas, R. L., Zeller, R., Vogt, T. F. and Leder, P. (1990). 'Formins': proteins deduced from the alternative transcripts of the limb deformity gene. Nature 346, 850-853.
    • (1990) Nature , vol.346 , pp. 850-853
    • Woychik, R.P.1    Maas, R.L.2    Zeller, R.3    Vogt, T.F.4    Leder, P.5
  • 41
    • 0033816998 scopus 로고    scopus 로고
    • FRL, a novel formin-related protein, binds to Rac and regulates cell motility and survival of macrophages
    • Yayoshi-Yamamoto, S., Taniuchi, I. and Watanabe, T. (2000). FRL, a novel formin-related protein, binds to Rac and regulates cell motility and survival of macrophages. Mol. Cell. Biol. 20, 6872-6881.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6872-6881
    • Yayoshi-Yamamoto, S.1    Taniuchi, I.2    Watanabe, T.3
  • 42
    • 0032926113 scopus 로고    scopus 로고
    • Formin defines a large family of morphoregulatory genes and functions in establishment of the polarising region
    • Zeller, R., Haramis, A. G., Zuniga, A., McGuigan, C., Dono, R., Davidson, G., Chabanis, S. and Gibson, T. (1999). Formin defines a large family of morphoregulatory genes and functions in establishment of the polarising region. Cell Tissue Res. 296, 85-93.
    • (1999) Cell Tissue Res. , vol.296 , pp. 85-93
    • Zeller, R.1    Haramis, A.G.2    Zuniga, A.3    McGuigan, C.4    Dono, R.5    Davidson, G.6    Chabanis, S.7    Gibson, T.8


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