메뉴 건너뛰기




Volumn 16, Issue 1, 2005, Pages 1-13

Phylogenetic analysis of the formin homology 2 domain

Author keywords

[No Author keywords available]

Indexed keywords

ISOPROTEIN; METHENAMINE;

EID: 11144281883     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E04-07-0565     Document Type: Review
Times cited : (215)

References (35)
  • 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
  • 4
    • 0028053435 scopus 로고
    • Diaphanous is required for cytokinesis in Drosophila and shares domains of similarity with the products of the limb deformity gene
    • Castrillon, D. H., and Wasserman, S. A. (1994). Diaphanous is required for cytokinesis in Drosophila and shares domains of similarity with the products of the limb deformity gene. Development 120, 3367-3377.
    • (1994) Development , vol.120 , pp. 3367-3377
    • Castrillon, D.H.1    Wasserman, S.A.2
  • 5
    • 2342450579 scopus 로고    scopus 로고
    • Systematic searches for molecular synapomorphies in model metazoan genomes give some support for Ecdysozoa after accounting for the idiosyncrasies of Caenorhabditis elegans
    • Copley, R. R., Aloy, P., Russell, R. B., and Telford, M. J. (2004). Systematic searches for molecular synapomorphies in model metazoan genomes give some support for Ecdysozoa after accounting for the idiosyncrasies of Caenorhabditis elegans. Evol. Dev. 6, 164-169.
    • (2004) Evol. Dev. , vol.6 , pp. 164-169
    • Copley, R.R.1    Aloy, P.2    Russell, R.B.3    Telford, M.J.4
  • 6
    • 9444255105 scopus 로고    scopus 로고
    • Formin homology 2 domains occur in mulitple contexts in angiosperms
    • Cvrckova, F., Novotny, M., Pickova, D., and Zarsky, V. (2004). Formin homology 2 domains occur in mulitple contexts in angiosperms. B.M. C. Genomics 5, 44.
    • (2004) B.M. C. Genomics , vol.5 , pp. 44
    • Cvrckova, F.1    Novotny, M.2    Pickova, D.3    Zarsky, V.4
  • 7
    • 0004034745 scopus 로고
    • John Murray (republished by Harvard University Press): London
    • Darwin, C. (1859). On the Origin of Species. John Murray (republished by Harvard University Press, 1964): London.
    • (1859) On the Origin of Species
    • Darwin, C.1
  • 8
    • 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
  • 10
    • 0036629334 scopus 로고    scopus 로고
    • Molecular evolution of the actin family
    • Goodson, H. V., and Hawse, W. F. (2002). Molecular evolution of the actin family. J. Cell Sci. 115, 2619-2622.
    • (2002) J. Cell Sci. , vol.115 , pp. 2619-2622
    • Goodson, H.V.1    Hawse, W.F.2
  • 11
    • 2442473140 scopus 로고    scopus 로고
    • The mouse formin, FRLa, slows actin filament barbed end elongation, competes with capping protein, accelerates polymerization from monomers, and severs filaments
    • Harris, E. S., Li, F., and Higgs, H. N. (2004). The mouse formin, FRLa, slows actin filament barbed end elongation, competes with capping protein, accelerates polymerization from monomers, and severs filaments. J. Biol. Chem. 279, 20076-20087.
    • (2004) J. Biol. Chem. , vol.279 , pp. 20076-20087
    • Harris, E.S.1    Li, F.2    Higgs, H.N.3
  • 12
    • 0036846746 scopus 로고    scopus 로고
    • The origin and evolution of model organisms
    • Hedges, S. B. (2002). The origin and evolution of model organisms. Nat. Rev. Genet. 3, 838-849.
    • (2002) Nat. Rev. Genet. , vol.3 , pp. 838-849
    • Hedges, S.B.1
  • 13
    • 0033766762 scopus 로고    scopus 로고
    • A myosin family tree
    • Hodge, T., and Cope, J.T.V. (2000). A myosin family tree. J. Cell Sci. 113, 3353-3354.
    • (2000) J. Cell Sci. , vol.113 , pp. 3353-3354
    • Hodge, T.1    Cope, J.T.V.2
  • 14
    • 0037780973 scopus 로고    scopus 로고
    • The fission yeast cytokinesis formin Cdc12p is a barbed end actin filament capping protein gated by profilin
    • Kovar, D. R., Kuhn, J. R., Tichy, A. L., and Pollard, T. D. (2003). The fission yeast cytokinesis formin Cdc12p is a barbed end actin filament capping protein gated by profilin. J. Cell Biol. 161, 875-887.
    • (2003) J. Cell Biol. , vol.161 , pp. 875-887
    • Kovar, D.R.1    Kuhn, J.R.2    Tichy, A.L.3    Pollard, T.D.4
  • 15
    • 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
  • 16
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas, Van Dyke, M., and Stock, J. (1991). Predicting coiled coils from protein sequences. Science 252, 1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas1    Van Dyke, M.2    Stock, J.3
  • 17
    • 0036469912 scopus 로고    scopus 로고
    • Delphilin: A novel PDZ and formin homology domain-containing protein that synaptically colocalizes and interacts with glutamate receptor d2 subunit
    • Miyagi, Y., et al. (2002). Delphilin: a novel PDZ and formin homology domain-containing protein that synaptically colocalizes and interacts with glutamate receptor d2 subunit. J. Neurosci. 22, 803-814.
    • (2002) J. Neurosci. , vol.22 , pp. 803-814
    • Miyagi, Y.1
  • 18
    • 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
  • 19
    • 0030458552 scopus 로고    scopus 로고
    • Phylogenetic analysis in molecular evolutionary genetics
    • Nei, M. (1996). Phylogenetic analysis in molecular evolutionary genetics. Annu. Rev. Genet. 30, 371-403.
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 371-403
    • Nei, M.1
  • 21
    • 0032101410 scopus 로고    scopus 로고
    • FH3, a domain found in formins, targets the fission yeast formin Fus1 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 Fus1 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
  • 22
  • 24
    • 0034677906 scopus 로고    scopus 로고
    • Myosins: A diverse superfamily
    • Sellers, J. R. (2000). Myosins: a diverse superfamily. Biochim. Biophys. Acta 1496, 3-22.
    • (2000) Biochim. Biophys. Acta , vol.1496 , pp. 3-22
    • Sellers, J.R.1
  • 25
    • 1542285173 scopus 로고    scopus 로고
    • The core FH2 domain of the Diaphanous-related formins is an elongated actin binding protein that inhibits polymerization
    • Shimada, A., Nyitrai, M., Vetter, I. R., Kuhlmann, D., Bugyi, B., Narumiya, S., Geeves, M. A., and Wittinghofer, A. (2004). The core FH2 domain of the Diaphanous-related formins is an elongated actin binding protein that inhibits polymerization. Mol. Cell 13, 511-522.
    • (2004) Mol. Cell , vol.13 , pp. 511-522
    • Shimada, A.1    Nyitrai, M.2    Vetter, I.R.3    Kuhlmann, D.4    Bugyi, B.5    Narumiya, S.6    Geeves, M.A.7    Wittinghofer, A.8
  • 28
    • 0041758426 scopus 로고    scopus 로고
    • The formins: Active scaffolds that remodel the cytoskeleton
    • Wallar, B. J., and Alberts, A. S. (2003). The formins: active scaffolds that remodel the cytoskeleton. Trends Cell Biol. 13, 435-446.
    • (2003) Trends Cell Biol. , vol.13 , pp. 435-446
    • Wallar, B.J.1    Alberts, A.S.2
  • 29
    • 0032031388 scopus 로고    scopus 로고
    • FH proteins as cytoskeletal organizers
    • Wasserman, S. (1998). FH proteins as cytoskeletal organizers. Trends Cell Biol. 8, 111-115.
    • (1998) Trends Cell Biol. , vol.8 , pp. 111-115
    • Wasserman, S.1
  • 30
    • 0035824618 scopus 로고    scopus 로고
    • The dormin/diaphanous-related protein, FHOS, interacts with Rac1 and activates transcription from the serum response element
    • Westendorf, J. J. (2001). The dormin/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
  • 31
    • 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
  • 32
    • 0025007616 scopus 로고
    • 'Formins': Proteins deduced from the alternative transcripts of the limb deformity gene
    • Woychik, R. P., Maas, R. L., Zeller, R., 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    Leder, P.4
  • 33
    • 1542269073 scopus 로고    scopus 로고
    • Crystal structures of a formin homology-2 domain reveal a tethered dimer architecture
    • Xu, Y., Moseley, J., Sagot, I., Poy, F., Pellman, D., Goode, B. L., and Eck, M. J. (2004). Crystal Structures of a formin homology-2 domain reveal a tethered dimer architecture. Cell 116, 711-723.
    • (2004) Cell , vol.116 , pp. 711-723
    • Xu, Y.1    Moseley, J.2    Sagot, I.3    Poy, F.4    Pellman, D.5    Goode, B.L.6    Eck, M.J.7
  • 34
    • 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
  • 35
    • 1642391823 scopus 로고    scopus 로고
    • Formin-induced nucleation of actin filaments
    • Zigmond, S. H. (2004). Formin-induced nucleation of actin filaments. Curr. Opin. Cell Biol. 16, 99-105.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 99-105
    • Zigmond, S.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.