메뉴 건너뛰기




Volumn 92, Issue 6-7, 2013, Pages 201-212

ForC lacks canonical formin activity but bundles actin filaments and is required for multicellular development of Dictyostelium cells

Author keywords

Actin bundles; Cell migration; Chemotaxis; Development; Dictyostelium; Formin; Morphogenesis; Phototaxis; Spore formation

Indexed keywords

CYCLIC AMP; F ACTIN; FORMIN C; PROTEIN; UNCLASSIFIED DRUG;

EID: 84883255526     PISSN: 01719335     EISSN: 16181298     Source Type: Journal    
DOI: 10.1016/j.ejcb.2013.07.001     Document Type: Article
Times cited : (8)

References (50)
  • 2
    • 0021884258 scopus 로고
    • Carbohydrate and other epitopes of the contact site A glycoprotein of Dictyostelium discoideum as characterized by monoclonal antibodies
    • Bertholdt G., Stadler J., Bozzaro S., Fichtner B., Gerisch G. Carbohydrate and other epitopes of the contact site A glycoprotein of Dictyostelium discoideum as characterized by monoclonal antibodies. Cell Differ. 1985, 16:187-202.
    • (1985) Cell Differ. , vol.16 , pp. 187-202
    • Bertholdt, G.1    Stadler, J.2    Bozzaro, S.3    Fichtner, B.4    Gerisch, G.5
  • 6
    • 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., Nurse P. Cdc12p, a protein required for cytokinesis in fission yeast, is a component of the cell division ring and interacts with profilin. J. Cell Biol. 1997, 137:169-182.
    • (1997) J. Cell Biol. , vol.137 , pp. 169-182
    • Chang, F.1    Drubin, D.2    Nurse, P.3
  • 7
    • 72949110575 scopus 로고    scopus 로고
    • Unleashing formins to remodel the actin and microtubule cytoskeletons
    • Chesarone M.A., DuPage A.G., Goode B.L. Unleashing formins to remodel the actin and microtubule cytoskeletons. Nat. Rev. Mol. Cell Biol. 2010, 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
  • 8
    • 34848927902 scopus 로고    scopus 로고
    • The many faces of actin: matching assembly factors with cellular structures
    • Chhabra E.S., Higgs H.N. The many faces of actin: matching assembly factors with cellular structures. Nat. Cell Biol. 2007, 9:1110-1121.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 1110-1121
    • Chhabra, E.S.1    Higgs, H.N.2
  • 9
    • 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., Geyer M. Structure, dynamics, lipid binding, and physiological relevance of the putative GTPase-binding domain of Dictyostelium formin C. J. Biol. Chem. 2011, 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
  • 10
    • 0024803255 scopus 로고
    • Optimization and in situ detection of Escherichia coli beta-galactosidase gene expression in Dictyostelium discoideum
    • Dingermann T., Reindl N., Werner H., Hildebrandt M., Nellen W., Harwood A., Williams J., Nerke K. Optimization and in situ detection of Escherichia coli beta-galactosidase gene expression in Dictyostelium discoideum. Gene 1989, 85:353-362.
    • (1989) Gene , vol.85 , pp. 353-362
    • Dingermann, T.1    Reindl, N.2    Werner, H.3    Hildebrandt, M.4    Nellen, W.5    Harwood, A.6    Williams, J.7    Nerke, K.8
  • 12
    • 0030574044 scopus 로고    scopus 로고
    • DGAP1, a homologue of rasGTPase activating proteins that controls growth, cytokinesis, and development in Dictyostelium discoideum
    • Faix J., Dittrich W. DGAP1, a homologue of rasGTPase activating proteins that controls growth, cytokinesis, and development in Dictyostelium discoideum. FEBS Lett. 1996, 394:251-257.
    • (1996) FEBS Lett. , vol.394 , pp. 251-257
    • Faix, J.1    Dittrich, W.2
  • 13
    • 33646864565 scopus 로고    scopus 로고
    • Staying in shape with formins
    • Faix J., Grosse R. Staying in shape with formins. Dev. Cell 2006, 10:693-706.
    • (2006) Dev. Cell , vol.10 , pp. 693-706
    • Faix, J.1    Grosse, R.2
  • 14
    • 0026650509 scopus 로고
    • Overexpression of the csA cell adhesion molecule under its own cAMP-regulated promoter impairs morphogenesis in Dictyostelium
    • Faix J., Gerisch G., Noegel A.A. Overexpression of the csA cell adhesion molecule under its own cAMP-regulated promoter impairs morphogenesis in Dictyostelium. J. Cell Sci. 1992, 102:203-214.
    • (1992) J. Cell Sci. , vol.102 , pp. 203-214
    • Faix, J.1    Gerisch, G.2    Noegel, A.A.3
  • 16
    • 0031149989 scopus 로고    scopus 로고
    • Genetics of phototaxis in a model eukaryote, Dictyostelium discoideum
    • Fisher P.R. Genetics of phototaxis in a model eukaryote, Dictyostelium discoideum. Bioessays 1997, 19:397-407.
    • (1997) Bioessays , vol.19 , pp. 397-407
    • Fisher, P.R.1
  • 17
    • 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
  • 18
    • 0343092090 scopus 로고    scopus 로고
    • Dictyostelium DdCP224 is a microtubule-associated protein and a permanent centrosomal resident involved in centrosome duplication
    • Gräf R., Daunderer C., Schliwa M. Dictyostelium DdCP224 is a microtubule-associated protein and a permanent centrosomal resident involved in centrosome duplication. J. Cell Sci. 2000, 113:1747-1758.
    • (2000) J. Cell Sci. , vol.113 , pp. 1747-1758
    • Gräf, R.1    Daunderer, C.2    Schliwa, M.3
  • 19
    • 0020434281 scopus 로고
    • Antigenic differences detected between prespore cells of Dictyostelium discoideum and Dictyostelium mucoroides using monoclonal antibodies
    • Gregg J.H., Krefft M., Haas-Kraus A., Williams K.L. Antigenic differences detected between prespore cells of Dictyostelium discoideum and Dictyostelium mucoroides using monoclonal antibodies. Exp. Cell Res. 1982, 142:229-233.
    • (1982) Exp. Cell Res. , vol.142 , pp. 229-233
    • Gregg, J.H.1    Krefft, M.2    Haas-Kraus, A.3    Williams, K.L.4
  • 20
    • 2442473140 scopus 로고    scopus 로고
    • The mouse formin, FRLalpha, slows actin filament barbed end elongation, competes with capping protein, accelerates polymerization from monomers, and severs filaments
    • Harris E.S., Li F., Higgs H.N. The mouse formin, FRLalpha, slows actin filament barbed end elongation, competes with capping protein, accelerates polymerization from monomers, and severs filaments. J. Biol. Chem. 2004, 279:20076-20087.
    • (2004) J. Biol. Chem. , vol.279 , pp. 20076-20087
    • Harris, E.S.1    Li, F.2    Higgs, H.N.3
  • 21
    • 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., Higgs H.N. Mechanistic differences in actin bundling activity of two mammalian formins, FRL1 and mDia2. J. Biol. Chem. 2006, 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
  • 24
    • 0037442388 scopus 로고    scopus 로고
    • ForC, a novel type of formin family protein lacking an FH1 domain, is involved in multicellular development in Dictyostelium discoideum
    • Kitayama C., Uyeda T.Q. ForC, a novel type of formin family protein lacking an FH1 domain, is involved in multicellular development in Dictyostelium discoideum. J. Cell Sci. 2003, 116:711-723.
    • (2003) J. Cell Sci. , vol.116 , pp. 711-723
    • Kitayama, C.1    Uyeda, T.Q.2
  • 25
    • 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., Pollard T.D. The fission yeast cytokinesis formin Cdc12p is a barbed end actin filament capping protein gated by profilin. J. Cell Biol. 2003, 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
  • 26
    • 0022273438 scopus 로고
    • Use of a monoclonal antibody recognizing a cell surface determinant to distinguish prestalk and prespore cells of Dictyostelium discoideum slugs
    • Krefft M., Voet L., Gregg J.H., Williams K.L. Use of a monoclonal antibody recognizing a cell surface determinant to distinguish prestalk and prespore cells of Dictyostelium discoideum slugs. J. Embryol. Exp. Morphol. 1985, 88:15-24.
    • (1985) J. Embryol. Exp. Morphol. , vol.88 , pp. 15-24
    • Krefft, M.1    Voet, L.2    Gregg, J.H.3    Williams, K.L.4
  • 27
    • 84855540299 scopus 로고    scopus 로고
    • Highly effective removal of floxed Blasticidin S resistance cassettes from Dictyostelium discoideum mutants by extrachromosomal expression of Cre
    • Linkner J., Nordholz B., Junemann A., Winterhoff M., Faix J. Highly effective removal of floxed Blasticidin S resistance cassettes from Dictyostelium discoideum mutants by extrachromosomal expression of Cre. Eur. J. Cell Biol. 2012, 91:156-160.
    • (2012) Eur. J. Cell Biol. , vol.91 , pp. 156-160
    • Linkner, J.1    Nordholz, B.2    Junemann, A.3    Winterhoff, M.4    Faix, J.5
  • 28
    • 23844516160 scopus 로고    scopus 로고
    • DNG1, a Dictyostelium homologue of tumor suppressor ING1 regulates differentiation of Dictyostelium cells
    • Mayanagi T., Amagai A., Maeda Y. DNG1, a Dictyostelium homologue of tumor suppressor ING1 regulates differentiation of Dictyostelium cells. Cell. Mol. Life Sci. 2005, 62:1734-1743.
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 1734-1743
    • Mayanagi, T.1    Amagai, A.2    Maeda, Y.3
  • 29
    • 23044510466 scopus 로고    scopus 로고
    • Differential activities and regulation of Saccharomyces cerevisiae formin proteins Bni1 and Bnr1 by Bud6
    • Moseley J.B., Goode B.L. Differential activities and regulation of Saccharomyces cerevisiae formin proteins Bni1 and Bnr1 by Bud6. J. Biol. Chem. 2005, 280:28023-28033.
    • (2005) J. Biol. Chem. , vol.280 , pp. 28023-28033
    • Moseley, J.B.1    Goode, B.L.2
  • 31
    • 34247644614 scopus 로고    scopus 로고
    • Regulation of actin filament assembly by Arp2/3 complex and formins
    • Pollard T.D. Regulation of actin filament assembly by Arp2/3 complex and formins. Annu. Rev. Biophys. Biomol. Struct. 2007, 36:451-477.
    • (2007) Annu. Rev. Biophys. Biomol. Struct. , vol.36 , pp. 451-477
    • Pollard, T.D.1
  • 33
    • 0032820879 scopus 로고    scopus 로고
    • Three actin cross-linking proteins, the 34 kDa actin-bundling protein, alpha-actinin and gelation factor (ABP-120), have both unique and redundant roles in the growth and development of Dictyostelium
    • Rivero F., Furukawa R., Fechheimer M., Noegel A.A. Three actin cross-linking proteins, the 34 kDa actin-bundling protein, alpha-actinin and gelation factor (ABP-120), have both unique and redundant roles in the growth and development of Dictyostelium. J. Cell Sci. 1999, 112:2737-2751.
    • (1999) J. Cell Sci. , vol.112 , pp. 2737-2751
    • Rivero, F.1    Furukawa, R.2    Fechheimer, M.3    Noegel, A.A.4
  • 34
    • 20444381052 scopus 로고    scopus 로고
    • A comparative sequence analysis reveals a common GBD/FH3-FH1-FH2-DAD architecture in formins from Dictyostelium, fungi and metazoan
    • Rivero F., Muramoto T., Meyer A.K., Urushihara H., Uyeda T.Q., Kitayama C. A comparative sequence analysis reveals a common GBD/FH3-FH1-FH2-DAD architecture in formins from Dictyostelium, fungi and metazoan. BMC Genom. 2005, 6:28.
    • (2005) BMC Genom. , vol.6 , pp. 28
    • Rivero, F.1    Muramoto, T.2    Meyer, A.K.3    Urushihara, H.4    Uyeda, T.Q.5    Kitayama, C.6
  • 36
    • 20444426470 scopus 로고    scopus 로고
    • The Diaphanous-related formin dDia2 is required for the formation and maintenance of filopodia
    • Schirenbeck A., Bretschneider T., Arasada R., Schleicher M., Faix J. The Diaphanous-related formin dDia2 is required for the formation and maintenance of filopodia. Nat. Cell Biol. 2005, 7:619-625.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 619-625
    • Schirenbeck, A.1    Bretschneider, T.2    Arasada, R.3    Schleicher, M.4    Faix, J.5
  • 37
    • 77649273530 scopus 로고    scopus 로고
    • Fifteen formins for an actin filament: a molecular view on the regulation of human formins
    • Schönichen A., Geyer M. Fifteen formins for an actin filament: a molecular view on the regulation of human formins. Biochim. Biophys. Acta 2010, 1803:152-163.
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 152-163
    • Schönichen, A.1    Geyer, M.2
  • 39
    • 84862907778 scopus 로고    scopus 로고
    • Actin cross-linking proteins cortexillin I and II are required for cAMP signaling during Dictyostelium chemotaxis and development
    • Shu S., Liu X., Kriebel P.W., Daniels M.P., Korn E.D. Actin cross-linking proteins cortexillin I and II are required for cAMP signaling during Dictyostelium chemotaxis and development. Mol. Biol. Cell 2012, 23:390-400.
    • (2012) Mol. Biol. Cell , vol.23 , pp. 390-400
    • Shu, S.1    Liu, X.2    Kriebel, P.W.3    Daniels, M.P.4    Korn, E.D.5
  • 40
    • 0028286341 scopus 로고
    • Extracellular cAMP can restore development in Dictyostelium cells lacking one, but not two subtypes of early cAMP receptors (cARs). Evidence for involvement of cAR1 in aggregative gene expression
    • Soede R.D., Insall R.H., Devreotes P.N., Schaap P. Extracellular cAMP can restore development in Dictyostelium cells lacking one, but not two subtypes of early cAMP receptors (cARs). Evidence for involvement of cAR1 in aggregative gene expression. Development 1994, 120:1997-2002.
    • (1994) Development , vol.120 , pp. 1997-2002
    • Soede, R.D.1    Insall, R.H.2    Devreotes, P.N.3    Schaap, P.4
  • 41
    • 0025832630 scopus 로고
    • Gene targeting of the aggregation stage cAMP receptor cAR1 in Dictyostelium
    • Sun T.J., Devreotes P.N. Gene targeting of the aggregation stage cAMP receptor cAR1 in Dictyostelium. Genes Dev. 1991, 5:572-582.
    • (1991) Genes Dev. , vol.5 , pp. 572-582
    • Sun, T.J.1    Devreotes, P.N.2
  • 42
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich J.A., Watt S. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J. Biol Chem. 1971, 246:4866-4871.
    • (1971) J. Biol Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 43
    • 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
  • 44
    • 84872043614 scopus 로고    scopus 로고
    • FMNL3 FH2-actin structure gives insight into formin-mediated actin nucleation and elongation
    • Thompson M.E., Heimsath E.G., Gauvin T.J., Higgs H.N., Kull F.J. FMNL3 FH2-actin structure gives insight into formin-mediated actin nucleation and elongation. Nat. Struct. Mol. Biol. 2013, 20:111-118.
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 111-118
    • Thompson, M.E.1    Heimsath, E.G.2    Gauvin, T.J.3    Higgs, H.N.4    Kull, F.J.5
  • 46
    • 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
  • 47
    • 0030295030 scopus 로고    scopus 로고
    • Wild-type strains of Dictyostelium discoideum can be transformed using a novel selection cassette driven by the promoter of the ribosomal V18 gene
    • Wetterauer B., Morandini P., Hribar I., Murgia-Morandini I., Hamker U., Singleton C., MacWilliams H.K. Wild-type strains of Dictyostelium discoideum can be transformed using a novel selection cassette driven by the promoter of the ribosomal V18 gene. Plasmid 1996, 36:169-181.
    • (1996) Plasmid , vol.36 , pp. 169-181
    • Wetterauer, B.1    Morandini, P.2    Hribar, I.3    Murgia-Morandini, I.4    Hamker, U.5    Singleton, C.6    MacWilliams, H.K.7
  • 48
    • 78349285170 scopus 로고    scopus 로고
    • Dictyostelium finds new roles to model
    • Williams J.G. Dictyostelium finds new roles to model. Genetics 2010, 185:717-726.
    • (2010) Genetics , vol.185 , pp. 717-726
    • Williams, J.G.1
  • 49
    • 0026593102 scopus 로고
    • Redundancy in the microfilament system: abnormal development of Dictyostelium cells lacking two F-actin cross-linking proteins
    • Witke W., Schleicher M., Noegel A.A. Redundancy in the microfilament system: abnormal development of Dictyostelium cells lacking two F-actin cross-linking proteins. Cell 1992, 68:53-62.
    • (1992) Cell , vol.68 , pp. 53-62
    • Witke, W.1    Schleicher, M.2    Noegel, A.A.3
  • 50
    • 1542269073 scopus 로고    scopus 로고
    • Crystal structures of a formin homology-2 domain reveal a tethered dimer architecture
    • Xu Y., Moseley J.B., Sagot I., Poy F., Pellman D., Goode B.L., Eck M.J. Crystal structures of a formin homology-2 domain reveal a tethered dimer architecture. Cell 2004, 116:711-723.
    • (2004) Cell , vol.116 , pp. 711-723
    • Xu, Y.1    Moseley, J.B.2    Sagot, I.3    Poy, F.4    Pellman, D.5    Goode, B.L.6    Eck, M.J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.