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0041758426
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The formins: Active scaffolds that remodel the cytoskeleton
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A recent review that summarizes information on formin structure.
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Wallar B.J., Alberts A.S. The formins: active scaffolds that remodel the cytoskeleton. Trends Cell Biol. 13:2003;435-466 A recent review that summarizes information on formin structure.
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Wallar, B.J.1
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Watanabe N., Kato T., Fujita A., Ishizaki T., Narumiya S. Cooperation between mDia1 and Rock in Rho-induced actin reorganization. Nat Cell Biol. 1:1999;136-143.
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Genetic dissection of the budding yeast Arp2/3 complex: A comparison of the in vivo and structural roles of individual subunits
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Winter D.C., Choe E.Y., Li R. Genetic dissection of the budding yeast Arp2/3 complex: a comparison of the in vivo and structural roles of individual subunits. Proc Natl Acad Sci USA. 96:1999;7288-7293.
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Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast
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Evangelista M., Pruyne D., Amberg D.C., Boone C., Bretscher A. Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast. Nat Cell Biol. 4:2002;32-41.
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Yeast formins regulate cell polarity by controlling the assembly of actin cables
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Sagot I., Klee S., Pellman D. Yeast formins regulate cell polarity by controlling the assembly of actin cables. Nat Cell Biol. 4:2002;42-50.
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Role of formins in actin assembly: Nucleation and barbed-end association
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This work demonstrates that a fragment of Bni1p containing the FH1 and FH2 domains can nucleate actin filaments. It also demonstrates that this fragment binds to the barbed end of the filament.
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Pruyne D., Evangelista M., Yang C., Bi E., Zigmond S., Bretscher A., Boone C. Role of formins in actin assembly: nucleation and barbed-end association. Science. 297:2002;612-615 This work demonstrates that a fragment of Bni1p containing the FH1 and FH2 domains can nucleate actin filaments. It also demonstrates that this fragment binds to the barbed end of the filament.
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Science
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Pruyne, D.1
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An actin nucleation mechanism mediated by Bni1 and profilin
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The paper demonstrates nucleation by fragments of Bni1p containing FH1and FH2 domains and shows that profilin-actin can contribute to the nucleation via the polyproline region of profilin binding to the FH1 domain.
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Sagot I., Rodal A.A., Moseley J., Goode B.L., Pellman D. An actin nucleation mechanism mediated by Bni1 and profilin. Nat Cell Biol. 4:2002;626-631 The paper demonstrates nucleation by fragments of Bni1p containing FH1and FH2 domains and shows that profilin-actin can contribute to the nucleation via the polyproline region of profilin binding to the FH1 domain.
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Sagot, I.1
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0037780973
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The fission yeast cytokinesis formin Cdc12p is a barbed end actin filament capping protein gated by profilin
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In fission yeast, the formin Cdc12 is shown to nucleate actin filaments that are tightly capped at their barbed end by Cdc12. Interestingly, the presence of profilin-actin (and the FH1 domain of Cdc12) removes the inhibition of both barbed-end elongation and depolymerization. Cdc12 still inhibits annealing, suggesting that it remains at the barbed end. Thus, in the presence of profilin-actin, Cdc12 changes from being a very tight to a very leaky cap.
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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. 161:2003;875-887 In fission yeast, the formin Cdc12 is shown to nucleate actin filaments that are tightly capped at their barbed end by Cdc12. Interestingly, the presence of profilin-actin (and the FH1 domain of Cdc12) removes the inhibition of both barbed-end elongation and depolymerization. Cdc12 still inhibits annealing, suggesting that it remains at the barbed end. Thus, in the presence of profilin-actin, Cdc12 changes from being a very tight to a very leaky cap.
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Kovar, D.R.1
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The mouse formin, mDia1, is a potent actin nucleation factor regulated by auto-inhibition
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This paper demonstrates potent actin nucleation by the mammalian formin Diaphanous 1 and shows that the nucleation is regulated by Rho binding to the N terminus. Interestingly, GTP-Rho does not cause complete relief of auto-inhibition for mDia1 in vitro, suggesting that additional activators might be required for full activation. The paper nicely documents the actin dependence of nucleation and the contribution of profilin-actin to nucleation when the FH1 domain is present.
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Li F., Higgs H.N. The mouse formin, mDia1, is a potent actin nucleation factor regulated by auto-inhibition. Curr Biol. 13:2003;1335-1340 This paper demonstrates potent actin nucleation by the mammalian formin Diaphanous 1 and shows that the nucleation is regulated by Rho binding to the N terminus. Interestingly, GTP-Rho does not cause complete relief of auto-inhibition for mDia1 in vitro, suggesting that additional activators might be required for full activation. The paper nicely documents the actin dependence of nucleation and the contribution of profilin-actin to nucleation when the FH1 domain is present.
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Li, F.1
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A recent review of existing literature on formin structure and function.
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Evangelista M., Zigmond S., Boone C. Formins: effectors for assembly and polarization of actin filaments. J Cell Sci. 116:2003;2603-2611 A recent review of existing literature on formin structure and function.
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Zeller R., Haramis A.G., Zuniga A., McGuigan C., Dono R., Davidson G., Chabanis S., Gibson T. Formin defines a large family of morphoregulatory genes and functions in establishment of the polarizing region. Cell Tissue Res. 296:1999;85-93.
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13
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Formin leaky cap allows elongation in the presence of capping proteins
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A demonstration that Bni1p competes with capping protein for the filament barbed end. The paper includes an animation of Bni1p functioning as a processive barbed-end cap.
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Zigmond S.H., Evangelista M., Boone C., Yang C., Dar A.C., Sicheri F., Forkey J., Pring M. Formin leaky cap allows elongation in the presence of capping proteins. Curr Biol. 13:2003;1820-1823 A demonstration that Bni1p competes with capping protein for the filament barbed end. The paper includes an animation of Bni1p functioning as a processive barbed-end cap.
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Zigmond, S.H.1
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RhoD regulates endosome dynamics through Diaphanous-related formin and src tyrosine kinase
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The paper demonstrates a role for formins in endosome movement.
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Gasman S., Kalaidzidis Y., Zerial M. RhoD regulates endosome dynamics through Diaphanous-related formin and src tyrosine kinase. Nat Cell Biol. 5:2003;195-204 The paper demonstrates a role for formins in endosome movement.
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Gasman, S.1
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Diaphanous-related formins bridge rho GTPase and Src tyrosine kinase signaling
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Tominaga T., Sahai E., Chardin P., McCormick F., Courtneidge S.A., Alberts A.S. Diaphanous-related formins bridge rho GTPase and Src tyrosine kinase signaling. Mol Cell. 5:2000;13-25.
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Wnt/Frizzled activation of Rho regulates vertebrate gastrulation and requires a novel Formin homology preotine DAAM1
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Habas R., Kato Y., He X. Wnt/Frizzled activation of Rho regulates vertebrate gastrulation and requires a novel Formin homology preotine DAAM1. Cell. 107:2001;843-854.
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Fujiwara T., Mammoto A., Kim Y., Takai Y. Rho small G-protein-dependent binding of mDia to a Src homology 3 domain-containing IRSp53/BAIAP2. Biochem Biophys Res Commun. 271:2000;626-629.
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Alberts A.S. Identification of a carboxyl-terminal Diaphanous-related formin homology protein autoreguatory domain. J Biol Chem. 276:2001;2824-2830.
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GTPase signalling: New functions for Diaphanous-related formins
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A discussion of papers showing RhoD binding to hDia2C and Cdc42 to mDia2.
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Olson M.F. GTPase signalling: new functions for Diaphanous-related formins. Curr Biol. 13:2003;R360-R362 A discussion of papers showing RhoD binding to hDia2C and Cdc42 to mDia2.
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Olson, M.F.1
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Formin-dependent actin assembly is regulated by distinct modes of Rho signaling in yeast
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The paper examines the regulation of Bni1p and Bnr1p by Rho family GTPases. The essential function of Rho3p and Rho4p is formin activation; Cdc42 is not required for formin-induced actin cable assembly but contributes to the organization of cable assembly during bud initiation.
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Dong Y., Pruyne D., Bretscher A. Formin-dependent actin assembly is regulated by distinct modes of Rho signaling in yeast. J Cell Biol. 161:2003;1081-1092 The paper examines the regulation of Bni1p and Bnr1p by Rho family GTPases. The essential function of Rho3p and Rho4p is formin activation; Cdc42 is not required for formin-induced actin cable assembly but contributes to the organization of cable assembly during bud initiation.
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Disruption of the Diaphanous-related formin Drf1 gene encoding mDia1 reveals a role for Drf3 as an effector for Cdc42
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The paper marks the beginning of genetic studies of formin function in mammalian cells. It shows that disruption of one formin, mDia1, reveals a new role for another formin, Drf3.
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Peng J., Wallar B.J., Flanders A., Swiatek P.J., Alberts A.S. Disruption of the Diaphanous-related formin Drf1 gene encoding mDia1 reveals a role for Drf3 as an effector for Cdc42. Curr Biol. 13:2003;534-545 The paper marks the beginning of genetic studies of formin function in mammalian cells. It shows that disruption of one formin, mDia1, reveals a new role for another formin, Drf3.
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Activation of the Rac binding partner formin homology 2 domain containing 1 induces actin stress fibers via a ROCK-dependent mechanism
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Gasteier J.E., Madrid R., Krautkramer E., Schroder S., Muranyi W., Benichou S., Fackler O.T. Activation of the Rac binding partner formin homology 2 domain containing 1 induces actin stress fibers via a ROCK-dependent mechanism. J Biol Chem. 278:2003;38902-38902.
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The small GTPase Rho3 and diaphanous/formin For3 function in polarized cell growth in fission yeast
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Nakano K., Imai J., Arai R., Toh-E A., Matsui Y., Mabuchi I. The small GTPase Rho3 and diaphanous/formin For3 function in polarized cell growth in fission yeast. J Cell Sci. 115:2002;4629-4639.
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Delphilin: A novel PDZ and formin homology domain-containing protein that synapically colocalizes and interacts with glutamate receptor δ2 subunit
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Miyagi Y., Yamashita T., Fukaya M., Sonoda T., Okuno T., Yamada K., Watanabe M., Nagashima Y., Aoki I., Okuda K., Mishina M., Kawamoto S. Delphilin: a novel PDZ and formin homology domain-containing protein that synapically colocalizes and interacts with glutamate receptor δ2 subunit. J Neurosci. 22:2002;803-814.
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Deeks M.J., Hussey P.J., Davies B. Formins: intermediates in signal-transduction cascades that affect cytoskeletal reorganization. Trends Plant Sci. 7:2002;492-498.
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A formin homology protein and profilin are required for cytokinesis and Arp2/3-independent assembly of cortical microfilaments in C. elegans
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Severson A.F., Baillie D.L., Bowerman B. A formin homology protein and profilin are required for cytokinesis and Arp2/3-independent assembly of cortical microfilaments in C. elegans. Curr Biol. 12:2002;2066-2075.
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Pellam R.J., Chang F. Actin dynamics in the contractile ring during cytokinesis in fission yeast. Nature. 419:2002;82-86.
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Tolliday N., VerPlank L., Li R. Rho1 directs formin-mediated actin ring assembly during budding yeast cytokinesis. Curr Biol. 12:2002;R813-R814.
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Focal contacts as mechanosensors: Externally applied local mechanical force induces growth of focal contacts by an mDIA1-dependent and ROCK-independent mechanism
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Riveline D., Zamir E., Balaban N.Q., Schwarz U.S., Ishizaki T., Narumiya S., Kam Z., Geiger B., Bershadsky A.D. Focal contacts as mechanosensors: externally applied local mechanical force induces growth of focal contacts by an mDIA1-dependent and ROCK-independent mechanism. J Cell Biol. 153:2001;1175-1186.
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FRL, a novel formin-related protein, binds to Rac and regulates cell motility and survival of macrophages
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The paper presents data indicating that the mechanism of nucleation by FH2-containing fragments of Bni1p involves dimer stabilization. It further shows that profilin-actin can contribute to nucleation if the FH1 domain of Bni1p is present.
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