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Volumn 16, Issue 1, 2004, Pages 99-105

Formin-induced nucleation of actin filaments

Author keywords

DAD; Diaphanous autoregulatory domain; FH; Formin homology domain; GBD; GTPase binding domain; hDia; Human homologue of Drosophila Diaphanous; mDia; Mouse homologue of Drosophila Diaphanous; WASP; Wiscott Aldrich syndrome protein

Indexed keywords

ACTIN; PROTEIN; PROTEIN FORMIN; UNCLASSIFIED DRUG;

EID: 1642391823     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2003.10.019     Document Type: Review
Times cited : (212)

References (67)
  • 1
    • 0041758426 scopus 로고    scopus 로고
    • The formins: Active scaffolds that remodel the cytoskeleton
    • A recent review that summarizes information on formin structure.
    • 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.
    • (2003) Trends Cell Biol , vol.13 , pp. 435-466
    • Wallar, B.J.1    Alberts, A.S.2
  • 2
    • 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. 1:1999;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
  • 3
    • 0033594955 scopus 로고    scopus 로고
    • Genetic dissection of the budding yeast Arp2/3 complex: A comparison of the in vivo and structural roles of individual subunits
    • 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.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 7288-7293
    • Winter, D.C.1    Choe, E.Y.2    Li, R.3
  • 4
    • 0036514271 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., Bretscher A. Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast. Nat Cell Biol. 4:2002;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
  • 5
    • 0036141585 scopus 로고    scopus 로고
    • Yeast formins regulate cell polarity by controlling the assembly of actin cables
    • 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.
    • (2002) Nat Cell Biol , vol.4 , pp. 42-50
    • Sagot, I.1    Klee, S.2    Pellman, D.3
  • 6
    • 0037178706 scopus 로고    scopus 로고
    • Role of formins in actin assembly: Nucleation and barbed-end association
    • 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.
    • 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.
    • (2002) Science , vol.297 , pp. 612-615
    • Pruyne, D.1    Evangelista, M.2    Yang, C.3    Bi, E.4    Zigmond, S.5    Bretscher, A.6    Boone, C.7
  • 7
    • 0036049615 scopus 로고    scopus 로고
    • An actin nucleation mechanism mediated by Bni1 and profilin
    • 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.
    • 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.
    • (2002) Nat Cell Biol , vol.4 , pp. 626-631
    • Sagot, I.1    Rodal, A.A.2    Moseley, J.3    Goode, B.L.4    Pellman, D.5
  • 8
    • 0037780973 scopus 로고    scopus 로고
    • The fission yeast cytokinesis formin Cdc12p is a barbed end actin filament capping protein gated by profilin
    • 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.
    • 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.
    • (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
  • 9
    • 0043202969 scopus 로고    scopus 로고
    • The mouse formin, mDia1, is a potent actin nucleation factor regulated by auto-inhibition
    • 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.
    • 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.
    • (2003) Curr Biol , vol.13 , pp. 1335-1340
    • Li, F.1    Higgs, H.N.2
  • 10
    • 0038445654 scopus 로고    scopus 로고
    • Formins: Effectors for assembly and polarization of actin filaments
    • A recent review of existing literature on formin structure and function.
    • 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.
    • (2003) J Cell Sci , vol.116 , pp. 2603-2611
    • Evangelista, M.1    Zigmond, S.2    Boone, C.3
  • 11
    • 0032031388 scopus 로고    scopus 로고
    • FH proteins as cytoskeletal organizers
    • Wasserman S. FH proteins as cytoskeletal organizers. Trends Cell Biol. 8:1998;111-115.
    • (1998) Trends Cell Biol , vol.8 , pp. 111-115
    • Wasserman, S.1
  • 13
    • 0142136092 scopus 로고    scopus 로고
    • Formin leaky cap allows elongation in the presence of capping proteins
    • 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.
    • 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.
    • (2003) Curr Biol , vol.13 , pp. 1820-1823
    • Zigmond, S.H.1    Evangelista, M.2    Boone, C.3    Yang, C.4    Dar, A.C.5    Sicheri, F.6    Forkey, J.7    Pring, M.8
  • 14
    • 0037341806 scopus 로고    scopus 로고
    • RhoD regulates endosome dynamics through Diaphanous-related formin and src tyrosine kinase
    • The paper demonstrates a role for formins in endosome movement.
    • 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.
    • (2003) Nat Cell Biol , vol.5 , pp. 195-204
    • Gasman, S.1    Kalaidzidis, Y.2    Zerial, M.3
  • 16
    • 0035966322 scopus 로고    scopus 로고
    • Wnt/Frizzled activation of Rho regulates vertebrate gastrulation and requires a novel Formin homology preotine DAAM1
    • 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.
    • (2001) Cell , vol.107 , pp. 843-854
    • Habas, R.1    Kato, Y.2    He, X.3
  • 17
    • 0034685631 scopus 로고    scopus 로고
    • Rho small G-protein-dependent binding of mDia to a Src homology 3 domain-containing IRSp53/BAIAP2
    • 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.
    • (2000) Biochem Biophys Res Commun , vol.271 , pp. 626-629
    • Fujiwara, T.1    Mammoto, A.2    Kim, Y.3    Takai, Y.4
  • 18
    • 0035951824 scopus 로고    scopus 로고
    • Identification of a carboxyl-terminal Diaphanous-related formin homology protein autoreguatory domain
    • Alberts A.S. Identification of a carboxyl-terminal Diaphanous-related formin homology protein autoreguatory domain. J Biol Chem. 276:2001;2824-2830.
    • (2001) J Biol Chem , vol.276 , pp. 2824-2830
    • Alberts, A.S.1
  • 19
    • 0037695052 scopus 로고    scopus 로고
    • GTPase signalling: New functions for Diaphanous-related formins
    • A discussion of papers showing RhoD binding to hDia2C and Cdc42 to mDia2.
    • 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.
    • (2003) Curr Biol , vol.13 , pp. 360-R362
    • Olson, M.F.1
  • 20
    • 0037815488 scopus 로고    scopus 로고
    • Formin-dependent actin assembly is regulated by distinct modes of Rho signaling in yeast
    • 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.
    • 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.
    • (2003) J Cell Biol , vol.161 , pp. 1081-1092
    • Dong, Y.1    Pruyne, D.2    Bretscher, A.3
  • 21
    • 0037382160 scopus 로고    scopus 로고
    • Disruption of the Diaphanous-related formin Drf1 gene encoding mDia1 reveals a role for Drf3 as an effector for Cdc42
    • 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.
    • 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.
    • (2003) Curr Biol , vol.13 , pp. 534-545
    • Peng, J.1    Wallar, B.J.2    Flanders, A.3    Swiatek, P.J.4    Alberts, A.S.5
  • 22
    • 0141866726 scopus 로고    scopus 로고
    • Activation of the Rac binding partner formin homology 2 domain containing 1 induces actin stress fibers via a ROCK-dependent mechanism
    • 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.
    • (2003) J Biol Chem , vol.278 , pp. 38902-38902
    • Gasteier, J.E.1    Madrid, R.2    Krautkramer, E.3    Schroder, S.4    Muranyi, W.5    Benichou, S.6    Fackler, O.T.7
  • 23
    • 12244291296 scopus 로고    scopus 로고
    • The small GTPase Rho3 and diaphanous/formin For3 function in polarized cell growth in fission yeast
    • 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.
    • (2002) J Cell Sci , vol.115 , pp. 4629-4639
    • Nakano, K.1    Imai, J.2    Arai, R.3    Toh-E, A.4    Matsui, Y.5    Mabuchi, I.6
  • 25
    • 0036835889 scopus 로고    scopus 로고
    • Formins: Intermediates in signal-transduction cascades that affect cytoskeletal reorganization
    • 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.
    • (2002) Trends Plant Sci , vol.7 , pp. 492-498
    • Deeks, M.J.1    Hussey, P.J.2    Davies, B.3
  • 26
    • 0348087045 scopus 로고    scopus 로고
    • A formin homology protein and profilin are required for cytokinesis and Arp2/3-independent assembly of cortical microfilaments in C. elegans
    • 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.
    • (2002) Curr Biol , vol.12 , pp. 2066-2075
    • Severson, A.F.1    Baillie, D.L.2    Bowerman, B.3
  • 27
    • 0037026486 scopus 로고    scopus 로고
    • Actin dynamics in the contractile ring during cytokinesis in fission yeast
    • Pellam R.J., Chang F. Actin dynamics in the contractile ring during cytokinesis in fission yeast. Nature. 419:2002;82-86.
    • (2002) Nature , vol.419 , pp. 82-86
    • Pellam, R.J.1    Chang, F.2
  • 28
    • 0037195254 scopus 로고    scopus 로고
    • Rho1 directs formin-mediated actin ring assembly during budding yeast cytokinesis
    • Tolliday N., VerPlank L., Li R. Rho1 directs formin-mediated actin ring assembly during budding yeast cytokinesis. Curr Biol. 12:2002;R813-R814.
    • (2002) Curr Biol , vol.12 , pp. 813-R814
    • Tolliday, N.1    Verplank, L.2    Li, R.3
  • 29
    • 0035975991 scopus 로고    scopus 로고
    • Role of the fission yeast formin for3p in cell polarity, actin cable formation and symmetric cell division
    • Feierbach B., Chang F. Role of the fission yeast formin for3p in cell polarity, actin cable formation and symmetric cell division. Curr Biol. 11:2001;1656-1665.
    • (2001) Curr Biol , vol.11 , pp. 1656-1665
    • Feierbach, B.1    Chang, F.2
  • 31
    • 0035844869 scopus 로고    scopus 로고
    • Focal contacts as mechanosensors: Externally applied local mechanical force induces growth of focal contacts by an mDIA1-dependent and ROCK-independent mechanism
    • 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.
    • (2001) J Cell Biol , vol.153 , pp. 1175-1186
    • Riveline, D.1    Zamir, E.2    Balaban, N.Q.3    Schwarz, U.S.4    Ishizaki, T.5    Narumiya, S.6    Kam, Z.7    Geiger, B.8    Bershadsky, A.D.9
  • 32
    • 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., Watanabe T. FRL, a novel formin-related protein, binds to Rac and regulates cell motility and survival of macrophages. Mol Cell Biol. 20:2000;6872-6881.
    • (2000) Mol Cell Biol , vol.20 , pp. 6872-6881
    • Yayoshi-Yamamoto, S.1    Taniuchi, I.2    Watanabe, T.3
  • 35
    • 0033163875 scopus 로고    scopus 로고
    • Stress fibers take shape
    • Ridley A.J. Stress fibers take shape. Nat Cell Biol. 1:1999;E64-E66.
    • (1999) Nat Cell Biol , vol.1 , pp. 64-E66
    • Ridley, A.J.1
  • 36
    • 0035914408 scopus 로고    scopus 로고
    • MDia-interacting protein acts downsream of Rho-mDia and modifies Src activation and stress fiber formation
    • Satoh S., Tominaga T. mDia-interacting protein acts downsream of Rho-mDia and modifies Src activation and stress fiber formation. J Biol Chem. 276:2001;39290-39294.
    • (2001) J Biol Chem , vol.276 , pp. 39290-39294
    • Satoh, S.1    Tominaga, T.2
  • 37
    • 0036854328 scopus 로고    scopus 로고
    • The Diaphanous-related formin mDia1 controls serum response factor activity through its effects on actin polymerization
    • Copeland J.W., Treisman R. The Diaphanous-related formin mDia1 controls serum response factor activity through its effects on actin polymerization. Mol Biol Cell. 13:2002;4088-4099.
    • (2002) Mol Biol Cell , vol.13 , pp. 4088-4099
    • Copeland, J.W.1    Treisman, R.2
  • 39
    • 0037458002 scopus 로고    scopus 로고
    • Mechanism of formin-induced nucleation of actin filaments
    • 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.
    • Pring M., Evangelista M., Boone C., Yang C., Zigmond S.H. Mechanism of formin-induced nucleation of actin filaments. Biochemistry. 42:2003;486-496 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.
    • (2003) Biochemistry , vol.42 , pp. 486-496
    • Pring, M.1    Evangelista, M.2    Boone, C.3    Yang, C.4    Zigmond, S.H.5
  • 40
    • 0034896467 scopus 로고    scopus 로고
    • Thermodynamics and kinetics of actin filament nucleation
    • Sept D., McCammon J.A. Thermodynamics and kinetics of actin filament nucleation. Biophys J. 81:2001;667-674.
    • (2001) Biophys J , vol.81 , pp. 667-674
    • Sept, D.1    McCammon, J.A.2
  • 41
    • 0032568650 scopus 로고    scopus 로고
    • The interaction of Arp2/3 complex with actin: Nucleation, high-affinity pointed end capping, and formation of branching networks of filaments
    • Mullins R.D., Heuser J.A., Pollard T.D. The interaction of Arp2/3 complex with actin: nucleation, high-affinity pointed end capping, and formation of branching networks of filaments. Proc. Natl. Acad. Sci. U.S.A. 95:1998;6181-6186.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 6181-6186
    • Mullins, R.D.1    Heuser, J.A.2    Pollard, T.D.3
  • 42
    • 0026439926 scopus 로고
    • Thymosin b4 sequesters the majority of G-actin in resting human polymorphonuclear leukocytes
    • Cassimeris L., Safer D., Nachmias V.T., Zigmond S.H. Thymosin b4 sequesters the majority of G-actin in resting human polymorphonuclear leukocytes. J Cell Biol. 119:1992;1261-1270.
    • (1992) J Cell Biol , vol.119 , pp. 1261-1270
    • Cassimeris, L.1    Safer, D.2    Nachmias, V.T.3    Zigmond, S.H.4
  • 43
    • 0030989560 scopus 로고    scopus 로고
    • Aip3p/Bud6p, a yeast actin-interacting protein that is involved in morphogenesis and the selection of bipolar budding sites
    • Amberg D.C., Zahner J.E., Mulholland J.W., Pringle J.R., Botstein D. Aip3p/Bud6p, a yeast actin-interacting protein that is involved in morphogenesis and the selection of bipolar budding sites. Mol Biol Cell. 8:1997;729-753.
    • (1997) Mol Biol Cell , vol.8 , pp. 729-753
    • Amberg, D.C.1    Zahner, J.E.2    Mulholland, J.W.3    Pringle, J.R.4    Botstein, D.5
  • 44
    • 0038240513 scopus 로고    scopus 로고
    • A role for VASP in RhoA-Diaphanous signalling to actin dynamics and SRF activity
    • Grosse R., Copeland J.W., Newsome T.P., Way M., Treisman R. A role for VASP in RhoA-Diaphanous signalling to actin dynamics and SRF activity. EMBO J. 22:2003;3050-3061.
    • (2003) EMBO J , vol.22 , pp. 3050-3061
    • Grosse, R.1    Copeland, J.W.2    Newsome, T.P.3    Way, M.4    Treisman, R.5
  • 45
    • 0032537023 scopus 로고    scopus 로고
    • Interaction of Rho1p target Bni1p with F-actin binding elongation factor 1α: Implication in Rho1p-regulated reorganization of the actin cytoskeleton in Saccharomyces cerevisiae
    • Umikawa M., Tanaka K., Kamei T., Shimizu K., Imamura H., Sasaki T., Takai Y. Interaction of Rho1p target Bni1p with F-actin binding elongation factor 1α: implication in Rho1p-regulated reorganization of the actin cytoskeleton in Saccharomyces cerevisiae. Oncogene. 16:1998;2011-2016.
    • (1998) Oncogene , vol.16 , pp. 2011-2016
    • Umikawa, M.1    Tanaka, K.2    Kamei, T.3    Shimizu, K.4    Imamura, H.5    Sasaki, T.6    Takai, Y.7
  • 46
    • 0026101084 scopus 로고
    • Mechanism of the insertion of actin monomers between the barbed ends of actin filaments and barbed-end bound insertin
    • Gaertner A., Wegner A. Mechanism of the insertion of actin monomers between the barbed ends of actin filaments and barbed-end bound insertin. J Muscle Res Cell Motil. 12:1991;27-36.
    • (1991) J Muscle Res Cell Motil , vol.12 , pp. 27-36
    • Gaertner, A.1    Wegner, A.2
  • 47
    • 0037154230 scopus 로고    scopus 로고
    • Actin cable dynamics in budding yeast
    • Yang H.-C., Pon L.A. Actin cable dynamics in budding yeast. Proc Natl Acad Sci USA. 99:2002;751-756.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 751-756
    • Yang, H.-C.1    Pon, L.A.2
  • 48
    • 0037459058 scopus 로고    scopus 로고
    • Asymmetric loading of Kar9 onto spindle poles and microtubules ensures proper spindle alignment
    • Liakopoulos D., Kusch J., Grava S., Vogel J., Barral Y. Asymmetric loading of Kar9 onto spindle poles and microtubules ensures proper spindle alignment. Cell. 112:2003;561-574.
    • (2003) Cell , vol.112 , pp. 561-574
    • Liakopoulos, D.1    Kusch, J.2    Grava, S.3    Vogel, J.4    Barral, Y.5
  • 49
    • 0037508893 scopus 로고    scopus 로고
    • Spindle orientation in Saccharomyces cerevisiae depends on the transport of microtubule ends along polarized actin cables
    • Hwang E., Kusch J., Barral Y., Huffaker T.C. Spindle orientation in Saccharomyces cerevisiae depends on the transport of microtubule ends along polarized actin cables. J Cell Biol. 161:2003;483-488.
    • (2003) J Cell Biol , vol.161 , pp. 483-488
    • Hwang, E.1    Kusch, J.2    Barral, Y.3    Huffaker, T.C.4
  • 50
    • 0037451174 scopus 로고    scopus 로고
    • Polarized growth and organelle segregation in yeast: The tracks, motors, and receptors
    • This paper reviews the evidence in yeast for myosin V movement along formin-induced actin cables being a means of delivering secretory vesicles, organelles and mRNA.
    • Bretscher A. Polarized growth and organelle segregation in yeast: the tracks, motors, and receptors. J Cell Biol. 160:2003;811-816 This paper reviews the evidence in yeast for myosin V movement along formin-induced actin cables being a means of delivering secretory vesicles, organelles and mRNA.
    • (2003) J Cell Biol , vol.160 , pp. 811-816
    • Bretscher, A.1
  • 51
    • 0037933457 scopus 로고    scopus 로고
    • Microtubule asymmetry
    • Gundersen G.G., Bretscher A. Microtubule asymmetry. Science. 300:2003;2040-2041.
    • (2003) Science , vol.300 , pp. 2040-2041
    • Gundersen, G.G.1    Bretscher, A.2
  • 52
    • 0034105436 scopus 로고    scopus 로고
    • Functional analysis of the Drosophila Diaphanous FH protein in early embryonic development
    • Afshar K., Stuart B., Wasserman S.A. Functional analysis of the Drosophila Diaphanous FH protein in early embryonic development. Development. 127:2000;1887-1897.
    • (2000) Development , vol.127 , pp. 1887-1897
    • Afshar, K.1    Stuart, B.2    Wasserman, S.A.3
  • 53
    • 0037244352 scopus 로고    scopus 로고
    • A RhoGEF and Rho family GTPase-activating protein complex links the contractile ring to cortical microtubules at the onset of cytokinesis
    • Somers W.G., Saint R. A RhoGEF and Rho family GTPase-activating protein complex links the contractile ring to cortical microtubules at the onset of cytokinesis. Dev Cell. 4:2003;29-39.
    • (2003) Dev Cell , vol.4 , pp. 29-39
    • Somers, W.G.1    Saint, R.2
  • 54
    • 0038709510 scopus 로고    scopus 로고
    • Cell division: The place and the time of cytokinesis
    • Gonzalez C. Cell division: the place and the time of cytokinesis. Curr Biol. 13:2003;R363-R365.
    • (2003) Curr Biol , vol.13 , pp. 363-R365
    • Gonzalez, C.1
  • 56
    • 0036305635 scopus 로고    scopus 로고
    • ROCK and Dia have opposing effects on adherens junctions downstream of Rho
    • Sahai E., Marshall C.J. ROCK and Dia have opposing effects on adherens junctions downstream of Rho. Nat Cell Biol. 4:2002;408-415.
    • (2002) Nat Cell Biol , vol.4 , pp. 408-415
    • Sahai, E.1    Marshall, C.J.2
  • 57
    • 0031746109 scopus 로고    scopus 로고
    • Further characterization of the DFNA1 audiovestibular phenotype
    • Lalvani A.K. Further characterization of the DFNA1 audiovestibular phenotype. Arch Otolaryngol. 124:1998;699-702.
    • (1998) Arch Otolaryngol , vol.124 , pp. 699-702
    • Lalvani, A.K.1
  • 58
    • 79961145390 scopus 로고    scopus 로고
    • Evidence for the binding of a human sperm component with Diaphanous protein
    • Zhang S.M., Miao S.Y., Wang L.F. Evidence for the binding of a human sperm component with Diaphanous protein. Arch Androl. 46:2001;29-35.
    • (2001) Arch Androl , vol.46 , pp. 29-35
    • Zhang, S.M.1    Miao, S.Y.2    Wang, L.F.3
  • 59
    • 0037743636 scopus 로고    scopus 로고
    • Gremilin is the BMP antagoist required for maintenance of Shh and Fgf signals during limb patterning
    • Khokha M.K., Hsu D., Brunet L.J., Dionne M.S., Harland R.M. Gremilin is the BMP antagoist required for maintenance of Shh and Fgf signals during limb patterning. Nat Genet. 34:2003;303-307.
    • (2003) Nat Genet , vol.34 , pp. 303-307
    • Khokha, M.K.1    Hsu, D.2    Brunet, L.J.3    Dionne, M.S.4    Harland, R.M.5
  • 60
    • 0034907213 scopus 로고    scopus 로고
    • MDia mediates Rho-regulated formation and orientation of stable microtubules
    • Palazzo A.F., Cook T.A., Alberts A.S., Gundersen G.G. mDia mediates Rho-regulated formation and orientation of stable microtubules. Nat Cell Biol. 3:2001;723-729.
    • (2001) Nat Cell Biol , vol.3 , pp. 723-729
    • Palazzo, A.F.1    Cook, T.A.2    Alberts, A.S.3    Gundersen, G.G.4
  • 61
    • 0035081810 scopus 로고    scopus 로고
    • Localization of mammalian homolog of diaphanous, mDia1, to the mitotic spindle in HeLa cells
    • Kato T., Watanabe N., Morishima Y., Fujita A., Ishizaki T., Narumiya S. Localization of mammalian homolog of diaphanous, mDia1, to the mitotic spindle in HeLa cells. J Cell Sci. 114:2001;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
  • 62
    • 0037339268 scopus 로고    scopus 로고
    • Force generation by actin polymerization II. The elastic ratchet and tethered filaments
    • Mogilner A., Oster G. Force generation by actin polymerization II. The elastic ratchet and tethered filaments. Biophys J. 84:2003;1591-1605.
    • (2003) Biophys J , vol.84 , pp. 1591-1605
    • Mogilner, A.1    Oster, G.2
  • 63
    • 0028607563 scopus 로고
    • Direct measurement of stiffness of single actin filaments with and without tropomyosin by in vitro nanomanipulation
    • Kojima H., Ishijima A., Yanagida T. Direct measurement of stiffness of single actin filaments with and without tropomyosin by in vitro nanomanipulation. Proc Natl Acad Sci U.S.A. 91:1994;12962-12966.
    • (1994) Proc Natl Acad Sci U.S.A. , vol.91 , pp. 12962-12966
    • Kojima, H.1    Ishijima, A.2    Yanagida, T.3
  • 65
    • 0036714316 scopus 로고    scopus 로고
    • Invasive cell migration is initiated by guided growth of long cellular extensions
    • Fulga T.A., Rorth P. Invasive cell migration is initiated by guided growth of long cellular extensions. Nat Cell Biol. 4:2002;E211-E212.
    • (2002) Nat Cell Biol , vol.4 , pp. 211-E212
    • Fulga, T.A.1    Rorth, P.2
  • 66
    • 0033868010 scopus 로고    scopus 로고
    • Substrate-cytoskeletal coupling as a mechanism for the regulation of growth cone motility and guidance
    • Suter D.M., Forscher P. Substrate-cytoskeletal coupling as a mechanism for the regulation of growth cone motility and guidance. J Neurobiol. 44:2000;97-113.
    • (2000) J Neurobiol , vol.44 , pp. 97-113
    • Suter, D.M.1    Forscher, P.2


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