메뉴 건너뛰기




Volumn 23, Issue 19, 2012, Pages 3801-3813

Autoinhibition of the formin Cappuccino in the absence of canonical autoinhibitory domains

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; DROSOPHILA PROTEIN; PROTEIN; PROTEIN CANONICAL AUTOINHIBITORY DOMAIN; PROTEIN CAPPUCCINO; UNCLASSIFIED DRUG;

EID: 84867152062     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E12-04-0288     Document Type: Article
Times cited : (27)

References (58)
  • 1
    • 0033609158 scopus 로고    scopus 로고
    • Identification of profilin and src homology 3 domains as binding partners for Drosophila Enabled
    • Ahern-Djamali SM (1999). Identification of profilin and src homology 3 domains as binding partners for Drosophila Enabled. Proc Natl Acad Sci USA 96, 4977-4982.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 4977-4982
    • Ahern-Djamali, S.M.1
  • 2
    • 0035951824 scopus 로고    scopus 로고
    • Identification of a carboxyl-terminal diaphanous-related formin homology protein autoregulatory domain
    • Alberts AS (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
  • 3
    • 54649083796 scopus 로고    scopus 로고
    • Spindle positioning in mouse oocytes relies on a dynamic meshwork of actin filaments
    • Azoury J, Lee KW, Georget V, Rassinier P, Leader B, Verlhac M-H (2008). Spindle positioning in mouse oocytes relies on a dynamic meshwork of actin filaments. Curr Biol 18, 1514-1519.
    • (2008) Curr Biol , vol.18 , pp. 1514-1519
    • Azoury, J.1    Lee, K.W.2    Georget, V.3    Rassinier, P.4    Leader, B.5    Verlhac, M.-H.6
  • 4
    • 80051498479 scopus 로고    scopus 로고
    • Anterior-posterior axis specification in Drosophila oocytes: Identification of novel bicoid and oskar mRNA localization factors
    • Chang C-W, Nashchekin D, Wheatley L, Irion U, Dahlgaard K, Montague TG, Hall J, Johnston DS (2011). Anterior-posterior axis specification in Drosophila oocytes: identification of novel bicoid and oskar mRNA localization factors. Genetics 188, 883-896.
    • (2011) Genetics , vol.188 , pp. 883-896
    • Chang, C.-W.1    Nashchekin, D.2    Wheatley, L.3    Irion, U.4    Dahlgaard, K.5    Montague, T.G.6    Hall, J.7    Johnston, D.S.8
  • 5
    • 84858967947 scopus 로고    scopus 로고
    • Multiple forms of Spire-actin complexes and their functional consequences
    • Chen CK, Sawaya MR, Phillips ML, Reisler E, Quinlan ME (2012). Multiple forms of Spire-actin complexes and their functional consequences. J Biol Chem 287, 10684-10692.
    • (2012) J Biol Chem , vol.287 , pp. 10684-10692
    • Chen, C.K.1    Sawaya, M.R.2    Phillips, M.L.3    Reisler, E.4    Quinlan, M.E.5
  • 6
    • 59649092799 scopus 로고    scopus 로고
    • Displacement of formins from growing barbed ends by bud14 is critical for actin cable architecture and function
    • Chesarone M, Gould CJ, Moseley JB, Goode BL (2009). Displacement of formins from growing barbed ends by bud14 is critical for actin cable architecture and function. Dev Cell 16, 292-302.
    • (2009) Dev Cell , vol.16 , pp. 292-302
    • Chesarone, M.1    Gould, C.J.2    Moseley, J.B.3    Goode, B.L.4
  • 7
    • 33748745132 scopus 로고    scopus 로고
    • INF2 is a WASP homology 2 motif-containing formin that severs actin filaments and accelerates both polymerization and depolymerization
    • DOI 10.1074/jbc.M604666200
    • Chhabra ES, Higgs HN (2006). INF2 Is a WASP homology 2 motif-containing formin that severs actin filaments and accelerates both polymerization and depolymerization. J Biol Chem 281, 26754-26767. (Pubitemid 44401884)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.36 , pp. 26754-26767
    • Chhabra, E.S.1    Higgs, H.N.2
  • 8
    • 67650566835 scopus 로고    scopus 로고
    • INF2 is an endoplasmic reticulum-associated formin protein
    • Chhabra ES, Ramabhadran V, Gerber SA, Higgs HN (2009). INF2 is an endoplasmic reticulum-associated formin protein. J Cell Sci 122, 1430-1440.
    • (2009) J Cell Sci , vol.122 , pp. 1430-1440
    • Chhabra, E.S.1    Ramabhadran, V.2    Gerber, S.A.3    Higgs, H.N.4
  • 9
    • 34848873760 scopus 로고    scopus 로고
    • Capu and Spire Assemble a Cytoplasmic Actin Mesh that Maintains Microtubule Organization in the Drosophila Oocyte
    • DOI 10.1016/j.devcel.2007.09.003, PII S1534580707003437
    • Dahlgaard K, Raposo AASF, Niccoli T, Johnston DS (2007). Capu and Spire assemble a cytoplasmic actin mesh that maintains microtubule organization in the Drosophila oocyte. Dev Cell 13, 539-553. (Pubitemid 47500810)
    • (2007) Developmental Cell , vol.13 , Issue.4 , pp. 539-553
    • Dahlgaard, K.1    Raposo, A.A.S.F.2    Niccoli, T.3    St, J.D.4
  • 10
    • 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, 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
  • 11
    • 34248154652 scopus 로고    scopus 로고
    • Mechanism and function of formins in the control of actin assembly
    • Goode BL, Eck MJ (2007). Mechanism and function of formins in the control of actin assembly. Annu Rev Biochem 76, 593-627.
    • (2007) Annu Rev Biochem , vol.76 , pp. 593-627
    • Goode, B.L.1    Eck, M.J.2
  • 12
    • 78751536310 scopus 로고    scopus 로고
    • Mechanisms of plasma membrane targeting of formin mDia2 through its amino terminal domains
    • Gorelik R, Yang C, Kameswaran V, Dominguez R, Svitkina T (2011). Mechanisms of plasma membrane targeting of formin mDia2 through its amino terminal domains. Mol Biol Cell 22, 189-201.
    • (2011) Mol Biol Cell , vol.22 , pp. 189-201
    • Gorelik, R.1    Yang, C.2    Kameswaran, V.3    Dominguez, R.4    Svitkina, T.5
  • 14
    • 78049521359 scopus 로고    scopus 로고
    • VASP is a processive actin polymerase that requires monomeric actin for barbed end association
    • Hansen SD, Mullins RD (2010). VASP is a processive actin polymerase that requires monomeric actin for barbed end association. J Cell Biol 191, 571-584.
    • (2010) J Cell Biol , vol.191 , pp. 571-584
    • Hansen, S.D.1    Mullins, R.D.2
  • 15
    • 84856279315 scopus 로고    scopus 로고
    • The C terminus of formin FMNL3 accelerates actin polymerization and contains a WH2 domain-like sequence that binds both monomers and filament barbed ends
    • Heimsath EG Jr, Higgs HN (2012). The C terminus of formin FMNL3 accelerates actin polymerization and contains a WH2 domain-like sequence that binds both monomers and filament barbed ends. J Biol Chem 287, 3087-3098.
    • (2012) J Biol Chem , vol.287 , pp. 3087-3098
    • Heimsath Jr., E.G.1    Higgs, H.N.2
  • 17
    • 11144281883 scopus 로고    scopus 로고
    • Phylogenetic analysis of the formin homology 2 domain
    • DOI 10.1091/mbc.E04-07-0565
    • Higgs HN, Peterson KJ (2005). Phylogenetic analysis of the formin homology 2 domain. Mol Biol Cell 16, 1-13. (Pubitemid 40024285)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.1 , pp. 1-13
    • Higgs, H.N.1    Peterson, K.J.2
  • 18
    • 1342310742 scopus 로고    scopus 로고
    • Mammalian formin-1 participates in adherens junctions and polymerization of linear actin cables
    • DOI 10.1038/ncb1075
    • Kobielak A, Pasolli HA, Fuchs E (2003). Mammalian formin-1 participates in adherens junctions and polymerization of linear actin cables. Nat Cell Biol 6, 21-30. (Pubitemid 38425726)
    • (2004) Nature Cell Biology , vol.6 , Issue.1 , pp. 21-30
    • Kobielak, A.1    Pasolli, H.A.2    Fuchs, E.3
  • 19
    • 31044433924 scopus 로고    scopus 로고
    • Control of the assembly of ATP- and ADP-actin by formins and profilin
    • DOI 10.1016/j.cell.2005.11.038, PII S009286740501398X
    • Kovar DR, Harris ES, Mahaffy R, Higgs HN, Pollard TD (2006). Control of the assembly of ATP- and ADP-actin by formins and profilin. Cell 124, 423-435. (Pubitemid 43121988)
    • (2006) Cell , vol.124 , Issue.2 , pp. 423-435
    • Kovar, D.R.1    Harris, E.S.2    Mahaffy, R.3    Higgs, H.N.4    Pollard, T.D.5
  • 20
    • 0037780973 scopus 로고    scopus 로고
    • The fission yeast cytokinesis formin Cdc12p is a barbed end actin filament capping protein gated by profilin
    • DOI 10.1083/jcb.200211078
    • Kovar DR, Kuhn JR, Tichy AL, Pollard TD (2003). The fission yeast cytokinesis formin Cdc12p is a barbed end actin filament capping protein gated by profilin. J Cell Biol 161, 875-887. (Pubitemid 36718421)
    • (2003) Journal of Cell Biology , vol.161 , Issue.5 , pp. 875-887
    • Kovar, D.R.1    Kuhn, J.R.2    Tichy, A.L.3    Pollard, T.D.4
  • 21
    • 24944535773 scopus 로고    scopus 로고
    • Crystal structure of non-fused glutathione S-transferase from Schistosoma japonicum in complex with glutathione
    • DOI 10.2174/0929866054696154
    • Kursula I, Heape AM, Kursula P (2005). Crystal structure of non-fused glutathione S-transferase from Schistosoma japonicum in complex with glutathione. Protein Pept Lett 12, 709-712. (Pubitemid 41305833)
    • (2005) Protein and Peptide Letters , vol.12 , Issue.7 , pp. 709-712
    • Kursula, I.1    Heape, A.M.2    Kursula, P.3
  • 22
    • 28644442126 scopus 로고    scopus 로고
    • The regulation of mDia1 by autoinhibition and its release by Rho*GTP
    • DOI 10.1038/sj.emboj.7600879
    • Lammers M, Rose R, Scrima A, Wittinghofer A (2005). The regulation of mDia1 by autoinhibition and its release by Rho*GTP. EMBO J 24, 4176-4187. (Pubitemid 41752886)
    • (2005) EMBO Journal , vol.24 , Issue.23 , pp. 4176-4187
    • Lammers, M.1    Rose, R.2    Scrima, A.3    Wittinghofer, A.4
  • 23
    • 0043202969 scopus 로고    scopus 로고
    • The mouse formin mDia1 is a potent actin nucleation factor regulated by autoinhibition
    • DOI 10.1016/S0960-9822(03)00540-2
    • Li F, Higgs HN (2003). The mouse formin mDia1 is a potent actin nucleation factor regulated by autoinhibition. Curr Biol 13, 1335-1340. (Pubitemid 36953308)
    • (2003) Current Biology , vol.13 , Issue.15 , pp. 1335-1340
    • Li, F.1    Higgs, H.N.2
  • 24
    • 14844288286 scopus 로고    scopus 로고
    • Dissecting requirements for auto-inhibition of actin nucleation by the formin, mDia1
    • DOI 10.1074/jbc.M411605200
    • Li F, Higgs HN (2005). Dissecting requirements for auto-inhibition of actin nucleation by the formin, mDia1. J Biol Chem 280, 6986-6992. (Pubitemid 40341254)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.8 , pp. 6986-6992
    • Li, F.1    Higgs, H.N.2
  • 26
    • 0035163855 scopus 로고    scopus 로고
    • Profilin binding to poly-L-proline and actin monomers along with ability to catalyze actin nucleotide exchange is required for viability of fission yeast
    • Lu J, Pollard TD (2001). Profilin binding to poly-L-proline and actin monomers along with ability to catalyze actin nucleotide exchange is required for viability of fission yeast. Mol Biol Cell 12, 1161-1175. (Pubitemid 33052006)
    • (2001) Molecular Biology of the Cell , vol.12 , Issue.4 , pp. 1161-1175
    • Lu, J.1    Pollard, T.D.2
  • 27
    • 0019135186 scopus 로고
    • Identification of a factor in conventional muscle actin preparations which inhibits actin filament self-association
    • MacLean-Fletcher S, Pollard TD (1980). Identification of a factor in conventional muscle actin preparations which inhibits actin filament self-association. Biochem Biophys Res Commun 96, 18-27.
    • (1980) Biochem Biophys Res Commun , vol.96 , pp. 18-27
    • MacLean-Fletcher, S.1    Pollard, T.D.2
  • 29
    • 0024723365 scopus 로고
    • Cappuccino and spire: Two unique maternal-effect loci required for both the anteroposterior and dorsoventral patterns of the Drosophila embryo
    • Manseau LJ, Schüpbach T (1989). Cappuccino and spire: two unique maternal-effect loci required for both the anteroposterior and dorsoventral patterns of the Drosophila embryo. Genes Dev 3, 1437-1452.
    • (1989) Genes Dev , vol.3 , pp. 1437-1452
    • Manseau, L.J.1    Schüpbach, T.2
  • 30
    • 58649122903 scopus 로고    scopus 로고
    • Formin differentially utilizes profilin isoforms to rapidly assemble actin filaments
    • Neidt EM, Scott BJ, Kovar DR (2009). Formin differentially utilizes profilin isoforms to rapidly assemble actin filaments. J Biol Chem 284, 673-684.
    • (2009) J Biol Chem , vol.284 , pp. 673-684
    • Neidt, E.M.1    Scott, B.J.2    Kovar, D.R.3
  • 31
    • 77958582305 scopus 로고    scopus 로고
    • Crystal structure of a complex between amino and carboxy terminal fragments of mDia1: Insights into autoinhibition of diaphanous-related formins
    • Nezami A, Poy F, Toms A, Zheng W, Eck MJ (2010). Crystal structure of a complex between amino and carboxy terminal fragments of mDia1: insights into autoinhibition of diaphanous-related formins. PLoS One 5, e12992.
    • (2010) PLoS One , vol.5
    • Nezami, A.1    Poy, F.2    Toms, A.3    Zheng, W.4    Eck, M.J.5
  • 32
    • 32044470440 scopus 로고    scopus 로고
    • Structure of the autoinhibitory switch in formin mDia1
    • Nezami AG, Poy F, Eck MJ (2006). Structure of the autoinhibitory switch in formin mDia1. Structure 14, 257-263.
    • (2006) Structure , vol.14 , pp. 257-263
    • Nezami, A.G.1    Poy, F.2    Eck, M.J.3
  • 33
  • 34
    • 13444280218 scopus 로고    scopus 로고
    • Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain
    • DOI 10.1038/nature03251
    • Otomo T, Tomchick DR, Otomo C, Panchal SC, Machius M, Rosen MK (2005). Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain. Nature 433, 488-494. (Pubitemid 40204299)
    • (2005) Nature , vol.433 , Issue.7025 , pp. 488-494
    • Otomo, T.1    Tomchick, D.R.2    Otomo, C.3    Panchal, S.C.4    Machius, M.5    Rosen, M.K.6
  • 36
    • 40149105917 scopus 로고    scopus 로고
    • The role of the FH1 domain and profilin in formin-mediated actin-filament elongation and nucleation
    • Paul AS, Paul A, Pollard TD, Pollard T (2008). The role of the FH1 domain and profilin in formin-mediated actin-filament elongation and nucleation. Curr Biol 18, 9-19.
    • (2008) Curr Biol , vol.18 , pp. 9-19
    • Paul, A.S.1    Paul, A.2    Pollard, T.D.3    Pollard, T.4
  • 37
    • 69949127688 scopus 로고    scopus 로고
    • Identification of a short Spir interaction sequence at the C-terminal end of formin subgroup proteins
    • Pechlivanis M, Samol A, Kerkhoff E (2009). Identification of a short Spir interaction sequence at the C-terminal end of formin subgroup proteins. J Biol Chem 284, 25324-25333.
    • (2009) J Biol Chem , vol.284 , pp. 25324-25333
    • Pechlivanis, M.1    Samol, A.2    Kerkhoff, E.3
  • 38
    • 79958075131 scopus 로고    scopus 로고
    • Spire-type actin nucleators cooperate with formin-2 to drive asymmetric oocyte division
    • Pfender S, Kuznetsov V, Pleiser S, Kerkhoff E, Schuh M (2011). Spire-type actin nucleators cooperate with formin-2 to drive asymmetric oocyte division. Curr Biol 21, 955-960.
    • (2011) Curr Biol , vol.21 , pp. 955-960
    • Pfender, S.1    Kuznetsov, V.2    Pleiser, S.3    Kerkhoff, E.4    Schuh, M.5
  • 39
    • 0022881322 scopus 로고
    • Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments
    • Pollard TD (1986). Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments. J Cell Biol 103, 2747-2754.
    • (1986) J Cell Biol , vol.103 , pp. 2747-2754
    • Pollard, T.D.1
  • 40
    • 0037178706 scopus 로고    scopus 로고
    • Role of formins in actin assembly: Nucleation and barbed-end association
    • DOI 10.1126/science.1072309
    • Pruyne D, Evangelista M, Yang C, Bi E, Zigmond S, Bretscher A, Boone C (2002). Role of formins in actin assembly: nucleation and barbed-end association. Science 297, 612-615. (Pubitemid 34815347)
    • (2002) Science , vol.297 , Issue.5581 , pp. 612-615
    • Pruyne, D.1    Evangelista, M.2    Yang, C.3    Bi, E.4    Zigmond, S.5    Bretscher, A.6    Boone, C.7
  • 41
    • 84858077472 scopus 로고    scopus 로고
    • The Pfam protein families database
    • Punta M et al. (2012). The Pfam protein families database. Nucleic Acids Res 40, D290-D301.
    • (2012) Nucleic Acids Res , vol.40
    • Punta, M.1
  • 42
    • 35349021033 scopus 로고    scopus 로고
    • Regulatory interactions between two actin nucleators, Spire and Cappuccino
    • DOI 10.1083/jcb.200706196
    • Quinlan ME, Hilgert S, Bedrossian A, Mullins RD, Kerkhoff E (2007). Regulatory interactions between two actin nucleators, Spire and Cappuccino. J Cell Biol 179, 117-128. (Pubitemid 47606688)
    • (2007) Journal of Cell Biology , vol.179 , Issue.1 , pp. 117-128
    • Quinlan, M.E.1    Hilgert, S.2    Bedrossian, A.3    Mullins, R.D.4    Kerkhoff, E.5
  • 45
    • 19544386803 scopus 로고    scopus 로고
    • Structural and mechanistic insights into the interaction between Rho and mammalian Dia
    • Rose R, Weyand M, Lammers M, Ishizaki T, Ahmadian MR, Wittinghofer A (2005). Structural and mechanistic insights into the interaction between Rho and mammalian Dia. Nature 435, 513-518.
    • (2005) Nature , vol.435 , pp. 513-518
    • Rose, R.1    Weyand, M.2    Lammers, M.3    Ishizaki, T.4    Ahmadian, M.R.5    Wittinghofer, A.6
  • 46
    • 77649273530 scopus 로고    scopus 로고
    • Fifteen formins for an actin filament: A molecular view on the regulation of human formins
    • Schönichen A, Geyer M (2010). Fifteen formins for an actin filament: A molecular view on the regulation of human formins. Biochim Biophys Acta 1803, 152-163.
    • (2010) Biochim Biophys Acta , vol.1803 , pp. 152-163
    • Schönichen, A.1    Geyer, M.2
  • 47
    • 57649245603 scopus 로고    scopus 로고
    • A new model for asymmetric spindle positioning in mouse oocytes
    • Schuh M, Ellenberg J (2008). A new model for asymmetric spindle positioning in mouse oocytes. Curr Biol 18, 1986-1992.
    • (2008) Curr Biol , vol.18 , pp. 1986-1992
    • Schuh, M.1    Ellenberg, J.2
  • 48
    • 50849103669 scopus 로고    scopus 로고
    • The human formin FHOD1 contains a bipartite structure of FH3 and GTPase-binding domains required for activation
    • Schulte A, Stolp B, Schönichen AS, Pylypenko O, Rak A, Fackler OT, Geyer M (2008). The human formin FHOD1 contains a bipartite structure of FH3 and GTPase-binding domains required for activation. Cell 16, 1313-1323.
    • (2008) Cell , vol.16 , pp. 1313-1323
    • Schulte, A.1    Stolp, B.2    Schönichen, A.S.3    Pylypenko, O.4    Rak, A.5    Fackler, O.T.6    Geyer, M.7
  • 49
    • 33748123994 scopus 로고    scopus 로고
    • Autoinhibition regulates cellular localization and actin assembly activity of the diaphanous-related formins FRLalpha and mDia1
    • DOI 10.1083/jcb.200605006
    • Seth A, Otomo C, Rosen MK (2006). Autoinhibition regulates cellular localization and actin assembly activity of the diaphanous-related formins FRLalpha and mDia1. J Cell Biol 174, 701-713. (Pubitemid 44306726)
    • (2006) Journal of Cell Biology , vol.174 , Issue.5 , pp. 701-713
    • Seth, A.1    Otomo, C.2    Rosen, M.K.3
  • 50
    • 77958568483 scopus 로고    scopus 로고
    • Segmentation and tracking of cytoskeletal filaments using open active contours
    • Smith MB, Li H, Shen T, Huang X, Yusuf E, Vavylonis D (2010). Segmentation and tracking of cytoskeletal filaments using open active contours. Cytoskeleton 67, 693-705.
    • (2010) Cytoskeleton , vol.67 , pp. 693-705
    • Smith, M.B.1    Li, H.2    Shen, T.3    Huang, X.4    Yusuf, E.5    Vavylonis, D.6
  • 51
    • 0027447099 scopus 로고
    • A self-consistent method for the analysis of protein secondary structure from circular dichroism
    • DOI 10.1006/abio.1993.1079
    • Sreerama N, Woody RW (1993). A self-consistent method for the analysis of protein secondary structure from circular dichroism. Anal Biochem 209, 32-44. (Pubitemid 23084702)
    • (1993) Analytical Biochemistry , vol.209 , Issue.1 , pp. 32-44
    • Sreerama, N.1    Woody, R.W.2
  • 52
    • 79957629724 scopus 로고    scopus 로고
    • Drosophila Mon2 couples Oskar-induced endocytosis with actin remodeling for cortical anchorage of the germ plasm
    • Tanaka T, Kato Y, Matsuda K, Hanyu-Nakamura K, Nakamura A (2011). Drosophila Mon2 couples Oskar-induced endocytosis with actin remodeling for cortical anchorage of the germ plasm. Development 138, 2523-2532.
    • (2011) Development , vol.138 , pp. 2523-2532
    • Tanaka, T.1    Kato, Y.2    Matsuda, K.3    Hanyu-Nakamura, K.4    Nakamura, A.5
  • 53
    • 0027945945 scopus 로고
    • Premature microtubule-dependent cytoplasmic streaming in cappuccino and spire mutant oocytes
    • Theurkauf W (1994). Premature microtubule-dependent cytoplasmic streaming in cappuccino and spire mutant oocytes. Science 265, 2093-2096.
    • (1994) Science , vol.265 , pp. 2093-2096
    • Theurkauf, W.1
  • 54
    • 57749105439 scopus 로고    scopus 로고
    • Interaction of the N- and C-terminal autoregulatory domains of FRL2 does not inhibit FRL2 activity
    • Vaillant DC, Copeland SJ, Davis C, Thurston SF, Abdennur N, Copeland JW (2008). Interaction of the N- and C-terminal autoregulatory domains of FRL2 does not inhibit FRL2 activity. J Biol Chem 283, 33750-33762.
    • (2008) J Biol Chem , vol.283 , pp. 33750-33762
    • Vaillant, D.C.1    Copeland, S.J.2    Davis, C.3    Thurston, S.F.4    Abdennur, N.5    Copeland, J.W.6
  • 55
    • 0032483044 scopus 로고    scopus 로고
    • Interactions of Acanthamoeba profilin with actin and nucleotides bound to actin
    • DOI 10.1021/bi980093l, PII S0006296098000932
    • Vinson VK, Cruz EMDL, Higgs HN, Pollard TD (1998). Interactions of Acanthamoeba profilin with actin and nucleotides bound to actin. Biochemistry 37, 10871-10880. (Pubitemid 28368911)
    • (1998) Biochemistry , vol.37 , Issue.31 , pp. 10871-10880
    • Vinson, V.K.1    De La, C.E.M.2    Higgs, H.N.3    Pollard, T.D.4
  • 57
    • 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 (1999). Cooperation between mDia1 and ROCK in Rho-induced actin reorganization. Nat Cell Biol 1, 136-143. (Pubitemid 129656017)
    • (1999) Nature Cell Biology , vol.1 , Issue.3 , pp. 136-143
    • Watanabe, N.1    Kato, T.2    Fujita, A.3    Ishizaki, T.4    Narumiya, S.5
  • 58
    • 0035793587 scopus 로고    scopus 로고
    • Activation of the Arp2/3 complex by the Listeria acta protein. Acta binds two actin monomers and three subunits of the Arp2/3 complex
    • Zalevsky J, Grigorova I, Mullins RD (2001). Activation of the Arp2/3 complex by the Listeria acta protein. Acta binds two actin monomers and three subunits of the Arp2/3 complex. J Biol Chem 276, 3468-3475.
    • (2001) J Biol Chem , vol.276 , pp. 3468-3475
    • Zalevsky, J.1    Grigorova, I.2    Mullins, R.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.