메뉴 건너뛰기




Volumn 15, Issue 10, 2014, Pages 677-689

Capping protein regulators fine-tune actin assembly dynamics

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTIN CAPPING PROTEIN; ACTIN RELATED PROTEIN 2-3 COMPLEX; CD2 ASSOCIATED PROTEIN; ELONGATION FACTOR; METHENAMINE; MYOSIN I; PHOSPHOLIPID; VASODILATOR STIMULATED PHOSPHOPROTEIN; ACTIN BINDING PROTEIN; CARMIL1 PROTEIN, HUMAN; CARRIER PROTEIN; CD2-ASSOCIATED PROTEIN; CYTOSKELETON PROTEIN; DNA BINDING PROTEIN; ENA/VASP PROTEINS; POLYPHOSPHOINOSITIDE; SIGNAL TRANSDUCING ADAPTOR PROTEIN; WASH PROTEIN, HUMAN;

EID: 84910150867     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm3869     Document Type: Review
Times cited : (225)

References (175)
  • 1
    • 70849098888 scopus 로고    scopus 로고
    • Actin a central player in cell shape and movement
    • Pollard, T. D., & Cooper, J. A. Actin, a central player in cell shape and movement. Science 326, 1208-1212 (2009
    • (2009) Science , vol.326 , pp. 1208-1212
    • Pollard, T.D.1    Cooper, J.A.2
  • 3
    • 84888428383 scopus 로고    scopus 로고
    • Guardians of the actin monomer
    • Xue, B., & Robinson, R. C. Guardians of the actin monomer. Eur. J. Cell Biol. 92, 316-332 (2013
    • (2013) Eur. J. Cell Biol. , vol.92 , pp. 316-332
    • Xue, B.1    Robinson, R.C.2
  • 4
    • 84857794759 scopus 로고    scopus 로고
    • Synergistic bar-npf interactions in actin-driven membrane remodeling
    • Suetsugu, S., & Gautreau, A. Synergistic BAR-NPF interactions in actin-driven membrane remodeling. Trends Cell Biol. 22, 141-150 (2012
    • (2012) Trends Cell Biol. , vol.22 , pp. 141-150
    • Suetsugu, S.1    Gautreau, A.2
  • 5
    • 84870209800 scopus 로고    scopus 로고
    • Rho family gtpases
    • Hall, A. Rho family GTPases. Biochem. Soc. Trans. 40, 1378-1382 (2012
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 1378-1382
    • Hall, A.1
  • 6
    • 77951272888 scopus 로고    scopus 로고
    • Structural insights into de novo actin polymerization
    • Dominguez, R. Structural insights into de novo actin polymerization. Curr. Opin. Struct. Biol. 20, 217-225 (2010
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 217-225
    • Dominguez, R.1
  • 7
    • 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, C. J., Moseley, J. B., & Goode, B. L. Displacement of formins from growing barbed ends by bud14 is critical for actin cable architecture and function. Dev. Cell 16, 292-302 (2009
    • (2009) Dev. Cell , vol.16 , pp. 292-302
    • Chesarone, M.1    Gould, C.J.2    Moseley, J.B.3    Goode, B.L.4
  • 9
    • 77950859278 scopus 로고    scopus 로고
    • Adf/cofilin: A functional node in cell biology
    • Bernstein, B. W., & Bamburg, J. R. ADF/cofilin: a functional node in cell biology. Trends Cell Biol. 20, 187-195 (2010
    • (2010) Trends Cell Biol. , vol.20 , pp. 187-195
    • Bernstein, B.W.1    Bamburg, J.R.2
  • 10
    • 80052990415 scopus 로고    scopus 로고
    • Actin-depolymerizing factor homology domain: A conserved fold performing diverse roles in cytoskeletal dynamics
    • Poukkula, M., Kremneva, E., Serlachius, M., & Lappalainen, P. Actin-depolymerizing factor homology domain: a conserved fold performing diverse roles in cytoskeletal dynamics. Cytoskeleton 68, 471-490 (2011
    • (2011) Cytoskeleton , vol.68 , pp. 471-490
    • Poukkula, M.1    Kremneva, E.2    Serlachius, M.3    Lappalainen, P.4
  • 11
    • 48949106158 scopus 로고    scopus 로고
    • New insights into mechanism and regulation of actin capping protein
    • Cooper, J. A., & Sept, D. New insights into mechanism and regulation of actin capping protein. Int. Rev. Cell. Mol. Biol. 267, 183-206 (2008
    • (2008) Int. Rev. Cell. Mol. Biol. , vol.267 , pp. 183-206
    • Cooper, J.A.1    Sept, D.2
  • 12
    • 4043115604 scopus 로고    scopus 로고
    • Lamellipodial versus filopodial mode of the actin nanomachinery: Pivotal role of the filament barbed end
    • Shows that loss of CP in migrating cultured cells leads to loss of ARP2/3-based lamellipodia and increased numbers of filopodia
    • Mejillano, M. R. et al. Lamellipodial versus filopodial mode of the actin nanomachinery: pivotal role of the filament barbed end. Cell 118, 363-373 (2004). Shows that loss of CP in migrating cultured cells leads to loss of ARP2/3-based lamellipodia and increased numbers of filopodia.
    • (2004) Cell , vol.118 , pp. 363-373
    • Mejillano, M.R.1
  • 13
    • 0019256032 scopus 로고
    • An actin-binding protein from acanthamoeba regulates actin filament polymerization and interactions
    • Discovers CP by biochemical purification from A. castellanii
    • Isenberg, G., Aebi, U., & Pollard, T. D. An actin-binding protein from Acanthamoeba regulates actin filament polymerization and interactions. Nature 288, 455-459 (1980). Discovers CP by biochemical purification from A. castellanii.
    • (1980) Nature , vol.288 , pp. 455-459
    • Isenberg, G.1    Aebi, U.2    Pollard, T.D.3
  • 14
    • 0023372284 scopus 로고
    • Cap z(36/32) a barbed end actin-capping protein is a component of the z-line of skeletal muscle
    • Casella, J. F., Craig, S. W., Maack, D. J., & Brown, A. E. Cap Z(36/32), a barbed end actin-capping protein, is a component of the Z-line of skeletal muscle. J. Cell Biol. 105, 371-379 (1987
    • (1987) J. Cell Biol. , vol.105 , pp. 371-379
    • Casella, J.F.1    Craig, S.W.2    Maack, D.J.3    Brown, A.E.4
  • 15
    • 0025333992 scopus 로고
    • Actinin is equivalent to cap z protein
    • Maruyama, K. et al. ?-Actinin is equivalent to Cap Z protein. J. Biol. Chem. 265, 8712-8715 (1990
    • (1990) J. Biol. Chem. , vol.265 , pp. 8712-8715
    • Maruyama, K.1
  • 16
    • 0001604571 scopus 로고
    • New actin-binding proteins from dictyostelium discoideum
    • Schleicher, M., Gerisch, G., & Isenberg, G. New actin-binding proteins from Dictyostelium discoideum. EMBO J. 3, 2095-2100 (1984
    • (1984) EMBO J. , vol.3 , pp. 2095-2100
    • Schleicher, M.1    Gerisch, G.2    Isenberg, G.3
  • 18
    • 84864861249 scopus 로고    scopus 로고
    • Multifunctional roles of gelsolin in health and diseases
    • Li, G. H., Arora, P. D., Chen, Y., McCulloch, C. A., & Liu, P. Multifunctional roles of gelsolin in health and diseases. Med. Res. Rev. 32, 999-1025 (2012
    • (2012) Med. Res. Rev. , vol.32 , pp. 999-1025
    • Li, G.H.1    Arora, P.D.2    Chen, Y.3    McCulloch, C.A.4    Liu, P.5
  • 19
    • 84887185966 scopus 로고    scopus 로고
    • The human erythrocyte plasma membrane: A rosetta stone for decoding membrane-cytoskeleton structure
    • Fowler, V. M. The human erythrocyte plasma membrane: a Rosetta Stone for decoding membrane-cytoskeleton structure. Curr. Top. Membr. 72, 39-88 (2013
    • (2013) Curr. Top. Membr. , vol.72 , pp. 39-88
    • Fowler, V.M.1
  • 20
    • 10344233664 scopus 로고    scopus 로고
    • There goes the neighbourhood: Eps8 joins the barbed-end crowd
    • Higgs, H. N. There goes the neighbourhood: Eps8 joins the barbed-end crowd. Nature Cell Biol. 6, 1147-1149 (2004
    • (2004) Nature Cell Biol. , vol.6 , pp. 1147-1149
    • Higgs, H.N.1
  • 21
    • 84882891890 scopus 로고    scopus 로고
    • Membrane and actin dynamics interplay at lamellipodia leading edge
    • Bisi, S. et al. Membrane and actin dynamics interplay at lamellipodia leading edge. Curr. Opin. Cell Biol. 25, 565-573 (2013
    • (2013) Curr. Opin. Cell Biol. , vol.25 , pp. 565-573
    • Bisi, S.1
  • 22
    • 33745842895 scopus 로고    scopus 로고
    • Identification of a novel inhibitory actin-capping protein binding motif in cd2-Associated protein
    • Identifies the CPI motif by analysis of CD2AP
    • Bruck, S. et al. Identification of a novel inhibitory actin-capping protein binding motif in CD2-Associated protein. J. Biol. Chem. 281, 19196-19203 (2006). Identifies the CPI motif by analysis of CD2AP.
    • (2006) J. Biol. Chem. , vol.281 , pp. 19196-19203
    • Bruck, S.1
  • 23
    • 77950500990 scopus 로고    scopus 로고
    • Structural characterization of a capping protein interaction motif defines a family of actin filament regulators
    • The structural and biochemical analysis of complexes of CPI and CSI motifs with CP
    • Hernandez-Valladares, M. et al. Structural characterization of a capping protein interaction motif defines a family of actin filament regulators. Nature Struct. Mol. Biol. 17, 497-503 (2010). The structural and biochemical analysis of complexes of CPI and CSI motifs with CP.
    • (2010) Nature Struct. Mol. Biol. , vol.17 , pp. 497-503
    • Hernandez-Valladares, M.1
  • 24
    • 0033552611 scopus 로고    scopus 로고
    • Vertebrate isoforms of actin capping protein ? Have distinct functions in vivo
    • Hart, M. C., & Cooper, J. A. Vertebrate isoforms of actin capping protein ? have distinct functions In vivo. J. Cell Biol. 147, 1287-1298 (1999
    • (1999) J. Cell Biol. , vol.147 , pp. 1287-1298
    • Hart, M.C.1    Cooper, J.A.2
  • 25
    • 0028891855 scopus 로고
    • Inhibition of capz during myofibrillogenesis alters assembly of actin filaments
    • Schafer, D. A. Inhibition of CapZ during myofibrillogenesis alters assembly of actin filaments. J. Cell Biol. 128, 61-70 (1995
    • (1995) J. Cell Biol. , vol.128 , pp. 61-70
    • Schafer, D.A.1
  • 26
    • 0027959864 scopus 로고
    • Differential localization and sequence analysis of capping protein ?-subunit isoforms of vertebrates
    • Schafer, D. A., Korshunova, Y. O., Schroer, T. A., & Cooper, J. A. Differential localization and sequence analysis of capping protein ?-subunit isoforms of vertebrates. J. Cell Biol. 127, 453-465 (1994
    • (1994) J. Cell Biol. , vol.127 , pp. 453-465
    • Schafer, D.A.1    Korshunova, Y.O.2    Schroer, T.A.3    Cooper, J.A.4
  • 27
    • 81255199170 scopus 로고    scopus 로고
    • Cease-fire at the leading edge: New perspectives on actin filament branching, debranching, and cross-linking
    • Ydenberg, C. A., Smith, B. A., Breitsprecher, D., Gelles, J., & Goode, B. L. Cease-fire at the leading edge: new perspectives on actin filament branching, debranching, and cross-linking. Cytoskeleton 68, 596-602 (2011
    • (2011) Cytoskeleton , vol.68 , pp. 596-602
    • Ydenberg, C.A.1    Smith, B.A.2    Breitsprecher, D.3    Gelles, J.4    Goode, B.L.5
  • 28
    • 33845700946 scopus 로고    scopus 로고
    • Actin turnover-dependent fast dissociation of capping protein in the dendritic nucleation actin network: Evidence of frequent filament severing
    • Miyoshi, T. et al. Actin turnover-dependent fast dissociation of capping protein in the dendritic nucleation actin network: evidence of frequent filament severing. J. Cell Biol. 175, 947-955 (2006
    • (2006) J. Cell Biol. , vol.175 , pp. 947-955
    • Miyoshi, T.1
  • 29
    • 33847315536 scopus 로고    scopus 로고
    • Spatial and temporal relationships between actin-filament nucleation, capping, and disassembly
    • Iwasa, J. H., & Mullins, R. D. Spatial and temporal relationships between actin-filament nucleation, capping, and disassembly. Curr. Biol. 17, 395-406 (2007
    • (2007) Curr. Biol. , vol.17 , pp. 395-406
    • Iwasa, J.H.1    Mullins, R.2
  • 30
    • 43949143882 scopus 로고    scopus 로고
    • Capping protein increases the rate of actin-based motility by promoting filament nucleation by the arp2/3 complex
    • Akin, O., & Mullins, R. D. Capping protein increases the rate of actin-based motility by promoting filament nucleation by the Arp2/3 complex. Cell 133, 841-851 (2008
    • (2008) Cell , vol.133 , pp. 841-851
    • Akin, O.1    Mullins, R.D.2
  • 31
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard, T. D., & Borisy, G. G. Cellular motility driven by assembly and disassembly of actin filaments. Cell 112, 453-465 (2003
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 32
    • 34249028789 scopus 로고    scopus 로고
    • Analysis of actin filament network organization in lamellipodia by comparing experimental and simulated images
    • Schaub, S., Meister, J. J., & Verkhovsky, A. B. Analysis of actin filament network organization in lamellipodia by comparing experimental and simulated images. J. Cell Sci. 120, 1491-1500 (2007
    • (2007) J. Cell Sci. , vol.120 , pp. 1491-1500
    • Schaub, S.1    Meister, J.J.2    Verkhovsky, A.B.3
  • 33
    • 84859420307 scopus 로고    scopus 로고
    • Actin branching in the initiation and maintenance of lamellipodia
    • Vinzenz, M. et al. Actin branching in the initiation and maintenance of lamellipodia. J. Cell Sci. 125, 2775-2785 (2012
    • (2012) J. Cell Sci. , vol.125 , pp. 2775-2785
    • Vinzenz, M.1
  • 34
    • 77952896939 scopus 로고    scopus 로고
    • Control of actin filament treadmilling in cell motility
    • Bugyi, B., & Carlier, M. F. Control of actin filament treadmilling in cell motility. Annu. Rev. Biophys. 39, 449-470 (2010
    • (2010) Annu. Rev. Biophys. , vol.39 , pp. 449-470
    • Bugyi, B.1    Carlier, M.F.2
  • 35
    • 41949088527 scopus 로고    scopus 로고
    • Arp2/3 complex interactions and actin network turnover in lamellipodia
    • Lai, F. P. et al. Arp2/3 complex interactions and actin network turnover in lamellipodia. EMBO J. 27, 982-992 (2008
    • (2008) EMBO J. , vol.27 , pp. 982-992
    • Lai, F.P.1
  • 36
    • 0037387121 scopus 로고    scopus 로고
    • Crystal structure of capz: Structural basis for actin filament barbed end capping
    • Reveals the crystal structure of CP and proposes a model for barbed-end capping
    • Yamashita, A., Maeda, K., & Maeda, Y. Crystal structure of CapZ: structural basis for actin filament barbed end capping. EMBO J. 22, 1529-1538 (2003). Reveals the crystal structure of CP and proposes a model for barbed-end capping.
    • (2003) EMBO J. , vol.22 , pp. 1529-1538
    • Yamashita, A.1    Maeda, K.2    Maeda, Y.3
  • 37
    • 0030064644 scopus 로고    scopus 로고
    • Mutational analysis of capping protein function in saccharomyces cerevisiae
    • Sizonenko, G. I., Karpova, T. S., Gattermeir, D. J., & Cooper, J. A. Mutational analysis of capping protein function in Saccharomyces cerevisiae. Mol. Biol. Cell 7, 1-15 (1996
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1-15
    • Sizonenko, G.I.1    Karpova, T.S.2    Gattermeir, D.J.3    Cooper, J.A.4
  • 38
    • 0029795850 scopus 로고    scopus 로고
    • Dynamics of capping protein and actin assembly in vitro: Uncapping barbed ends by polyphosphoinositides
    • Reports dynamic uncapping of CP by polyphosphoinositides
    • Schafer, D. A., Jennings, P. B., & Cooper, J. A. Dynamics of capping protein and actin assembly in vitro: uncapping barbed ends by polyphosphoinositides. J. Cell Biol. 135, 169-179 (1996). Reports dynamic uncapping of CP by polyphosphoinositides.
    • (1996) J. Cell Biol. , vol.135 , pp. 169-179
    • Schafer, D.A.1    Jennings, P.B.2    Cooper, J.A.3
  • 39
    • 78649529338 scopus 로고    scopus 로고
    • The interaction of capping protein with the barbed end of the actin filament
    • Kim, T., Cooper, J. A., & Sept, D. The interaction of capping protein with the barbed end of the actin filament. J. Mol. Biol. 404, 794-802 (2010
    • (2010) J. Mol. Biol. , vol.404 , pp. 794-802
    • Kim, T.1    Cooper, J.A.2    Sept, D.3
  • 40
    • 0042420366 scopus 로고    scopus 로고
    • How capping protein binds the barbed end of the actin filament
    • Wear, M. A., Yamashita, A., Kim, K., Maeda, Y., & Cooper, J. A. How capping protein binds the barbed end of the actin filament. Curr. Biol. 13, 1531-1537 (2003
    • (2003) Curr. Biol. , vol.13 , pp. 1531-1537
    • Wear, M.A.1    Yamashita, A.2    Kim, K.3    Maeda, Y.4    Cooper, J.A.5
  • 41
    • 33751531532 scopus 로고    scopus 로고
    • Molecular determination by electron microscopy of the actin filament end structure
    • Narita, A., & Maeda, Y. Molecular determination by electron microscopy of the actin filament end structure. J. Mol. Biol. 365, 480-501 (2007
    • (2007) J. Mol. Biol. , vol.365 , pp. 480-501
    • Narita, A.1    Maeda, Y.2
  • 42
    • 33751567905 scopus 로고    scopus 로고
    • Structural basis of actin filament capping at the barbed-end: A cryo-electron microscopy study
    • Narita, A., Takeda, S., Yamashita, A., & Maeda, Y. Structural basis of actin filament capping at the barbed-end: a cryo-electron microscopy study. EMBO J. 25, 5626-5633 (2006
    • (2006) EMBO J. , vol.25 , pp. 5626-5633
    • Narita, A.1    Takeda, S.2    Yamashita, A.3    Maeda, Y.4
  • 44
    • 0142136092 scopus 로고    scopus 로고
    • Formin leaky cap allows elongation in the presence of tight capping proteins
    • Zigmond, S. H. et al. Formin leaky cap allows elongation in the presence of tight capping proteins. Curr. Biol. 13, 1820-1823 (2003
    • (2003) Curr. Biol. , vol.13 , pp. 1820-1823
    • Zigmond, S.H.1
  • 45
    • 77955927654 scopus 로고    scopus 로고
    • Phospholipids regulate localization and activity of mdia1 formin
    • Ramalingam, N. et al. Phospholipids regulate localization and activity of mDia1 formin. Eur. J. Cell Biol. 89, 723-732 (2010
    • (2010) Eur. J. Cell Biol. , vol.89 , pp. 723-732
    • Ramalingam, N.1
  • 46
    • 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. Mechanisms of plasma membrane targeting of formin mDia2 through its amino terminal domains. Mol. Biol. Cell 22, 189-201 (2011
    • (2011) Mol. Biol. Cell , vol.22 , pp. 189-201
    • Gorelik, R.1    Yang, C.2    Kameswaran, V.3    Dominguez, R.4    Svitkina, T.5
  • 47
    • 0030911424 scopus 로고    scopus 로고
    • P140mdia, a mammalian homolog of drosophila diaphanous, is a target protein for rho small gtpase and is a ligand for profilin
    • Watanabe, N. et al. p140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin. EMBO J. 16, 3044-3056 (1997
    • (1997) EMBO J. , vol.16 , pp. 3044-3056
    • Watanabe, N.1
  • 48
    • 0030932405 scopus 로고    scopus 로고
    • Bni1p, a yeast formin linking cdc42p and the actin cytoskeleton during polarized morphogenesis
    • Evangelista, M. et al. Bni1p, a yeast formin linking cdc42p and the actin cytoskeleton during polarized morphogenesis. Science 276, 118-122 (1997
    • (1997) Science , vol.276 , pp. 118-122
    • Evangelista, M.1
  • 49
    • 0043202969 scopus 로고    scopus 로고
    • The mouse formin mdia1 is a potent actin nucleation factor regulated by autoinhibition
    • Li, F., & Higgs, H. N. The mouse formin mDia1 is a potent actin nucleation factor regulated by autoinhibition. Curr. Biol. 13, 1335-1340 (2003
    • (2003) Curr. Biol. , vol.13 , pp. 1335-1340
    • Li, F.1    Higgs, H.N.2
  • 50
    • 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. Nature Rev. Mol. Cell Biol. 11, 62-74 (2010
    • (2010) Nature Rev. Mol. Cell Biol. , vol.11 , pp. 62-74
    • Chesarone, M.A.1    Dupage, A.G.2    Goode, B.L.3
  • 51
    • 84867477942 scopus 로고    scopus 로고
    • Actin-capping protein promotes microtubule stability by antagonizing the actin activity of mdia1
    • Bartolini, F., Ramalingam, N., & Gundersen, G. G. Actin-capping protein promotes microtubule stability by antagonizing the actin activity of mDia1. Mol. Biol. Cell 23, 4032-4040 (2012
    • (2012) Mol. Biol. Cell , vol.23 , pp. 4032-4040
    • Bartolini, F.1    Ramalingam, N.2    Gundersen, G.G.3
  • 52
    • 67749135871 scopus 로고    scopus 로고
    • Review of the mechanism of processive actin filament elongation by formins
    • Paul, A. S., & Pollard, T. D. Review of the mechanism of processive actin filament elongation by formins. Cell. Motil. Cytoskeleton 66, 606-617 (2009
    • (2009) Cell. Motil. Cytoskeleton , vol.66 , pp. 606-617
    • Paul, A.S.1    Pollard, T.D.2
  • 53
    • 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. 76, 593-627 (2007
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 593-627
    • Goode, B.L.1    Eck, M.2
  • 54
    • 46549086642 scopus 로고    scopus 로고
    • Ena/vasp: Proteins at the tip of the nervous system
    • Drees, F., & Gertler, F. B. Ena/VASP: proteins at the tip of the nervous system. Curr. Opin. Neurobiol. 18, 53-59 (2008
    • (2008) Curr. Opin. Neurobiol. , vol.18 , pp. 53-59
    • Drees, F.1    Gertler, F.B.2
  • 55
    • 0037048683 scopus 로고    scopus 로고
    • The vasodilator-stimulated phosphoprotein promotes actin polymerisation through direct binding to monomeric actin
    • Walders-Harbeck, B., Khaitlina, S. Y., Hinssen, H., Jockusch, B. M., & Illenberger, S. The vasodilator-stimulated phosphoprotein promotes actin polymerisation through direct binding to monomeric actin. FEBS Lett. 529, 275-280 (2002
    • (2002) FEBS Lett. , vol.529 , pp. 275-280
    • Walders-Harbeck, B.1    Khaitlina, S.Y.2    Hinssen, H.3    Jockusch, B.M.4    Illenberger, S.5
  • 56
    • 33746860849 scopus 로고    scopus 로고
    • Understanding the role of the g-Actin-binding domain of ena/vasp in actin assembly
    • Chereau, D., & Dominguez, R. Understanding the role of the G-Actin-binding domain of Ena/VASP in actin assembly. J. Struct. Biol. 155, 195-201 (2006
    • (2006) J. Struct. Biol. , vol.155 , pp. 195-201
    • Chereau, D.1    Dominguez, R.2
  • 57
    • 18444389953 scopus 로고    scopus 로고
    • Antagonism between ena/vasp proteins and actin filament capping regulates fibroblast motility
    • Bear, J. E. et al. Antagonism between Ena/VASP proteins and actin filament capping regulates fibroblast motility. Cell 109, 509-521 (2002
    • (2002) Cell , vol.109 , pp. 509-521
    • Bear, J.E.1
  • 58
    • 23344442354 scopus 로고    scopus 로고
    • Ena/vasp proteins enhance actin polymerization in the presence of barbed end capping proteins
    • Shows that ENA/VASP proteins promote elongation in the presence of CP
    • Barzik, M. et al. Ena/VASP proteins enhance actin polymerization in the presence of barbed end capping proteins. J. Biol. Chem. 280, 28653-28662 (2005). Shows that ENA/VASP proteins promote elongation in the presence of CP.
    • (2005) J. Biol. Chem. , vol.280 , pp. 28653-28662
    • Barzik, M.1
  • 59
    • 56549108193 scopus 로고    scopus 로고
    • Clustering of vasp actively drives processive wh2 domain-mediated actin filament elongation
    • Breitsprecher, D. et al. Clustering of VASP actively drives processive, WH2 domain-mediated actin filament elongation. EMBO J. 27, 2943-2954 (2008
    • (2008) EMBO J. , vol.27 , pp. 2943-2954
    • Breitsprecher, D.1
  • 60
    • 79551578685 scopus 로고    scopus 로고
    • Molecular mechanism of ena/vasp-mediated actin-filament elongation
    • Breitsprecher, D. et al. Molecular mechanism of Ena/VASP-mediated actin-filament elongation. EMBO J. 30, 456-467 (2011
    • (2011) EMBO J. , vol.30 , pp. 456-467
    • Breitsprecher, D.1
  • 61
    • 78049521359 scopus 로고    scopus 로고
    • Vasp is a processive actin polymerase that requires monomeric actin for barbed end association
    • Hansen, S. D., & Mullins, R. D. VASP is a processive actin polymerase that requires monomeric actin for barbed end association. J. Cell Biol. 191, 571-584 (2010
    • (2010) J. Cell Biol. , vol.191 , pp. 571-584
    • Hansen, S.D.1    Mullins, R.D.2
  • 62
    • 84896519018 scopus 로고    scopus 로고
    • Ena/vasp enabled is a highly processive actin polymerase tailored to self-Assemble parallel-bundled f-Actin networks with fascin
    • Winkelman, J. D., Bilancia, C. G., Peifer, M., & Kovar, D. R. Ena/VASP Enabled is a highly processive actin polymerase tailored to self-Assemble parallel-bundled F-Actin networks with Fascin. Proc. Natl Acad. Sci. USA 111, 4121-4126 (2014
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 4121-4126
    • Winkelman, J.D.1    Bilancia, C.G.2    Peifer, M.3    Kovar, D.R.4
  • 63
    • 0030710460 scopus 로고    scopus 로고
    • Structure of the profilin-poly-l-proline complex involved in morphogenesis and cytoskeletal regulation
    • Mahoney, N. M., Janmey, P. A., & Almo, S. C. Structure of the profilin-poly-l-proline complex involved in morphogenesis and cytoskeletal regulation. Nature Struct. Biol. 4, 953-960 (1997
    • (1997) Nature Struct. Biol. , vol.4 , pp. 953-960
    • Mahoney, N.M.1    Janmey, P.A.2    Almo, S.C.3
  • 64
    • 35649021883 scopus 로고    scopus 로고
    • Structural basis for the recruitment of profilin-Actin complexes during filament elongation by ena/vasp
    • Ferron, F., Rebowski, G., Lee, S. H., & Dominguez, R. Structural basis for the recruitment of profilin-Actin complexes during filament elongation by Ena/VASP. EMBO J. 26, 4597-4606 (2007
    • (2007) EMBO J. , vol.26 , pp. 4597-4606
    • Ferron, F.1    Rebowski, G.2    Lee, S.H.3    Dominguez, R.4
  • 65
    • 44349090393 scopus 로고    scopus 로고
    • Ena/vasp proteins capture actin filament barbed ends
    • Pasic, L., Kotova, T., & Schafer, D. A. Ena/VASP proteins capture actin filament barbed ends. J. Biol. Chem. 283, 9814-9819 (2008
    • (2008) J. Biol. Chem. , vol.283 , pp. 9814-9819
    • Pasic, L.1    Kotova, T.2    Schafer, D.A.3
  • 66
    • 0032524455 scopus 로고    scopus 로고
    • The structural basis of ankyrin-like repeat function as revealed by the solution structure of myotrophin
    • Yang, Y., Nanduri, S., Sen, S., & Qin, J. The structural basis of ankyrin-like repeat function as revealed by the solution structure of myotrophin. Structure 6, 619-626 (1998
    • (1998) Structure , vol.6 , pp. 619-626
    • Yang, Y.1    Nanduri, S.2    Sen, S.3    Qin, J.4
  • 67
    • 0037458625 scopus 로고    scopus 로고
    • V-1, a protein expressed transiently during murine cerebellar development, regulates actin polymerization via interaction with capping protein
    • Reports that V-1 interacts with CP
    • Taoka, M. et al. V-1, a protein expressed transiently during murine cerebellar development, regulates actin polymerization via interaction with capping protein. J. Biol. Chem. 278, 5864-5870 (2003). Reports that V-1 interacts with CP.
    • (2003) J. Biol. Chem. , vol.278 , pp. 5864-5870
    • Taoka, M.1
  • 68
    • 0028241537 scopus 로고
    • Murine cerebellar neurons express a novel gene encoding a protein related to cell cycle control and cell fate determination proteins
    • Taoka, M. et al. Murine cerebellar neurons express a novel gene encoding a protein related to cell cycle control and cell fate determination proteins. J. Biol. Chem. 269, 9946-9951 (1994
    • (1994) J. Biol. Chem. , vol.269 , pp. 9946-9951
    • Taoka, M.1
  • 69
    • 0025131865 scopus 로고
    • Myotrophin: Purification of a novel peptide from spontaneously hypertensive rat heart that influences myocardial growth
    • Sen, S. et al. Myotrophin: purification of a novel peptide from spontaneously hypertensive rat heart that influences myocardial growth. J. Biol. Chem. 265, 16635-16643 (1990
    • (1990) J. Biol. Chem. , vol.265 , pp. 16635-16643
    • Sen, S.1
  • 70
    • 0027254445 scopus 로고
    • Myotrophin in human cardiomyopathic heart
    • Sil, P., Misono, K., & Sen, S. Myotrophin in human cardiomyopathic heart. Circ. Res. 73, 98-108 (1993
    • (1993) Circ. Res. , vol.73 , pp. 98-108
    • Sil, P.1    Misono, K.2    Sen, S.3
  • 71
    • 0029077050 scopus 로고
    • Quantification of myotrophin from spontaneously hypertensive and normal rat hearts
    • Sil, P., Mukherjee, D., & Sen, S. Quantification of myotrophin from spontaneously hypertensive and normal rat hearts. Circ. Res. 76, 1020-1027 (1995
    • (1995) Circ. Res. , vol.76 , pp. 1020-1027
    • Sil, P.1    Mukherjee, D.2    Sen, S.3
  • 72
    • 0037164814 scopus 로고    scopus 로고
    • Activation of nuclear factor-?b is necessary for myotrophin-induced cardiac hypertrophy
    • Gupta, S., Purcell, N. H., Lin, A., & Sen, S. Activation of nuclear factor-?B is necessary for myotrophin-induced cardiac hypertrophy. J. Cell Biol. 159, 1019-1028 (2002
    • (2002) J. Cell Biol. , vol.159 , pp. 1019-1028
    • Gupta, S.1    Purcell, N.H.2    Lin, A.3    Sen, S.4
  • 73
    • 55549106135 scopus 로고    scopus 로고
    • Nuclear co-translocation of myotrophin and p65 stimulates myocyte growth. Regulation by myotrophin hairpin loops
    • Das, B. et al. Nuclear co-translocation of myotrophin and p65 stimulates myocyte growth. Regulation by myotrophin hairpin loops. J. Biol. Chem. 283, 27947-27956 (2008
    • (2008) J. Biol. Chem. , vol.283 , pp. 27947-27956
    • Das, B.1
  • 74
    • 68049102296 scopus 로고    scopus 로고
    • Silencing the myotrophin gene by rna interference leads to the regression of cardiac hypertrophy
    • Gupta, S., Maitra, R., Young, D., Gupta, A., & Sen, S. Silencing the myotrophin gene by RNA interference leads to the regression of cardiac hypertrophy. Am. J. Physiol. Heart Circ. Physiol. 297, H627-H636 (2009
    • (2009) Am. J. Physiol. Heart Circ. Physiol. , vol.297 , pp. H627-H636
    • Gupta, S.1    Maitra, R.2    Young, D.3    Gupta, A.4    Sen, S.5
  • 75
    • 33750063180 scopus 로고    scopus 로고
    • Binding of myotrophin/v-1 to actin-capping protein: Implications for how capping protein binds to the filament barbed end
    • Bhattacharya, N., Ghosh, S., Sept, D., & Cooper, J. A. Binding of myotrophin/V-1 to actin-capping protein: implications for how capping protein binds to the filament barbed end. J. Biol. Chem. 281, 31021-31030 (2006
    • (2006) J. Biol. Chem. , vol.281 , pp. 31021-31030
    • Bhattacharya, N.1    Ghosh, S.2    Sept, D.3    Cooper, J.A.4
  • 76
    • 77955488192 scopus 로고    scopus 로고
    • Structural basis for capping protein sequestration by myotrophin v-1)
    • Reveals the mechanism of V-1 interaction with CP
    • Zwolak, A., Fujiwara, I., Hammer, J. A., & Tjandra, N. Structural basis for capping protein sequestration by myotrophin (V-1). J. Biol. Chem. 285, 25767-25781 (2010). Reveals the mechanism of V-1 interaction with CP.
    • (2010) J. Biol. Chem. , vol.285 , pp. 25767-25781
    • Zwolak, A.1    Fujiwara, I.2    Hammer, J.A.3    Tjandra, N.4
  • 77
    • 77955014560 scopus 로고    scopus 로고
    • Two distinct mechanisms for actin capping protein regulation - Steric and allosteric inhibition
    • Identified contrasting steric and allosteric mechanisms to regulate CP
    • Takeda, S. et al. Two distinct mechanisms for actin capping protein regulation - steric and allosteric inhibition. PLoS Biol. 8, e1000416 (2010). Identified contrasting steric and allosteric mechanisms to regulate CP.
    • (2010) PLoS Biol. , vol.8 , pp. e1000416
    • Takeda, S.1
  • 78
    • 0038311944 scopus 로고    scopus 로고
    • Phosphoinositide regulation of the actin cytoskeleton
    • Yin, H. L., & Janmey, P. A. Phosphoinositide regulation of the actin cytoskeleton. Annu. Rev. Physiol. 65, 761-789 (2003
    • (2003) Annu. Rev. Physiol. , vol.65 , pp. 761-789
    • Yin, H.L.1    Janmey, P.A.2
  • 79
    • 74949100104 scopus 로고    scopus 로고
    • Regulation of the actin cytoskeleton-plasma membrane interplay by phosphoinositides
    • Saarikangas, J., Zhao, H., & Lappalainen, P. Regulation of the actin cytoskeleton-plasma membrane interplay by phosphoinositides. Physiol. Rev. 90, 259-289 (2010
    • (2010) Physiol. Rev. , vol.90 , pp. 259-289
    • Saarikangas, J.1    Zhao, H.2    Lappalainen, P.3
  • 80
    • 0025748580 scopus 로고
    • Regulation of capz, an actin capping protein of chicken muscle, by anionic phospholipids
    • Heiss, S. G., & Cooper, J. A. Regulation of CapZ, an actin capping protein of chicken muscle, by anionic phospholipids. Biochemistry 30, 8753-8758 (1991
    • (1991) Biochemistry , vol.30 , pp. 8753-8758
    • Heiss, S.G.1    Cooper, J.A.2
  • 81
    • 34247173028 scopus 로고    scopus 로고
    • Structure/function analysis of the interaction of phosphatidylinositol 4,5-bisphosphate with actin-capping protein: Implications for how capping protein binds the actin filament
    • Kim, K. et al. Structure/function analysis of the interaction of phosphatidylinositol 4,5-bisphosphate with actin-capping protein: implications for how capping protein binds the actin filament. J. Biol. Chem. 282, 5871-5879 (2007
    • (2007) J. Biol. Chem. , vol.282 , pp. 5871-5879
    • Kim, K.1
  • 82
    • 34948838501 scopus 로고    scopus 로고
    • Single molecule kinetic analysis of actin filament capping. Polyphosphoinositides do not dissociate capping proteins
    • Kuhn, J. R., & Pollard, T. D. Single molecule kinetic analysis of actin filament capping. Polyphosphoinositides do not dissociate capping proteins. J. Biol. Chem. 282, 28014-28024 (2007
    • (2007) J. Biol. Chem. , vol.282 , pp. 28014-28024
    • Kuhn, J.R.1    Pollard, T.D.2
  • 83
    • 84868154444 scopus 로고    scopus 로고
    • Capping protein modulates the dynamic behavior of actin filaments in response to phosphatidic acid in arabidopsis
    • Li, J. et al. Capping protein modulates the dynamic behavior of actin filaments in response to phosphatidic acid in Arabidopsis. Plant Cell 24, 3742-3754 (2012
    • (2012) Plant Cell , vol.24 , pp. 3742-3754
    • Li, J.1
  • 84
    • 0028790030 scopus 로고
    • Identification of acan125 as a myosin-i-binding protein present with myosin-i on cellular organelles of acanthamoeba
    • Discovers Acan125, the first CARMIL, in A. castellanii
    • Xu, P., Zot, A. S., & Zot, H. G. Identification of Acan125 as a myosin-I-binding protein present with myosin-I on cellular organelles of Acanthamoeba. J. Biol. Chem. 270, 25316-25319 (1995). Discovers Acan125, the first CARMIL, in A. castellanii.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25316-25319
    • Xu, P.1    Zot, A.S.2    Zot, H.G.3
  • 85
    • 0035954433 scopus 로고    scopus 로고
    • The dictyostelium carmil protein links capping protein and the arp2/3 complex to type i myosins through their sh3 domains
    • Characterizes D. discoideum CARMIL interactions and mutant phenotypes
    • Jung, G., Remmert, K., Wu, X., Volosky, J. M., & Hammer, J. A. The Dictyostelium CARMIL protein links capping protein and the Arp2/3 complex to type I myosins through their SH3 domains. J. Cell Biol. 153, 1479-1497 (2001). Characterizes D. discoideum CARMIL interactions and mutant phenotypes.
    • (2001) J. Cell Biol. , vol.153 , pp. 1479-1497
    • Jung, G.1    Remmert, K.2    Wu, X.3    Volosky, J.M.4    Hammer, J.A.5
  • 86
    • 22944474598 scopus 로고    scopus 로고
    • Mammalian carmil inhibits actin filament capping by capping protein
    • Shows that mammalian CARMIL inhibits CP and causes uncapping. Also shows that the CARMIL1-CP complex retains capping activity, which suggests an allosteric mechanism
    • Yang, C. et al. Mammalian CARMIL inhibits actin filament capping by capping protein. Dev. Cell 9, 209-221 (2005). Shows that mammalian CARMIL inhibits CP and causes uncapping. Also shows that the CARMIL1-CP complex retains capping activity, which suggests an allosteric mechanism.
    • (2005) Dev. Cell , vol.9 , pp. 209-221
    • Yang, C.1
  • 87
    • 73849090221 scopus 로고    scopus 로고
    • Distinct roles for carmil isoforms in cell migration
    • Reports that CARMIL1 and CARMIL2 have distinct functions in vertebrate cells
    • Liang, Y., Niederstrasser, H., Edwards, M., Jackson, C. E., & Cooper, J. A. Distinct roles for CARMIL isoforms in cell migration. Mol. Biol. Cell 20, 5290-5305 (2009). Reports that CARMIL1 and CARMIL2 have distinct functions in vertebrate cells.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 5290-5305
    • Liang, Y.1    Niederstrasser, H.2    Edwards, M.3    Jackson, C.E.4    Cooper, J.A.5
  • 88
    • 84900516894 scopus 로고    scopus 로고
    • Capping protein regulatory cycle driven by carmil and v-1 may promote actin network assembly at protruding edges
    • Fujiwara, I., Remmert, K., Piszczek, G., & Hammer, J. A. Capping protein regulatory cycle driven by CARMIL and V-1 may promote actin network assembly at protruding edges. Proc. Natl Acad. Sci. USA 111, E1970-E1979 (2014
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. E1970-E1979
    • Fujiwara, I.1    Remmert, K.2    Piszczek, G.3    Hammer, J.A.4
  • 89
    • 84884792947 scopus 로고    scopus 로고
    • Physiological role of the interaction between carmil1 and capping protein
    • Shows the physiological relevance of the CARMIL1-CP interaction
    • Edwards, M., Liang, Y., Kim, T., & Cooper, J. A. Physiological role of the interaction between CARMIL1 and capping protein. Mol. Biol. Cell 24, 3047-3055 (2013). Shows the physiological relevance of the CARMIL1-CP interaction.
    • (2013) Mol. Biol. Cell , vol.24 , pp. 3047-3055
    • Edwards, M.1    Liang, Y.2    Kim, T.3    Cooper, J.A.4
  • 90
    • 77949319432 scopus 로고    scopus 로고
    • An experimentally based computer search identifies unstructured membrane-binding sites in proteins: Application to class i myosins paks, and carmil
    • Brzeska, H., Guag, J., Remmert, K., Chacko, S., & Korn, E. D. An experimentally based computer search identifies unstructured membrane-binding sites in proteins: application to class I myosins, PAKS, and CARMIL. J. Biol. Chem. 285, 5738-5747 (2010
    • (2010) J. Biol. Chem. , vol.285 , pp. 5738-5747
    • Brzeska, H.1    Guag, J.2    Remmert, K.3    Chacko, S.4    Korn, E.D.5
  • 91
    • 79954569217 scopus 로고    scopus 로고
    • Vimentin organization modulates the formation of lamellipodia
    • Helfand, B. T. et al. Vimentin organization modulates the formation of lamellipodia. Mol. Biol. Cell 22, 1274-1289 (2011
    • (2011) Mol. Biol. Cell , vol.22 , pp. 1274-1289
    • Helfand, B.T.1
  • 92
    • 34548472221 scopus 로고    scopus 로고
    • Gef what? Dock180 and related proteins help rac to polarize cells in new ways
    • Cote, J. F., & Vuori, K. GEF what? Dock180 and related proteins help Rac to polarize cells in new ways. Trends Cell Biol. 17, 383-393 (2007
    • (2007) Trends Cell Biol. , vol.17 , pp. 383-393
    • Cote, J.F.1    Vuori, K.2
  • 93
    • 79951517321 scopus 로고    scopus 로고
    • Identifying lrrc16b as an oncofetal gene with transforming enhancing capability using a combined bioinformatics and experimental approach
    • Hsu, C. C. et al. Identifying LRRC16B as an oncofetal gene with transforming enhancing capability using a combined bioinformatics and experimental approach. Oncogene 30, 654-667 (2011
    • (2011) Oncogene , vol.30 , pp. 654-667
    • Hsu, C.C.1
  • 94
    • 84885148208 scopus 로고    scopus 로고
    • Carmil leading edge localization depends on a non-canonical ph domain and dimerization
    • Determines the structure of a large N-terminal fragment of CARMIL, and identifies and characterizes the PH and HD domains
    • Zwolak, A. et al. CARMIL leading edge localization depends on a non-canonical PH domain and dimerization. Nature Commun. 4, 2523 (2013). Determines the structure of a large N-terminal fragment of CARMIL, and identifies and characterizes the PH and HD domains.
    • (2013) Nature Commun. , vol.4 , pp. 2523
    • Zwolak, A.1
  • 95
    • 0035692811 scopus 로고    scopus 로고
    • The leucine-rich repeat as a protein recognition motif
    • Kobe, B., & Kajava, A. V. The leucine-rich repeat as a protein recognition motif. Curr. Opin. Struct. Biol. 11, 725-732 (2001
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 725-732
    • Kobe, B.1    Kajava, A.V.2
  • 97
    • 0033521128 scopus 로고    scopus 로고
    • Organization and ligand binding properties of the tail of acanthamoeba myosin-ia. Identification of an actin-binding site in the basic (tail homology-1) domain
    • Lee, W. L., Ostap, E. M., Zot, H. G., & Pollard, T. D. Organization and ligand binding properties of the tail of Acanthamoeba myosin-IA. Identification of an actin-binding site in the basic (tail homology-1) domain. J. Biol. Chem. 274, 35159-35171 (1999
    • (1999) J. Biol. Chem. , vol.274 , pp. 35159-35171
    • Lee, W.L.1    Ostap, E.M.2    Zot, H.G.3    Pollard, T.4
  • 98
    • 0034163368 scopus 로고    scopus 로고
    • Acan125 binding to the sh3 domain of acanthamoeba myosin-ic
    • Zot, H. G., Bhaskara, V., & Liu, L. Acan125 binding to the SH3 domain of acanthamoeba myosin-IC. Arch. Biochem. Biophys. 375, 161-164 (2000
    • (2000) Arch. Biochem. Biophys. , vol.375 , pp. 161-164
    • Zot, H.G.1    Bhaskara, V.2    Liu, L.3
  • 99
    • 0034640476 scopus 로고    scopus 로고
    • Identification and characterization of ckip-1, a novel pleckstrin homology domain-containing protein that interacts with protein kinase ck2
    • Bosc, D. G. et al. Identification and characterization of CKIP-1, a novel pleckstrin homology domain-containing protein that interacts with protein kinase CK2. J. Biol. Chem. 275, 14295-14306 (2000
    • (2000) J. Biol. Chem. , vol.275 , pp. 14295-14306
    • Bosc, D.G.1
  • 100
    • 17644371009 scopus 로고    scopus 로고
    • The pleckstrin homology domain-containing protein ckip-1 is involved in regulation of cell morphology and the actin cytoskeleton and interaction with actin capping protein
    • Canton, D. A. et al. The pleckstrin homology domain-containing protein CKIP-1 is involved in regulation of cell morphology and the actin cytoskeleton and interaction with actin capping protein. Mol. Cell. Biol. 25, 3519-3534 (2005
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 3519-3534
    • Canton, D.A.1
  • 101
    • 33846012906 scopus 로고    scopus 로고
    • The role of ckip-1 in cell morphology depends on its interaction with actin-capping protein
    • Reports that the interaction of CKIP1 with CP is physiologically relevant in cells
    • Canton, D. A., Olsten, M. E., Niederstrasser, H., Cooper, J. A., & Litchfield, D. W. The role of CKIP-1 in cell morphology depends on its interaction with actin-capping protein. J. Biol. Chem. 281, 36347-36359 (2006). Reports that the interaction of CKIP1 with CP is physiologically relevant in cells.
    • (2006) J. Biol. Chem. , vol.281 , pp. 36347-36359
    • Canton, D.A.1    Olsten, M.E.2    Niederstrasser, H.3    Cooper, J.A.4    Litchfield, D.W.5
  • 102
    • 84867474747 scopus 로고    scopus 로고
    • Ckip-1: A scaffold protein and potential therapeutic target integrating multiple signaling pathways and physiological functions
    • Nie, J. et al. CKIP-1: a scaffold protein and potential therapeutic target integrating multiple signaling pathways and physiological functions. Ageing Res. Rev. 12, 276-281 (2013
    • (2013) Ageing Res. Rev. , vol.12 , pp. 276-281
    • Nie, J.1
  • 103
    • 4744338740 scopus 로고    scopus 로고
    • The pleckstrin homology domain of ck2 interacting protein-1 is required for interactions and recruitment of protein kinase ck2 to the plasma membrane
    • Olsten, M. E., Canton, D. A., Zhang, C., Walton, P. A., & Litchfield, D. W. The Pleckstrin homology domain of CK2 interacting protein-1 is required for interactions and recruitment of protein kinase CK2 to the plasma membrane. J. Biol. Chem. 279, 42114-42127 (2004
    • (2004) J. Biol. Chem. , vol.279 , pp. 42114-42127
    • Olsten, M.E.1    Canton, D.A.2    Zhang, C.3    Walton, P.A.4    Litchfield, D.W.5
  • 104
    • 20144367088 scopus 로고    scopus 로고
    • Role for the pleckstrin homology domain-containing protein ckip-1 in ap-1 regulation and apoptosis
    • Zhang, L. et al. Role for the pleckstrin homology domain-containing protein CKIP-1 in AP-1 regulation and apoptosis. EMBO J. 24, 766-778 (2005
    • (2005) EMBO J. , vol.24 , pp. 766-778
    • Zhang, L.1
  • 105
    • 35448935143 scopus 로고    scopus 로고
    • Casein kinase 2-interacting protein-1, a novel akt pleckstrin homology domain-interacting protein, down-regulates pi3k/akt signaling and suppresses tumor growth in vivo
    • Tokuda, E. et al. Casein kinase 2-interacting protein-1, a novel Akt pleckstrin homology domain-interacting protein, down-regulates PI3K/Akt signaling and suppresses tumor growth in vivo. Cancer Res. 67, 9666-9676 (2007
    • (2007) Cancer Res. , vol.67 , pp. 9666-9676
    • Tokuda, E.1
  • 106
    • 33744805133 scopus 로고    scopus 로고
    • Ckip-1 recruits nuclear atm partially to the plasma membrane through interaction with atm
    • Zhang, L. et al. CKIP-1 recruits nuclear ATM partially to the plasma membrane through interaction with ATM. Cell. Signal. 18, 1386-1395 (2006
    • (2006) Cell. Signal. , vol.18 , pp. 1386-1395
    • Zhang, L.1
  • 107
    • 33947259324 scopus 로고    scopus 로고
    • The ph domain containing protein ckip-1 binds to ifp35 and nmi and is involved in cytokine signaling
    • Zhang, L. et al. The PH domain containing protein CKIP-1 binds to IFP35 and Nmi and is involved in cytokine signaling. Cell. Signal. 19, 932-944 (2007
    • (2007) Cell. Signal. , vol.19 , pp. 932-944
    • Zhang, L.1
  • 108
    • 48649104139 scopus 로고    scopus 로고
    • Targeting ww domains linker of hect-type ubiquitin ligase smurf1 for activation by ckip-1
    • Lu, K. et al. Targeting WW domains linker of HECT-type ubiquitin ligase Smurf1 for activation by CKIP-1. Nature Cell Biol. 10, 994-1002 (2008
    • (2008) Nature Cell Biol. , vol.10 , pp. 994-1002
    • Lu, K.1
  • 109
    • 84904249833 scopus 로고    scopus 로고
    • Ckip-1 acts as a colonic tumor suppressor by repressing oncogenic smurf1 synthesis and promoting smurf1 autodegradation
    • Nie, J. et al. CKIP-1 acts as a colonic tumor suppressor by repressing oncogenic Smurf1 synthesis and promoting Smurf1 autodegradation. Oncogene 33, 3677-3687 (2013
    • (2013) Oncogene , vol.33 , pp. 3677-3687
    • Nie, J.1
  • 110
    • 71549146571 scopus 로고    scopus 로고
    • The arp2/3 activator wash controls the fission of endosomes through a large multiprotein complex
    • Derivery, E. et al. The Arp2/3 activator WASH controls the fission of endosomes through a large multiprotein complex. Dev. Cell 17, 712-723 (2009
    • (2009) Dev. Cell , vol.17 , pp. 712-723
    • Derivery, E.1
  • 111
    • 77949801905 scopus 로고    scopus 로고
    • Wash and the arp2/3 complex regulate endosome shape and trafficking
    • Duleh, S. N., & Welch, M. D. WASH and the Arp2/3 complex regulate endosome shape and trafficking. Cytoskeleton 67, 193-206 (2010
    • (2010) Cytoskeleton , vol.67 , pp. 193-206
    • Duleh, S.N.1    Welch, M.2
  • 112
    • 71549167371 scopus 로고    scopus 로고
    • A fam21-containing wash complex regulates retromer-dependent sorting
    • Gomez, T. S., & Billadeau, D. D. A FAM21-containing WASH complex regulates retromer-dependent sorting. Dev. Cell 17, 699-711 (2009
    • (2009) Dev. Cell , vol.17 , pp. 699-711
    • Gomez, T.S.1    Billadeau, D.D.2
  • 113
    • 84870520072 scopus 로고    scopus 로고
    • Trafficking defects in wash-knockout fibroblasts originate from collapsed endosomal and lysosomal networks
    • Gomez, T. S., Gorman, J. A., de Narvajas, A. A., Koenig, A. O., & Billadeau, D. D. Trafficking defects in WASH-knockout fibroblasts originate from collapsed endosomal and lysosomal networks. Mol. Biol. Cell 23, 3215-3228 (2012
    • (2012) Mol. Biol. Cell , vol.23 , pp. 3215-3228
    • Gomez, T.S.1    Gorman, J.A.2    De Narvajas, A.A.3    Koenig, A.O.4    Billadeau, D.D.5
  • 114
    • 84856794322 scopus 로고    scopus 로고
    • The arp2/3 activator wash regulates ?5?1-integrin-mediated invasive migration
    • Zech, T. et al. The Arp2/3 activator WASH regulates ?5?1-integrin-mediated invasive migration. J. Cell Sci. 124, 3753-3759 (2011
    • (2011) J. Cell Sci. , vol.124 , pp. 3753-3759
    • Zech, T.1
  • 115
    • 77953757324 scopus 로고    scopus 로고
    • Wash and wave actin regulators of the wiskott-Aldrich syndrome protein (wasp) family are controlled by analogous structurally related complexes
    • Shows that FAM21 interacts with CP in the WASH complex
    • Jia, D. et al. WASH and WAVE actin regulators of the Wiskott-Aldrich syndrome protein (WASP) family are controlled by analogous structurally related complexes. Proc. Natl Acad. Sci. USA 107, 10442-10447 (2010). Shows that FAM21 interacts with CP in the WASH complex.
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 10442-10447
    • Jia, D.1
  • 116
    • 84856281728 scopus 로고    scopus 로고
    • Recruitment of the endosomal wash complex is mediated by the extended 'tail' of fam21 binding to the retromer protein vps35
    • Harbour, M. E., Breusegem, S. Y., & Seaman, M. N. Recruitment of the endosomal WASH complex is mediated by the extended 'tail' of Fam21 binding to the retromer protein Vps35. Biochem. J. 442, 209-220 (2012
    • (2012) Biochem. J. , vol.442 , pp. 209-220
    • Harbour, M.E.1    Breusegem, S.Y.2    Seaman, M.N.3
  • 117
    • 84862573732 scopus 로고    scopus 로고
    • Multiple repeat elements within the fam21 tail link the wash actin regulatory complex to the retromer
    • Jia, D., Gomez, T. S., Billadeau, D. D., & Rosen, M. K. Multiple repeat elements within the FAM21 tail link the WASH actin regulatory complex to the retromer. Mol. Biol. Cell 23, 2352-2361 (2012
    • (2012) Mol. Biol. Cell , vol.23 , pp. 2352-2361
    • Jia, D.1    Gomez, T.S.2    Billadeau, D.D.3    Rosen, M.K.4
  • 118
    • 84873843570 scopus 로고    scopus 로고
    • Cyclical action of the wash complex: Fam21 and capping protein drive wash recycling, not initial recruitment
    • Identifies the trafficking function of FAM21 and CP in the WASH complex
    • Park, L. et al. Cyclical action of the WASH complex: FAM21 and capping protein drive WASH recycling, not initial recruitment. Dev. Cell 24, 169-181 (2013). Identifies the trafficking function of FAM21 and CP in the WASH complex.
    • (2013) Dev. Cell , vol.24 , pp. 169-181
    • Park, L.1
  • 119
    • 0032483559 scopus 로고    scopus 로고
    • A novel adaptor protein orchestrates receptor patterning and cytoskeletal polarity in t-cell contacts
    • Dustin, M. L. et al. A novel adaptor protein orchestrates receptor patterning and cytoskeletal polarity in T-cell contacts. Cell 94, 667-677 (1998
    • (1998) Cell , vol.94 , pp. 667-677
    • Dustin, M.L.1
  • 120
    • 0033536599 scopus 로고    scopus 로고
    • Congenital nephrotic syndrome in mice lacking cd2-Associated protein
    • Shih, N. Congenital nephrotic syndrome in mice lacking CD2-Associated protein. Science 286, 312-315 (1999
    • (1999) Science , vol.286 , pp. 312-315
    • Shih, N.1
  • 121
    • 80053439688 scopus 로고    scopus 로고
    • Cd2ap in mouse and human podocytes controls a proteolytic program that regulates cytoskeletal structure and cellular survival
    • Yaddanapudi, S. et al. CD2AP in mouse and human podocytes controls a proteolytic program that regulates cytoskeletal structure and cellular survival. J. Clin. Invest. 121, 3965-3980 (2011
    • (2011) J. Clin. Invest. , vol.121 , pp. 3965-3980
    • Yaddanapudi, S.1
  • 123
    • 34547782856 scopus 로고    scopus 로고
    • Structure and function analysis of the cms/cin85 protein family identifies actin-bundling properties and heterotypic-complex formation
    • Gaidos, G., Soni, S., Oswald, D. J., Toselli, P. A., & Kirsch, K. H. Structure and function analysis of the CMS/CIN85 protein family identifies actin-bundling properties and heterotypic-complex formation. J. Cell Sci. 120, 2366-2377 (2007
    • (2007) J. Cell Sci. , vol.120 , pp. 2366-2377
    • Gaidos, G.1    Soni, S.2    Oswald, D.J.3    Toselli, P.A.4    Kirsch, K.H.5
  • 124
    • 0035895966 scopus 로고    scopus 로고
    • The adapter type protein cms/cd2ap binds to the proto-oncogenic protein c-cbl through a tyrosine phosphorylation-regulated src homology 3 domain interaction
    • Kirsch, K. H. et al. The adapter type protein CMS/CD2AP binds to the proto-oncogenic protein c-Cbl through a tyrosine phosphorylation-regulated Src homology 3 domain interaction. J. Biol. Chem. 276, 4957-4963 (2001
    • (2001) J. Biol. Chem. , vol.276 , pp. 4957-4963
    • Kirsch, K.H.1
  • 125
    • 80051688323 scopus 로고    scopus 로고
    • Solution structure, dynamics and thermodynamics of the three sh3 domains of cd2ap
    • Roldan, J. L., Blackledge, M., van Nuland, N. A., & Azuaga, A. I. Solution structure, dynamics and thermodynamics of the three SH3 domains of CD2AP. J. Biomol. NMR 50, 103-117 (2011
    • (2011) J. Biomol. NMR , vol.50 , pp. 103-117
    • Roldan, J.L.1    Blackledge, M.2    Van Nuland, N.A.3    Azuaga, A.I.4
  • 126
    • 84871902136 scopus 로고    scopus 로고
    • Cd2ap links cortactin and capping protein at the cell periphery to facilitate formation of lamellipodia
    • Reports that CD2AP recruits CP and cortactin to the plasma membrane
    • Zhao, J. et al. CD2AP links cortactin and capping protein at the cell periphery to facilitate formation of lamellipodia. Mol. Cell. Biol. 33, 38-47 (2013). Reports that CD2AP recruits CP and cortactin to the plasma membrane.
    • (2013) Mol. Cell. Biol. , vol.33 , pp. 38-47
    • Zhao, J.1
  • 127
    • 22144462425 scopus 로고    scopus 로고
    • The phosphorylation of capz-interacting protein (capzip) by stress-Activated protein kinases triggers its dissociation from capz
    • Shows that phosphorylation of CapZIP inhibits its interaction with CP
    • Eyers, C. E. et al. The phosphorylation of CapZ-interacting protein (CapZIP) by stress-Activated protein kinases triggers its dissociation from CapZ. Biochem. J. 389, 127-135 (2005). Shows that phosphorylation of CapZIP inhibits its interaction with CP.
    • (2005) Biochem. J. , vol.389 , pp. 127-135
    • Eyers, C.E.1
  • 128
    • 0036500929 scopus 로고    scopus 로고
    • Twinfilin a molecular mailman for actin monomers
    • Palmgren, S., Vartiainen, M., & Lappalainen, P. Twinfilin, a molecular mailman for actin monomers. J. Cell Sci. 115, 881-886 (2002
    • (2002) J. Cell Sci. , vol.115 , pp. 881-886
    • Palmgren, S.1    Vartiainen, M.2    Lappalainen, P.3
  • 129
    • 33645295750 scopus 로고    scopus 로고
    • Mammalian twinfilin sequesters adp-g-Actin and caps filament barbed ends: Implications in motility
    • Helfer, E. et al. Mammalian twinfilin sequesters ADP-G-Actin and caps filament barbed ends: implications in motility. EMBO J. 25, 1184-1195 (2006
    • (2006) EMBO J. , vol.25 , pp. 1184-1195
    • Helfer, E.1
  • 130
    • 0035886026 scopus 로고    scopus 로고
    • Interactions with pip2 adp-Actin monomers and capping protein regulate the activity and localization of yeast twinfilin
    • Palmgren, S., Ojala, P. J., Wear, M. A., Cooper, J. A., & Lappalainen, P. Interactions with PIP2, ADP-Actin monomers, and capping protein regulate the activity and localization of yeast twinfilin. J. Cell Biol. 155, 251-260 (2001
    • (2001) J. Cell Biol. , vol.155 , pp. 251-260
    • Palmgren, S.1    Ojala, P.J.2    Wear, M.A.3    Cooper, J.A.4    Lappalainen, P.5
  • 131
    • 0141445987 scopus 로고    scopus 로고
    • Mammals have two twinfilin isoforms whose subcellular localizations and tissue distributions are differentially regulated
    • Vartiainen, M. K., Sarkkinen, E. M., Matilainen, T., Salminen, M., & Lappalainen, P. Mammals have two twinfilin isoforms whose subcellular localizations and tissue distributions are differentially regulated. J. Biol. Chem. 278, 34347-34355 (2003
    • (2003) J. Biol. Chem. , vol.278 , pp. 34347-34355
    • Vartiainen, M.K.1    Sarkkinen, E.M.2    Matilainen, T.3    Salminen, M.4    Lappalainen, P.5
  • 132
    • 4143141100 scopus 로고    scopus 로고
    • Biological role and structural mechanism of twinfilin-capping protein interaction
    • Falck, S. et al. Biological role and structural mechanism of twinfilin-capping protein interaction. EMBO J. 23, 3010-3019 (2004
    • (2004) EMBO J. , vol.23 , pp. 3010-3019
    • Falck, S.1
  • 133
    • 58249091719 scopus 로고    scopus 로고
    • Two biochemically distinct and tissue-specific twinfilin isoforms are generated from the mouse twf2 gene by alternative promoter usage
    • Nevalainen, E. M., Skwarek-Maruszewska, A., Braun, A., Moser, M., & Lappalainen, P. Two biochemically distinct and tissue-specific twinfilin isoforms are generated from the mouse Twf2 gene by alternative promoter usage. Biochem. J. 417, 593-600 (2009
    • (2009) Biochem. J. , vol.417 , pp. 593-600
    • Nevalainen, E.M.1    Skwarek-Maruszewska, A.2    Braun, A.3    Moser, M.4    Lappalainen, P.5
  • 134
    • 0036854364 scopus 로고    scopus 로고
    • The two adf-h domains of twinfilin play functionally distinct roles in interactions with actin monomers
    • Ojala, P. J. et al. The two ADF-H domains of twinfilin play functionally distinct roles in interactions with actin monomers. Mol. Biol. Cell 13, 3811-3821 (2002
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3811-3821
    • Ojala, P.J.1
  • 135
    • 0031828002 scopus 로고    scopus 로고
    • Regulation of the cortical actin cytoskeleton in budding yeast by twinfilin, a ubiquitous actin monomer-sequestering protein
    • Goode, B. L., Drubin, D. G., & Lappalainen, P. Regulation of the cortical actin cytoskeleton in budding yeast by twinfilin, a ubiquitous actin monomer-sequestering protein. J. Cell Biol. 142, 723-733 (1998
    • (1998) J. Cell Biol. , vol.142 , pp. 723-733
    • Goode, B.L.1    Drubin, D.G.2    Lappalainen, P.3
  • 136
    • 0035956417 scopus 로고    scopus 로고
    • Twinfilin is required for actin-dependent developmental processes in drosophila
    • Wahlstrom, G. et al. Twinfilin is required for actin-dependent developmental processes in Drosophila. J. Cell Biol. 155, 787-796 (2001
    • (2001) J. Cell Biol. , vol.155 , pp. 787-796
    • Wahlstrom, G.1
  • 137
    • 33744521654 scopus 로고    scopus 로고
    • Carmil is a potent capping protein antagonist: Identification of a conserved carmil domain that inhibits the activity of capping protein and uncaps capped actin filaments
    • Shows that CARMIL inhibits CP and uncaps actin filaments, and that full-length CARMIL is autoinhibited
    • Uruno, T., Remmert, K., & Hammer, J. A. CARMIL is a potent capping protein antagonist: identification of a conserved CARMIL domain that inhibits the activity of capping protein and uncaps capped actin filaments. J. Biol. Chem. 281, 10635-10650 (2006). Shows that CARMIL inhibits CP and uncaps actin filaments, and that full-length CARMIL is autoinhibited.
    • (2006) J. Biol. Chem. , vol.281 , pp. 10635-10650
    • Uruno, T.1    Remmert, K.2    Hammer, J.A.3
  • 138
    • 77956514665 scopus 로고    scopus 로고
    • Molecular basis for barbed end uncapping by carmil homology domain 3 of mouse carmil-1
    • Zwolak, A., Uruno, T., Piszczek, G., Hammer, J. A., & Tjandra, N. Molecular basis for barbed end uncapping by CARMIL homology domain 3 of mouse CARMIL-1. J. Biol. Chem. 285, 29014-29026 (2010
    • (2010) J. Biol. Chem. , vol.285 , pp. 29014-29026
    • Zwolak, A.1    Uruno, T.2    Piszczek, G.3    Hammer, J.A.4    Tjandra, N.5
  • 139
    • 84860877885 scopus 로고    scopus 로고
    • Mechanism for carmil protein inhibition of heterodimeric actin-capping protein
    • Reports the allosteric mechanism for CARMIL-mediated inhibition of CP
    • Kim, T., Ravilious, G. E., Sept, D., & Cooper, J. A. Mechanism for CARMIL protein inhibition of heterodimeric actin-capping protein. J. Biol. Chem. 287, 15251-15262 (2012). Reports the allosteric mechanism for CARMIL-mediated inhibition of CP.
    • (2012) J. Biol. Chem. , vol.287 , pp. 15251-15262
    • Kim, T.1    Ravilious, G.E.2    Sept, D.3    Cooper, J.A.4
  • 140
    • 79956194275 scopus 로고    scopus 로고
    • Actin capping protein and its inhibitor carmil: How intrinsically disordered regions function
    • Takeda, S. et al. Actin capping protein and its inhibitor CARMIL: how intrinsically disordered regions function. Phys. Biol. 8, 035005 (2011
    • (2011) Phys. Biol. , vol.8 , pp. 035005
    • Takeda, S.1
  • 141
    • 77449152025 scopus 로고    scopus 로고
    • Direct observation of the uncapping of capping protein-capped actin filaments by carmil homology domain
    • Uses single-molecule imaging to show uncapping by CARMIL
    • Fujiwara, I., Remmert, K., & Hammer, J. A. Direct observation of the uncapping of capping protein-capped actin filaments by CARMIL homology domain J. Biol. Chem. 285, 2707-2720 (2010). Uses single-molecule imaging to show uncapping by CARMIL.
    • (2010) J. Biol. Chem. , vol.285 , pp. 2707-2720
    • Fujiwara, I.1    Remmert, K.2    Hammer, J.A.3
  • 142
    • 75549083753 scopus 로고    scopus 로고
    • Piecemeal or big bangs: Correlating the vertebrate evolution with proposed models of gene expansion events
    • Abbasi, A. A. Piecemeal or big bangs: correlating the vertebrate evolution with proposed models of gene expansion events. Nature Rev. Genet. 11, 166 (2010
    • (2010) Nature Rev. Genet. , vol.11 , pp. 166
    • Abbasi, A.A.1
  • 143
    • 84904332552 scopus 로고    scopus 로고
    • Capping protein is essential for cell migration in vivo and for filopodial morphology and dynamics
    • Sinnar, S. A., Antoku, S., Saffin, J. M., Cooper, J. A., & Halpain, S. Capping protein is essential for cell migration in vivo and for filopodial morphology and dynamics. Mol. Biol. Cell 25, 2152-2160 (2014
    • (2014) Mol. Biol. Cell , vol.25 , pp. 2152-2160
    • Sinnar, S.A.1    Antoku, S.2    Saffin, J.M.3    Cooper, J.A.4    Halpain, S.5
  • 144
    • 0037415574 scopus 로고    scopus 로고
    • Mechanism of filopodia initiation by reorganization of a dendritic network
    • Svitkina, T. M. et al. Mechanism of filopodia initiation by reorganization of a dendritic network. J. Cell Biol. 160, 409-421 (2003
    • (2003) J. Cell Biol. , vol.160 , pp. 409-421
    • Svitkina, T.M.1
  • 145
    • 84893217541 scopus 로고    scopus 로고
    • Correlation of actin crosslinker and capper expression levels with stereocilia growth phases
    • Avenarius, M. R. et al. Correlation of actin crosslinker and capper expression levels with stereocilia growth phases. Mol. Cell Proteom. 13, 606-620 (2014
    • (2014) Mol. Cell Proteom. , vol.13 , pp. 606-620
    • Avenarius, M.R.1
  • 146
    • 84890810942 scopus 로고    scopus 로고
    • Fsgs3/cd2ap is a barbed-end capping protein that stabilizes actin and strengthens adherens junctions
    • Tang, V. W., & Brieher, W. M. FSGS3/CD2AP is a barbed-end capping protein that stabilizes actin and strengthens adherens junctions. J. Cell Biol. 203, 815-833 (2013
    • (2013) J. Cell Biol. , vol.203 , pp. 815-833
    • Tang, V.W.1    Brieher, W.M.2
  • 147
    • 0026439926 scopus 로고
    • Thymosin ?4 sequesters the majority of g-Actin in resting human polymorphonuclear leukoctyes
    • Cassimeris, L., Safer, D., Nachmias, V. T., & Zigmond, S. H. Thymosin ?4 sequesters the majority of G-Actin in resting human polymorphonuclear leukoctyes. J. Cell Biol. 119, 1261-1270 (1992
    • (1992) J. Cell Biol. , vol.119 , pp. 1261-1270
    • Cassimeris, L.1    Safer, D.2    Nachmias, V.T.3    Zigmond, S.H.4
  • 148
    • 1642535385 scopus 로고    scopus 로고
    • Carmil is a bona fide capping protein interactant
    • Shows that CARMIL purified from cells contains CP and that it exists as a dimer
    • Remmert, K. et al. CARMIL is a bona fide capping protein interactant. J. Biol. Chem. 279, 3068-3077 (2004). Shows that CARMIL purified from cells contains CP and that it exists as a dimer.
    • (2004) J. Biol. Chem. , vol.279 , pp. 3068-3077
    • Remmert, K.1
  • 149
    • 0025259496 scopus 로고
    • Mechanism of the formation of contractile ring in dividing cultured animal cells. I. Recruitment of preexisting actin filaments into the cleavage furrow
    • Cao, L. G. Mechanism of the formation of contractile ring in dividing cultured animal cells. I. Recruitment of preexisting actin filaments into the cleavage furrow. J. Cell Biol. 110, 1089-1095 (1990
    • (1990) J. Cell Biol. , vol.110 , pp. 1089-1095
    • Cao, L.G.1
  • 150
    • 84880830434 scopus 로고    scopus 로고
    • The lymphoid lineage-specific actin-uncapping protein rltpr is essential for costimulation via cd28 and the development of regulatory t cells
    • Liang, Y. et al. The lymphoid lineage-specific actin-uncapping protein Rltpr is essential for costimulation via CD28 and the development of regulatory T cells. Nature Immunol. 14, 858-866 (2013
    • (2013) Nature Immunol. , vol.14 , pp. 858-866
    • Liang, Y.1
  • 151
    • 0035191415 scopus 로고    scopus 로고
    • Cd2ap localizes to the slit diaphragm and binds to nephrin via a novel c-terminal domain
    • Shih, N. Y. et al. CD2AP localizes to the slit diaphragm and binds to nephrin via a novel C-terminal domain. Am. J. Pathol. 159, 2303-2308 (2001
    • (2001) Am. J. Pathol. , vol.159 , pp. 2303-2308
    • Shih, N.Y.1
  • 152
    • 0026078290 scopus 로고
    • Domain structure in actin-binding proteins: Expression and functional characterization of truncated severin
    • Eichinger, L., Noegel, A. A., & Schleicher, M. Domain structure in actin-binding proteins: expression and functional characterization of truncated severin. J. Cell Biol. 112, 665-676 (1991
    • (1991) J. Cell Biol. , vol.112 , pp. 665-676
    • Eichinger, L.1    Noegel, A.A.2    Schleicher, M.3
  • 153
    • 0034693131 scopus 로고    scopus 로고
    • In vivo interaction of the adapter protein cd2-Associated protein with the type 2 polycystic kidney disease protein, polycystin-2
    • Lehtonen, S. et al. In vivo interaction of the adapter protein CD2-Associated protein with the type 2 polycystic kidney disease protein, polycystin-2. J. Biol. Chem. 275, 32888-32893 (2000
    • (2000) J. Biol. Chem. , vol.275 , pp. 32888-32893
    • Lehtonen, S.1
  • 154
    • 0026061084 scopus 로고
    • Three different actin filament assemblies occur in every hair cell: Each contains a specific actin crosslinking protein
    • Drenckhahn, D. et al. Three different actin filament assemblies occur in every hair cell: each contains a specific actin crosslinking protein. J. Cell Biol. 112, 641-651 (1991
    • (1991) J. Cell Biol. , vol.112 , pp. 641-651
    • Drenckhahn, D.1
  • 155
    • 0038105017 scopus 로고    scopus 로고
    • Cd2ap/cms regulates endosome morphology and traffic to the degradative pathway through its interaction with rab4 and c-cbl
    • Cormont, M. et al. CD2AP/CMS regulates endosome morphology and traffic to the degradative pathway through its interaction with Rab4 and c-Cbl. Traffic 4, 97-112 (2003
    • (2003) Traffic , vol.4 , pp. 97-112
    • Cormont, M.1
  • 156
    • 0034673361 scopus 로고    scopus 로고
    • Cloning and characterization of a novel adaptor protein, cin85, that interacts with c-cbl
    • Take, H. et al. Cloning and characterization of a novel adaptor protein, CIN85, that interacts with c-Cbl. Biochem. Biophys. Res. Commun. 268, 321-328 (2000
    • (2000) Biochem. Biophys. Res. Commun. , vol.268 , pp. 321-328
    • Take, H.1
  • 157
    • 0034254677 scopus 로고    scopus 로고
    • Negative regulation of pi 3-kinase by ruk, a novel adaptor protein
    • Gout, I. et al. Negative regulation of PI 3-kinase by Ruk, a novel adaptor protein. EMBO J. 19, 4015-4025 (2000
    • (2000) EMBO J. , vol.19 , pp. 4015-4025
    • Gout, I.1
  • 158
    • 0038498066 scopus 로고    scopus 로고
    • A cortactin-cd2-Associated protein (cd2ap) complex provides a novel link between epidermal growth factor receptor endocytosis and the actin cytoskeleton
    • Lynch, D. K. et al. A Cortactin-CD2-Associated protein (CD2AP) complex provides a novel link between epidermal growth factor receptor endocytosis and the actin cytoskeleton. J. Biol. Chem. 278, 21805-21813 (2003
    • (2003) J. Biol. Chem. , vol.278 , pp. 21805-21813
    • Lynch, D.K.1
  • 159
    • 0035210324 scopus 로고    scopus 로고
    • Podocin, a raft-Associated component of the glomerular slit diaphragm, interacts with cd2ap and nephrin
    • Schwarz, K. et al. Podocin, a raft-Associated component of the glomerular slit diaphragm, interacts with CD2AP and nephrin. J. Clin. Invest. 108, 1621-1629 (2001
    • (2001) J. Clin. Invest. , vol.108 , pp. 1621-1629
    • Schwarz, K.1
  • 160
    • 0036278105 scopus 로고    scopus 로고
    • Accessory protein recruitment motifs in clathrin-mediated endocytosis
    • Brett, T. J., Traub, L. M., & Fremont, D. H. Accessory protein recruitment motifs in clathrin-mediated endocytosis. Structure 10, 797-809 (2002
    • (2002) Structure , vol.10 , pp. 797-809
    • Brett, T.J.1    Traub, L.M.2    Fremont, D.H.3
  • 161
    • 0038788840 scopus 로고    scopus 로고
    • Nephrin and cd2ap associate with phosphoinositide 3-oh kinase and stimulate akt-dependent signaling
    • Huber, T. B. et al. Nephrin and CD2AP associate with phosphoinositide 3-OH kinase and stimulate AKT-dependent signaling. Mol. Cell. Biol. 23, 4917-4928 (2003
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 4917-4928
    • Huber, T.B.1
  • 162
    • 34547213485 scopus 로고    scopus 로고
    • Nuclear relocation of the nephrin and cd2ap-binding protein dendrin promotes apoptosis of podocytes
    • Asanuma, K., Campbell, K. N., Kim, K., Faul, C., & Mundel, P. Nuclear relocation of the nephrin and CD2AP-binding protein dendrin promotes apoptosis of podocytes. Proc. Natl Acad. Sci. USA 104, 10134-10139 (2007
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 10134-10139
    • Asanuma, K.1    Campbell, K.N.2    Kim, K.3    Faul, C.4    Mundel, P.5
  • 163
    • 3042765835 scopus 로고    scopus 로고
    • Cin85 associates with multiple effectors controlling intracellular trafficking of epidermal growth factor receptors
    • Kowanetz, K. et al. CIN85 associates with multiple effectors controlling intracellular trafficking of epidermal growth factor receptors. Mol. Biol. Cell 15, 3155-3166 (2004
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3155-3166
    • Kowanetz, K.1
  • 164
    • 15744368813 scopus 로고    scopus 로고
    • Mislocalization or reduced expression of arf gtpase-Activating protein asap1 inhibits cell spreading and migration by influencing arf1 gtpase cycling
    • Liu, Y., Yerushalmi, G. M., Grigera, P. R., & Parsons, J. T. Mislocalization or reduced expression of Arf GTPase-Activating protein ASAP1 inhibits cell spreading and migration by influencing Arf1 GTPase cycling. J. Biol. Chem. 280, 8884-8892 (2005
    • (2005) J. Biol. Chem. , vol.280 , pp. 8884-8892
    • Liu, Y.1    Yerushalmi, G.M.2    Grigera, P.R.3    Parsons, J.T.4
  • 165
    • 6344228185 scopus 로고    scopus 로고
    • Actin-binding proteins - A unifying hypothesis
    • Dominguez, R. Actin-binding proteins - a unifying hypothesis. Trends Biochem. Sci. 29, 572-578 (2004
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 572-578
    • Dominguez, R.1
  • 166
    • 34447276909 scopus 로고    scopus 로고
    • F-bar proteins join the bar family fold
    • Frost, A., De Camilli, P., & Unger, V. M. F-BAR proteins join the BAR family fold. Structure 15, 751-753 (2007
    • (2007) Structure , vol.15 , pp. 751-753
    • Frost, A.1    De Camilli, P.2    Unger, V.M.3
  • 167
    • 1642580751 scopus 로고    scopus 로고
    • Role for the pleckstrin homology domain-containing protein ckip-1 in phosphatidylinositol 3-kinase-regulated muscle differentiation
    • Safi, A. et al. Role for the pleckstrin homology domain-containing protein CKIP-1 in phosphatidylinositol 3-kinase-regulated muscle differentiation. Mol. Cell. Biol. 24, 1245-1255 (2004
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 1245-1255
    • Safi, A.1
  • 168
    • 84869121921 scopus 로고    scopus 로고
    • Ckip-1 regulates mammalian and zebrafish myoblast fusion
    • Baas, D. et al. CKIP-1 regulates mammalian and zebrafish myoblast fusion. J. Cell Sci. 125, 3790-3800 (2012
    • (2012) J. Cell Sci. , vol.125 , pp. 3790-3800
    • Baas, D.1
  • 169
    • 0025612125 scopus 로고
    • Microinjection of villin into cultured cells induces rapid and long-lasting changes in cell morphology but does not inhibit cytokinesis, cell motility, or membrane ruffling
    • Franck, Z. Microinjection of villin into cultured cells induces rapid and long-lasting changes in cell morphology but does not inhibit cytokinesis, cell motility, or membrane ruffling. J. Cell Biol. 111, 2475-2485 (1990
    • (1990) J. Cell Biol. , vol.111 , pp. 2475-2485
    • Franck, Z.1
  • 170
    • 84898443651 scopus 로고    scopus 로고
    • Ckip-1 is an intrinsic negative regulator of t-cell activation through an interaction with carma1
    • Sakamoto, T. et al. CKIP-1 is an intrinsic negative regulator of T-cell activation through an interaction with CARMA1. PLoS ONE 9, e85762 (2014
    • (2014) PLoS ONE , vol.9 , pp. e85762
    • Sakamoto, T.1
  • 171
    • 84871334776 scopus 로고    scopus 로고
    • Ckip-1 inhibits cardiac hypertrophy by regulating class ii histone deacetylase phosphorylation through recruiting pp2a
    • Ling, S. et al. CKIP-1 inhibits cardiac hypertrophy by regulating class II histone deacetylase phosphorylation through recruiting PP2A. Circulation 126, 3028-3040 (2012
    • (2012) Circulation , vol.126 , pp. 3028-3040
    • Ling, S.1
  • 173
    • 0025192475 scopus 로고
    • Structure and function of the cytoskeleton of a dictyostelium myosin-defective mutant
    • Fukui, Y. Structure and function of the cytoskeleton of a Dictyostelium myosin-defective mutant. J. Cell Biol. 110, 367-378 (1990
    • (1990) J. Cell Biol. , vol.110 , pp. 367-378
    • Fukui, Y.1
  • 174
    • 0025091625 scopus 로고
    • Fimbrin is a homologue of the cytoplasmic phosphoprotein plastin and has domains homologous with calmodulin and actin gelation proteins
    • de Arruda, M. V., Watson, S., Lin, C. S., Leavitt, J., & Matsudaira, P. Fimbrin is a homologue of the cytoplasmic phosphoprotein plastin and has domains homologous with calmodulin and actin gelation proteins. J. Cell Biol. 111, 1069-1079 (1990
    • (1990) J. Cell Biol. , vol.111 , pp. 1069-1079
    • De Arruda, M.V.1    Watson, S.2    Lin, C.S.3    Leavitt, J.4    Matsudaira, P.5
  • 175
    • 84877617563 scopus 로고    scopus 로고
    • Endosomal recruitment of the wash complex: Active sequences and mutations impairing interaction with the retromer
    • Helfer, E. et al. Endosomal recruitment of the WASH complex: active sequences and mutations impairing interaction with the retromer. Biol. Cell 105, 191-207 (2013).
    • (2013) Biol. Cell , vol.105 , pp. 191-207
    • Helfer, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.