메뉴 건너뛰기




Volumn 125, Issue 15, 2012, Pages 3519-3527

Actin nucleators in the nucleus: An emerging theme

Author keywords

Actin; Nucleation; Nucleus

Indexed keywords

ACTIN; APC PROTEIN; ARP PROTEIN; FHOD1 PROTEIN; MDIA PROTEIN; NEURAL WISKOTT ALDRICH SYNDROME PROTEIN; PROTEIN; UNCLASSIFIED DRUG; WASH PROTEIN;

EID: 84869105145     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.099523     Document Type: Note
Times cited : (33)

References (121)
  • 2
    • 38949145356 scopus 로고    scopus 로고
    • The actin-related protein hArp8 accumulates on the mitotic chromosomes and functions in chromosome alignment
    • Aoyama, N., Oka, A., Kitayama, K., Kurumizaka, H. and Harata, M. (2008). The actin-related protein hArp8 accumulates on the mitotic chromosomes and functions in chromosome alignment. Exp. Cell Res. 314, 859-868.
    • (2008) Exp. Cell Res. , vol.314 , pp. 859-868
    • Aoyama, N.1    Oka, A.2    Kitayama, K.3    Kurumizaka, H.4    Harata, M.5
  • 5
    • 67650581556 scopus 로고    scopus 로고
    • Recent advances in understanding the pathophysiology of Wiskott-Aldrich syndrome
    • Bosticardo, M., Marangoni, F., Aiuti, A., Villa, A. and Grazia Roncarolo, M. (2009). Recent advances in understanding the pathophysiology of Wiskott-Aldrich syndrome. Blood 113, 6288-6295.
    • (2009) Blood , vol.113 , pp. 6288-6295
    • Bosticardo, M.1    Marangoni, F.2    Aiuti, A.3    Villa, A.4    Grazia Roncarolo, M.5
  • 6
    • 14644390357 scopus 로고    scopus 로고
    • Redefining the subcellular location and transport of APC: new insights using a panel of antibodies
    • Brocardo, M., Näthke, I. S. and Henderson, B. R. (2005). Redefining the subcellular location and transport of APC: new insights using a panel of antibodies. EMBO Rep. 6, 184-190.
    • (2005) EMBO Rep , vol.6 , pp. 184-190
    • Brocardo, M.1    Näthke, I.S.2    Henderson, B.R.3
  • 7
    • 0031941159 scopus 로고    scopus 로고
    • Chromatin remodeling machines: similar motors, ulterior motives
    • Cairns, B. R. (1998). Chromatin remodeling machines: similar motors, ulterior motives. Trends Biochem. Sci. 23, 20-25.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 20-25
    • Cairns, B.R.1
  • 8
    • 84861394054 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase (MAPK/ERK) regulates adenomatous polyposis coli during growth-factor-induced cell extension
    • Caro-Gonzalez, H. Y., Nejsum, L. N., Siemers, K. A., Shaler, T. A., Nelson, W. J. and Barth, A. I. (2012). Mitogen-activated protein kinase (MAPK/ERK) regulates adenomatous polyposis coli during growth-factor-induced cell extension. J. Cell Sci. 125, 1247-1258.
    • (2012) J. Cell Sci. , vol.125 , pp. 1247-1258
    • Caro-Gonzalez, H.Y.1    Nejsum, L.N.2    Siemers, K.A.3    Shaler, T.A.4    Nelson, W.J.5    Barth, A.I.6
  • 9
    • 36549053109 scopus 로고    scopus 로고
    • Mammalian diaphanous-related formin Dia1 controls the organization of E-cadherinmediated cell-cell junctions
    • Carramusa, L., Ballestrem, C., Zilberman, Y. and Bershadsky, A. D. (2007). Mammalian diaphanous-related formin Dia1 controls the organization of E-cadherinmediated cell-cell junctions. J. Cell Sci. 120, 3870-3882.
    • (2007) J. Cell Sci. , vol.120 , pp. 3870-3882
    • Carramusa, L.1    Ballestrem, C.2    Zilberman, Y.3    Bershadsky, A.D.4
  • 10
    • 72949110575 scopus 로고    scopus 로고
    • Unleashing formins to remodel the actin and microtubule cytoskeletons
    • Chesarone, M. A., DuPage, A. G. and Goode, B. L. (2010). Unleashing formins to remodel the actin and microtubule cytoskeletons. Nat. Rev. Mol. Cell Biol. 11, 62-74.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 62-74
    • Chesarone, M.A.1    DuPage, A.G.2    Goode, B.L.3
  • 11
    • 34848927902 scopus 로고    scopus 로고
    • The many faces of actin: matching assembly factors with cellular structures
    • Chhabra, E. S. and Higgs, H. N. (2007). The many faces of actin: matching assembly factors with cellular structures. Nat. Cell Biol. 9, 1110-1121.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 1110-1121
    • Chhabra, E.S.1    Higgs, H.N.2
  • 12
    • 0036854328 scopus 로고    scopus 로고
    • The diaphanous-related formin mDia1 controls serum response factor activity through its effects on actin polymerization
    • Copeland, J. W. and Treisman, R. (2002). The diaphanous-related formin mDia1 controls serum response factor activity through its effects on actin polymerization. Mol. Biol. Cell 13, 4088-4099.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4088-4099
    • Copeland, J.W.1    Treisman, R.2
  • 13
    • 33846030177 scopus 로고    scopus 로고
    • Mdm2 targets the p53 transcription cofactor JMY for degradation
    • Coutts, A. S., Boulahbel, H., Graham, A. and La Thangue, N. B. (2007). Mdm2 targets the p53 transcription cofactor JMY for degradation. EMBO Rep. 8, 84-90.
    • (2007) EMBO Rep , vol.8 , pp. 84-90
    • Coutts, A.S.1    Boulahbel, H.2    Graham, A.3    La Thangue, N.B.4
  • 14
    • 73949120862 scopus 로고    scopus 로고
    • A transcription co-factor integrates cell adhesion and motility with the p53 response
    • Coutts, A. S., Weston, L. and La Thangue, N. B. (2009). A transcription co-factor integrates cell adhesion and motility with the p53 response. Proc. Natl. Acad. Sci. USA 106, 19872-19877.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 19872-19877
    • Coutts, A.S.1    Weston, L.2    La Thangue, N.B.3
  • 15
    • 62649104179 scopus 로고    scopus 로고
    • Loss of cell-cell contacts induces NF-kappaB via RhoA-mediated activation of protein kinase D1
    • Cowell, C. F., Yan, I. K., Eiseler, T., Leightner, A. C., Döppler, H. and Storz, P. (2009). Loss of cell-cell contacts induces NF-kappaB via RhoA-mediated activation of protein kinase D1. J. Cell. Biochem. 106, 714-728.
    • (2009) J. Cell. Biochem. , vol.106 , pp. 714-728
    • Cowell, C.F.1    Yan, I.K.2    Eiseler, T.3    Leightner, A.C.4    Döppler, H.5    Storz, P.6
  • 16
  • 17
    • 71549146571 scopus 로고    scopus 로고
    • The Arp2/3 activator WASH controls the fission of endosomes through a large multiprotein complex
    • Derivery, E., Sousa, C., Gautier, J. J., Lombard, B., Loew, D. and Gautreau, A. (2009). The Arp2/3 activator WASH controls the fission of endosomes through a large multiprotein complex. Dev. Cell 17, 712-723.
    • (2009) Dev. Cell , vol.17 , pp. 712-723
    • Derivery, E.1    Sousa, C.2    Gautier, J.J.3    Lombard, B.4    Loew, D.5    Gautreau, A.6
  • 18
    • 0027937223 scopus 로고
    • Isolation of a novel gene mutated in Wiskott-Aldrich syndrome
    • Derry, J. M., Ochs, H. D. and Francke, U. (1994). Isolation of a novel gene mutated in Wiskott-Aldrich syndrome. Cell 78, 635-644.
    • (1994) Cell , vol.78 , pp. 635-644
    • Derry, J.M.1    Ochs, H.D.2    Francke, U.3
  • 19
    • 77956163491 scopus 로고    scopus 로고
    • Regulation of WASp by phosphorylation: Activation or other functions? Commun
    • Dovas, A. and Cox, D. (2010). Regulation of WASp by phosphorylation: Activation or other functions? Commun. Integr. Biol. 3, 101-105.
    • (2010) Integr. Biol. , vol.3 , pp. 101-105
    • Dovas, A.1    Cox, D.2
  • 20
    • 77949801905 scopus 로고    scopus 로고
    • WASH and the Arp2/3 complex regulate endosome shape and trafficking
    • Duleh, S. N. and Welch, M. D. (2010). WASH and the Arp2/3 complex regulate endosome shape and trafficking. Cytoskeleton (Hoboken) 67, 193-206.
    • (2010) Cytoskeleton (Hoboken) , vol.67 , pp. 193-206
    • Duleh, S.N.1    Welch, M.D.2
  • 21
    • 27844455570 scopus 로고    scopus 로고
    • Mechanism of filament nucleation and branch stability revealed by the structure of the Arp2/3 complex at actin branch junctions
    • doi:310.1371/ journal.pbio.0030383
    • Egile, C., Rouiller, I., Xu, X. P., Volkmann, N., Li, R. and Hanein, D. (2005). Mechanism of filament nucleation and branch stability revealed by the structure of the Arp2/3 complex at actin branch junctions. PLoS Biol. 3, e383. doi:310.1371/ journal.pbio.0030383
    • (2005) PLoS Biol , vol.3
    • Egile, C.1    Rouiller, I.2    Xu, X.P.3    Volkmann, N.4    Li, R.5    Hanein, D.6
  • 22
    • 79957907752 scopus 로고    scopus 로고
    • Structural biochemistry of nuclear actin-related proteins 4 and 8 reveals their interaction with actin
    • Fenn, S., Breitsprecher, D., Gerhold, C. B., Witte, G., Faix, J. and Hopfner, K. P. (2011). Structural biochemistry of nuclear actin-related proteins 4 and 8 reveals their interaction with actin. EMBO J. 30, 2153-2166
    • (2011) EMBO J , vol.30 , pp. 2153-2166
    • Fenn, S.1    Breitsprecher, D.2    Gerhold, C.B.3    Witte, G.4    Faix, J.5    Hopfner, K.P.6
  • 23
    • 1242316973 scopus 로고    scopus 로고
    • An actin-myosin complex on actively transcribing genes
    • Fomproix, N. and Percipalle, P. (2004). An actin-myosin complex on actively transcribing genes. Exp. Cell Res. 294, 140-148.
    • (2004) Exp. Cell Res. , vol.294 , pp. 140-148
    • Fomproix, N.1    Percipalle, P.2
  • 24
    • 0035824622 scopus 로고    scopus 로고
    • ARM domain-dependent nuclear import of adenomatous polyposis coli protein is stimulated by the B56 alpha subunit of protein phosphatase 2A
    • Galea, M. A., Eleftheriou, A. and Henderson, B. R. (2001). ARM domain-dependent nuclear import of adenomatous polyposis coli protein is stimulated by the B56 alpha subunit of protein phosphatase 2A. J. Biol. Chem. 276, 45833-45839.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45833-45839
    • Galea, M.A.1    Eleftheriou, A.2    Henderson, B.R.3
  • 25
    • 0037341806 scopus 로고    scopus 로고
    • RhoD regulates endosome dynamics through Diaphanous-related Formin and Src tyrosine kinase
    • Gasman, S., Kalaidzidis, Y. and Zerial, M. (2003). RhoD regulates endosome dynamics through Diaphanous-related Formin and Src tyrosine kinase. Nat. Cell Biol. 5, 195-204.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 195-204
    • Gasman, S.1    Kalaidzidis, Y.2    Zerial, M.3
  • 27
  • 28
    • 65249111020 scopus 로고    scopus 로고
    • Actin dynamics and functions in the interphase nucleus: moving toward an understanding of nuclear polymeric actin
    • Gieni, R. S. and Hendzel, M. J. (2009). Actin dynamics and functions in the interphase nucleus: moving toward an understanding of nuclear polymeric actin. Biochem. Cell Biol. 87, 283-306.
    • (2009) Biochem. Cell Biol. , vol.87 , pp. 283-306
    • Gieni, R.S.1    Hendzel, M.J.2
  • 29
    • 33749037156 scopus 로고    scopus 로고
    • The Arp2/3 complex: an actin nucleator comes of age
    • Goley, E. D. and Welch, M. D. (2006). The Arp2/3 complex: an actin nucleator comes of age. Nat. Rev. Mol. Cell Biol. 7, 713-726.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 713-726
    • Goley, E.D.1    Welch, M.D.2
  • 30
    • 6344258806 scopus 로고    scopus 로고
    • Critical conformational changes in the Arp2/3 complex are induced by nucleotide and nucleation promoting factor
    • Goley, E. D., Rodenbusch, S. E., Martin, A. C. and Welch, M. D. (2004). Critical conformational changes in the Arp2/3 complex are induced by nucleotide and nucleation promoting factor. Mol. Cell 16, 269-279.
    • (2004) Mol. Cell , vol.16 , pp. 269-279
    • Goley, E.D.1    Rodenbusch, S.E.2    Martin, A.C.3    Welch, M.D.4
  • 31
    • 71549167371 scopus 로고    scopus 로고
    • A FAM21-containing WASH complex regulates retromer-dependent sorting
    • Gomez, T. S. and Billadeau, D. D. (2009). A FAM21-containing WASH complex regulates retromer-dependent sorting. Dev. Cell 17, 699-711.
    • (2009) Dev. Cell , vol.17 , pp. 699-711
    • Gomez, T.S.1    Billadeau, D.D.2
  • 32
    • 0032957520 scopus 로고    scopus 로고
    • Conformational difference between nuclear and cytoplasmic actin as detected by a monoclonal antibody
    • Gonsior, S. M., Platz, S., Buchmeier, S., Scheer, U., Jockusch, B. M. and Hinssen, H. (1999). Conformational difference between nuclear and cytoplasmic actin as detected by a monoclonal antibody. J. Cell Sci. 112, 797-809.
    • (1999) J. Cell Sci. , vol.112 , pp. 797-809
    • Gonsior, S.M.1    Platz, S.2    Buchmeier, S.3    Scheer, U.4    Jockusch, B.M.5    Hinssen, H.6
  • 33
    • 35648943165 scopus 로고    scopus 로고
    • mDia2 regulates actin and focal adhesion dynamics and organization in the lamella for efficient epithelial cell migration
    • Gupton, S. L., Eisenmann, K., Alberts, A. S. and Waterman-Storer, C. M. (2007). mDia2 regulates actin and focal adhesion dynamics and organization in the lamella for efficient epithelial cell migration. J. Cell Sci. 120, 3475-3487.
    • (2007) J. Cell Sci. , vol.120 , pp. 3475-3487
    • Gupton, S.L.1    Eisenmann, K.2    Alberts, A.S.3    Waterman-Storer, C.M.4
  • 35
    • 0033129407 scopus 로고    scopus 로고
    • Two isoforms of a human actinrelated protein show nuclear localization and mutually selective expression between brain and other tissues
    • Harata, M., Mochizuki, R. and Mizuno, S. (1999). Two isoforms of a human actinrelated protein show nuclear localization and mutually selective expression between brain and other tissues. Biosci. Biotechnol. Biochem. 63, 917-923.
    • (1999) Biosci. Biotechnol. Biochem. , vol.63 , pp. 917-923
    • Harata, M.1    Mochizuki, R.2    Mizuno, S.3
  • 36
    • 77955104690 scopus 로고    scopus 로고
    • Adenomatous polyposis coli regulates endothelial cell migration independent of roles in beta-catenin signaling and cell-cell adhesion
    • Harris, E. S. and Nelson, W. J. (2010). Adenomatous polyposis coli regulates endothelial cell migration independent of roles in beta-catenin signaling and cell-cell adhesion. Mol. Biol. Cell 21, 2611-2623.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2611-2623
    • Harris, E.S.1    Nelson, W.J.2
  • 37
    • 0034282097 scopus 로고    scopus 로고
    • Nuclear-cytoplasmic shuttling of APC regulates beta-catenin subcellular localization and turnover
    • Henderson, B. R. (2000). Nuclear-cytoplasmic shuttling of APC regulates beta-catenin subcellular localization and turnover. Nat. Cell Biol. 2, 653-660.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 653-660
    • Henderson, B.R.1
  • 38
    • 11144281883 scopus 로고    scopus 로고
    • Phylogenetic analysis of the formin homology 2 domain
    • Higgs, H. N. and Peterson, K. J. (2005). Phylogenetic analysis of the formin homology 2 domain. Mol. Biol. Cell 16, 1-13.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1-13
    • Higgs, H.N.1    Peterson, K.J.2
  • 39
    • 0037191755 scopus 로고    scopus 로고
    • TRF2 associates with DREF and directs promoter-selective gene expression in Drosophila
    • Hochheimer, A., Zhou, S., Zheng, S., Holmes, M. C. and Tjian, R. (2002). TRF2 associates with DREF and directs promoter-selective gene expression in Drosophila. Nature 420, 439-445.
    • (2002) Nature , vol.420 , pp. 439-445
    • Hochheimer, A.1    Zhou, S.2    Zheng, S.3    Holmes, M.C.4    Tjian, R.5
  • 40
    • 59649083719 scopus 로고    scopus 로고
    • Cell and molecular biology of nuclear actin
    • Hofmann, W. A. (2009). Cell and molecular biology of nuclear actin. Int Rev Cell Mol Biol 273, 219-263.
    • (2009) Int Rev Cell Mol Biol , vol.273 , pp. 219-263
    • Hofmann, W.A.1
  • 42
    • 33646386142 scopus 로고    scopus 로고
    • Stress fibers are generated by two distinct actin assembly mechanisms in motile cells
    • Hotulainen, P. and Lappalainen, P. (2006). Stress fibers are generated by two distinct actin assembly mechanisms in motile cells. J. Cell Biol. 173, 383-394.
    • (2006) J. Cell Biol. , vol.173 , pp. 383-394
    • Hotulainen, P.1    Lappalainen, P.2
  • 43
    • 10644294832 scopus 로고    scopus 로고
    • A role for beta-actin in RNA polymerase III transcription
    • Hu, P., Wu, S. and Hernandez, N. (2004). A role for beta-actin in RNA polymerase III transcription. Genes Dev. 18, 3010-3015.
    • (2004) Genes Dev , vol.18 , pp. 3010-3015
    • Hu, P.1    Wu, S.2    Hernandez, N.3
  • 44
    • 0037093315 scopus 로고    scopus 로고
    • T-cell factors: turn-ons and turn-offs
    • Hurlstone, A. and Clevers, H. (2002). T-cell factors: turn-ons and turn-offs. EMBO J. 21, 2303-2311.
    • (2002) EMBO J , vol.21 , pp. 2303-2311
    • Hurlstone, A.1    Clevers, H.2
  • 45
    • 85012414651 scopus 로고
    • Electron microscope studies on the structure of natural and synthetic protein filaments from striated muscle
    • Huxley, H. E. (1963). Electron microscope studies on the structure of natural and synthetic protein filaments from striated muscle. J. Mol. Biol. 7, 281-308.
    • (1963) J. Mol. Biol. , vol.7 , pp. 281-308
    • Huxley, H.E.1
  • 47
    • 78049241459 scopus 로고    scopus 로고
    • INO80 chromatin remodeling complex promotes the removal of UV lesions by the nucleotide excision repair pathway
    • Jiang, Y., Wang, X., Bao, S., Guo, R., Johnson, D. G., Shen, X. and Li, L. (2010). INO80 chromatin remodeling complex promotes the removal of UV lesions by the nucleotide excision repair pathway. Proc. Natl. Acad. Sci. USA 107, 17274-17279.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 17274-17279
    • Jiang, Y.1    Wang, X.2    Bao, S.3    Guo, R.4    Johnson, D.G.5    Shen, X.6    Li, L.7
  • 49
    • 8444240109 scopus 로고    scopus 로고
    • The LIM domain: from the cytoskeleton to the nucleus
    • Kadrmas, J. L. and Beckerle, M. C. (2004). The LIM domain: from the cytoskeleton to the nucleus. Nat. Rev. Mol. Cell Biol. 5, 920-931.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 920-931
    • Kadrmas, J.L.1    Beckerle, M.C.2
  • 50
    • 50549179991 scopus 로고
    • The G-F equilibrium in actin solutions under various conditions
    • Kasai, M., Asakura, S. and Oosawa, F. (1962). The G-F equilibrium in actin solutions under various conditions. Biochim. Biophys. Acta 57, 13-21.
    • (1962) Biochim. Biophys. Acta , vol.57 , pp. 13-21
    • Kasai, M.1    Asakura, S.2    Oosawa, F.3
  • 52
    • 0035795666 scopus 로고    scopus 로고
    • Novel actin-related proteins in vertebrates: similarities of structure and expression pattern to Arp6 localized on Drosophila heterochromatin
    • Kato, M., Sasaki, M., Mizuno, S. and Harata, M. (2001). Novel actin-related proteins in vertebrates: similarities of structure and expression pattern to Arp6 localized on Drosophila heterochromatin. Gene 268, 133-140.
    • (2001) Gene , vol.268 , pp. 133-140
    • Kato, M.1    Sasaki, M.2    Mizuno, S.3    Harata, M.4
  • 54
    • 0038325646 scopus 로고    scopus 로고
    • The formin-homology-domain-containing protein FHOD1 enhances cell migration
    • Koka, S., Neudauer, C. L., Li, X., Lewis, R. E., McCarthy, J. B. and Westendorf, J. J. (2003). The formin-homology-domain-containing protein FHOD1 enhances cell migration. J. Cell Sci. 116, 1745-1755.
    • (2003) J. Cell Sci. , vol.116 , pp. 1745-1755
    • Koka, S.1    Neudauer, C.L.2    Li, X.3    Lewis, R.E.4    McCarthy, J.B.5    Westendorf, J.J.6
  • 55
    • 6944220067 scopus 로고    scopus 로고
    • Insertional assembly of actin filament barbed ends in association with formins produces piconewton forces
    • Kovar, D. R. and Pollard, T. D. (2004). Insertional assembly of actin filament barbed ends in association with formins produces piconewton forces. Proc. Natl. Acad. Sci. USA 101, 14725-14730.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 14725-14730
    • Kovar, D.R.1    Pollard, T.D.2
  • 56
    • 31044433924 scopus 로고    scopus 로고
    • Control of the assembly of ATP- and ADP-actin by formins and profilin
    • Kovar, D. R., Harris, E. S., Mahaffy, R., Higgs, H. N. and Pollard, T. D. (2006). Control of the assembly of ATP- and ADP-actin by formins and profilin. Cell 124, 423-435.
    • (2006) Cell , vol.124 , pp. 423-435
    • Kovar, D.R.1    Harris, E.S.2    Mahaffy, R.3    Higgs, H.N.4    Pollard, T.D.5
  • 57
    • 34548289288 scopus 로고    scopus 로고
    • Septins regulate actin organization and cell-cycle arrest through nuclear accumulation of NCK mediated by SOCS7
    • Kremer, B. E., Adang, L. A. and Macara, I. G. (2007). Septins regulate actin organization and cell-cycle arrest through nuclear accumulation of NCK mediated by SOCS7. Cell 130, 837-850.
    • (2007) Cell , vol.130 , pp. 837-850
    • Kremer, B.E.1    Adang, L.A.2    Macara, I.G.3
  • 58
    • 3042780593 scopus 로고    scopus 로고
    • Cytoplasmic localization and nucleo-cytoplasmic shuttling of BAF53, a component of chromatin-modifying complexes
    • Lee, J. H., Chang, S. H., Shim, J. H., Lee, J. Y., Yoshida, M. and Kwon, H. (2003). Cytoplasmic localization and nucleo-cytoplasmic shuttling of BAF53, a component of chromatin-modifying complexes. Mol. Cells 16, 78-83.
    • (2003) Mol. Cells , vol.16 , pp. 78-83
    • Lee, J.H.1    Chang, S.H.2    Shim, J.H.3    Lee, J.Y.4    Yoshida, M.5    Kwon, H.6
  • 59
    • 26044461504 scopus 로고    scopus 로고
    • Effects of Ser2 and Tyr6 mutants of BAF53 on cell growth and p53-dependent transcription
    • Lee, J. H., Lee, J. Y., Chang, S. H., Kang, M. J. and Kwon, H. (2005). Effects of Ser2 and Tyr6 mutants of BAF53 on cell growth and p53-dependent transcription. Mol. Cells 19, 289-293.
    • (2005) Mol. Cells , vol.19 , pp. 289-293
    • Lee, J.H.1    Lee, J.Y.2    Chang, S.H.3    Kang, M.J.4    Kwon, H.5
  • 62
    • 0032585538 scopus 로고    scopus 로고
    • Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex
    • Machesky, L. M. and Insall, R. H. (1998). Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex. Curr. Biol. 8, 1347-1356.
    • (1998) Curr. Biol. , vol.8 , pp. 1347-1356
    • Machesky, L.M.1    Insall, R.H.2
  • 63
    • 0028136434 scopus 로고
    • Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography on profilin-agarose
    • Machesky, L. M., Atkinson, S. J., Ampe, C., Vandekerckhove, J. and Pollard, T. D. (1994). Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography on profilin-agarose. J. Cell Biol. 127, 107-115.
    • (1994) J. Cell Biol. , vol.127 , pp. 107-115
    • Machesky, L.M.1    Atkinson, S.J.2    Ampe, C.3    Vandekerckhove, J.4    Pollard, T.D.5
  • 65
    • 32644451623 scopus 로고    scopus 로고
    • Nucleoplasmic beta-actin exists in a dynamic equilibrium between low-mobility polymeric species and rapidly diffusing populations
    • McDonald, D., Carrero, G., Andrin, C., de Vries, G. and Hendzel, M. J. (2006). Nucleoplasmic beta-actin exists in a dynamic equilibrium between low-mobility polymeric species and rapidly diffusing populations. J. Cell Biol. 172, 541-552.
    • (2006) J. Cell Biol. , vol.172 , pp. 541-552
    • McDonald, D.1    Carrero, G.2    Andrin, C.3    de Vries, G.4    Hendzel, M.J.5
  • 66
    • 33750615868 scopus 로고    scopus 로고
    • Caspase-3 cleaves the formin-homology-domain-containing protein FHOD1 during apoptosis to generate a C-terminal fragment that is targeted to the nucleolus
    • Ménard, I., Gervais, F. G., Nicholson, D. W. and Roy, S. (2006). Caspase-3 cleaves the formin-homology-domain-containing protein FHOD1 during apoptosis to generate a C-terminal fragment that is targeted to the nucleolus. Apoptosis 11, 1863-1876.
    • (2006) Apoptosis , vol.11 , pp. 1863-1876
    • Ménard, I.1    Gervais, F.G.2    Nicholson, D.W.3    Roy, S.4
  • 67
    • 33846301667 scopus 로고    scopus 로고
    • Serum response factor: master regulator of the actin cytoskeleton and contractile apparatus
    • Miano, J. M., Long, X. and Fujiwara, K. (2007). Serum response factor: master regulator of the actin cytoskeleton and contractile apparatus. Am. J. Physiol. Cell Physiol. 292, C70-C81.
    • (2007) Am. J. Physiol. Cell Physiol. , vol.292
    • Miano, J.M.1    Long, X.2    Fujiwara, K.3
  • 68
    • 0029815611 scopus 로고    scopus 로고
    • N-WASP, a novel actin-depolymerizing protein, regulates the cortical cytoskeletal rearrangement in a PIP2-dependent manner downstream of tyrosine kinases
    • Miki, H., Miura, K. and Takenawa, T. (1996). N-WASP, a novel actin-depolymerizing protein, regulates the cortical cytoskeletal rearrangement in a PIP2-dependent manner downstream of tyrosine kinases. EMBO J. 15, 5326-5335.
    • (1996) EMBO J , vol.15 , pp. 5326-5335
    • Miki, H.1    Miura, K.2    Takenawa, T.3
  • 69
    • 65549124105 scopus 로고    scopus 로고
    • mDia2 shuttles between the nucleus and the cytoplasm through the importin-alpha/beta- and CRM1-mediated nuclear transport mechanism
    • Miki, T., Okawa, K., Sekimoto, T., Yoneda, Y., Watanabe, S., Ishizaki, T. and Narumiya, S. (2009). mDia2 shuttles between the nucleus and the cytoplasm through the importin-alpha/beta- and CRM1-mediated nuclear transport mechanism. J. Biol. Chem. 284, 5753-5762.
    • (2009) J. Biol. Chem. , vol.284 , pp. 5753-5762
    • Miki, T.1    Okawa, K.2    Sekimoto, T.3    Yoneda, Y.4    Watanabe, S.5    Ishizaki, T.6    Narumiya, S.7
  • 70
    • 0038737042 scopus 로고    scopus 로고
    • Actin dynamics control SRF activity by regulation of its coactivator MAL
    • Miralles, F., Posern, G., Zaromytidou, A. I. and Treisman, R. (2003). Actin dynamics control SRF activity by regulation of its coactivator MAL. Cell 113, 329-342.
    • (2003) Cell , vol.113 , pp. 329-342
    • Miralles, F.1    Posern, G.2    Zaromytidou, A.I.3    Treisman, R.4
  • 71
    • 79955683477 scopus 로고    scopus 로고
    • Nuclear actin polymerization is required for transcriptional reprogramming of Oct4 by oocytes
    • Miyamoto, K., Pasque, V., Jullien, J. and Gurdon, J. B. (2011). Nuclear actin polymerization is required for transcriptional reprogramming of Oct4 by oocytes. Genes Dev. 25, 946-958.
    • (2011) Genes Dev , vol.25 , pp. 946-958
    • Miyamoto, K.1    Pasque, V.2    Jullien, J.3    Gurdon, J.B.4
  • 72
    • 68549122708 scopus 로고    scopus 로고
    • Rho signaling, ROCK and mDia1, in transformation, metastasis and invasion
    • Narumiya, S., Tanji, M. and Ishizaki, T. (2009). Rho signaling, ROCK and mDia1, in transformation, metastasis and invasion. Cancer Metastasis Rev. 28, 65-76.
    • (2009) Cancer Metastasis Rev , vol.28 , pp. 65-76
    • Narumiya, S.1    Tanji, M.2    Ishizaki, T.3
  • 73
    • 1542347695 scopus 로고    scopus 로고
    • Convergence of Wnt, beta-catenin, and cadherin pathways
    • Nelson, W. J. and Nusse, R. (2004). Convergence of Wnt, beta-catenin, and cadherin pathways. Science 303, 1483-1487.
    • (2004) Science , vol.303 , pp. 1483-1487
    • Nelson, W.J.1    Nusse, R.2
  • 75
    • 0034710914 scopus 로고    scopus 로고
    • Adenomatous polyposis coli protein contains two nuclear export signals and shuttles between the nucleus and cytoplasm
    • Neufeld, K. L., Nix, D. A., Bogerd, H., Kang, Y., Beckerle, M. C., Cullen, B. R. and White, R. L. (2000a). Adenomatous polyposis coli protein contains two nuclear export signals and shuttles between the nucleus and cytoplasm. Proc. Natl. Acad. Sci. USA 97, 12085-12090.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12085-12090
    • Neufeld, K.L.1    Nix, D.A.2    Bogerd, H.3    Kang, Y.4    Beckerle, M.C.5    Cullen, B.R.6    White, R.L.7
  • 76
    • 0034576628 scopus 로고    scopus 로고
    • APC-mediated downregulation of beta-catenin activity involves nuclear sequestration and nuclear export
    • Neufeld, K. L., Zhang, F., Cullen, B. R. and White, R. L. (2000b). APC-mediated downregulation of beta-catenin activity involves nuclear sequestration and nuclear export. EMBO Rep. 1, 519-523.
    • (2000) EMBO Rep , vol.1 , pp. 519-523
    • Neufeld, K.L.1    Zhang, F.2    Cullen, B.R.3    White, R.L.4
  • 78
    • 33646487161 scopus 로고    scopus 로고
    • Vertebrate Arp6, a novel nuclear actin-related protein, interacts with heterochromatin protein 1
    • Ohfuchi, E., Kato, M., Sasaki, M., Sugimoto, K., Oma, Y. and Harata, M. (2006). Vertebrate Arp6, a novel nuclear actin-related protein, interacts with heterochromatin protein 1. Eur. J. Cell Biol. 85, 411-421.
    • (2006) Eur. J. Cell Biol. , vol.85 , pp. 411-421
    • Ohfuchi, E.1    Kato, M.2    Sasaki, M.3    Sugimoto, K.4    Oma, Y.5    Harata, M.6
  • 80
    • 0035997387 scopus 로고    scopus 로고
    • Nuclear actin and actinrelated proteins in chromatin remodeling
    • Olave, I. A., Reck-Peterson, S. L. and Crabtree, G. R. (2002). Nuclear actin and actinrelated proteins in chromatin remodeling. Annu. Rev. Biochem. 71, 755-781.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 755-781
    • Olave, I.A.1    Reck-Peterson, S.L.2    Crabtree, G.R.3
  • 81
    • 77951582061 scopus 로고    scopus 로고
    • Linking actin dynamics and gene transcription to drive cellular motile functions
    • Olson, E. N. and Nordheim, A. (2010). Linking actin dynamics and gene transcription to drive cellular motile functions. Nat. Rev. Mol. Cell Biol. 11, 353-365.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 353-365
    • Olson, E.N.1    Nordheim, A.2
  • 82
    • 79952650662 scopus 로고    scopus 로고
    • Actin-related proteins localized in the nucleus: from discovery to novel roles in nuclear organization
    • Oma, Y. and Harata, M. (2011). Actin-related proteins localized in the nucleus: from discovery to novel roles in nuclear organization. Nucleus 2, 38-46.
    • (2011) Nucleus , vol.2 , pp. 38-46
    • Oma, Y.1    Harata, M.2
  • 83
    • 0017338851 scopus 로고
    • Actin-actin bond strength and the conformational change of F-actin
    • Oosawa, F. (1977). Actin-actin bond strength and the conformational change of F-actin. Biorheology 14, 11-19.
    • (1977) Biorheology , vol.14 , pp. 11-19
    • Oosawa, F.1
  • 84
    • 0031005156 scopus 로고    scopus 로고
    • Morphological and molecular processes of polyp formation in Apc(delta716) knockout mice
    • Oshima, H., Oshima, M., Kobayashi, M., Tsutsumi, M. and Taketo, M. M. (1997). Morphological and molecular processes of polyp formation in Apc(delta716) knockout mice. Cancer Res. 57, 1644-1649.
    • (1997) Cancer Res , vol.57 , pp. 1644-1649
    • Oshima, H.1    Oshima, M.2    Kobayashi, M.3    Tsutsumi, M.4    Taketo, M.M.5
  • 85
    • 33749548025 scopus 로고    scopus 로고
    • Cdc42 GEF Tuba regulates the junctional configuration of simple epithelial cells
    • Otani, T., Ichii, T., Aono, S. and Takeichi, M. (2006). Cdc42 GEF Tuba regulates the junctional configuration of simple epithelial cells. J. Cell Biol. 175, 135-146.
    • (2006) J. Cell Biol. , vol.175 , pp. 135-146
    • Otani, T.1    Ichii, T.2    Aono, S.3    Takeichi, M.4
  • 86
    • 12544253725 scopus 로고    scopus 로고
    • The Rho family GTPase Rif induces filopodia through mDia2
    • Pellegrin, S. and Mellor, H. (2005). The Rho family GTPase Rif induces filopodia through mDia2. Curr. Biol. 15, 129-133.
    • (2005) Curr. Biol. , vol.15 , pp. 129-133
    • Pellegrin, S.1    Mellor, H.2
  • 88
  • 89
    • 13444292982 scopus 로고    scopus 로고
    • Drosophila Spire is an actin nucleation factor
    • Quinlan, M. E., Heuser, J. E., Kerkhoff, E. and Mullins, R. D. (2005). Drosophila Spire is an actin nucleation factor. Nature 433, 382-388.
    • (2005) Nature , vol.433 , pp. 382-388
    • Quinlan, M.E.1    Heuser, J.E.2    Kerkhoff, E.3    Mullins, R.D.4
  • 91
    • 7044224754 scopus 로고    scopus 로고
    • Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis
    • Romero, S., Le Clainche, C., Didry, D., Egile, C., Pantaloni, D. and Carlier, M. F. (2004). Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis. Cell 119, 419-429.
    • (2004) Cell , vol.119 , pp. 419-429
    • Romero, S.1    Le Clainche, C.2    Didry, D.3    Egile, C.4    Pantaloni, D.5    Carlier, M.F.6
  • 92
    • 0034739023 scopus 로고    scopus 로고
    • The APC tumour suppressor has a nuclear export function
    • Rosin-Arbesfeld, R., Townsley, F. and Bienz, M. (2000). The APC tumour suppressor has a nuclear export function. Nature 406, 1009-1012.
    • (2000) Nature , vol.406 , pp. 1009-1012
    • Rosin-Arbesfeld, R.1    Townsley, F.2    Bienz, M.3
  • 93
    • 0037416148 scopus 로고    scopus 로고
    • Nuclear export of the APC tumour suppressor controls beta-catenin function in transcription
    • Rosin-Arbesfeld, R., Cliffe, A., Brabletz, T. and Bienz, M. (2003). Nuclear export of the APC tumour suppressor controls beta-catenin function in transcription. EMBO J. 22, 1101-1113.
    • (2003) EMBO J , vol.22 , pp. 1101-1113
    • Rosin-Arbesfeld, R.1    Cliffe, A.2    Brabletz, T.3    Bienz, M.4
  • 94
    • 63049113736 scopus 로고    scopus 로고
    • Regulation of cell-cell adhesion by Abi/Diaphanous complexes
    • Ryu, J. R., Echarri, A., Li, R. and Pendergast, A. M. (2009). Regulation of cell-cell adhesion by Abi/Diaphanous complexes. Mol. Cell. Biol. 29, 1735-1748.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 1735-1748
    • Ryu, J.R.1    Echarri, A.2    Li, R.3    Pendergast, A.M.4
  • 95
    • 0025355476 scopus 로고
    • Isolation of a 5-kilodalton actinsequestering peptide from human blood platelets
    • Safer, D. R., Golla, R. and Nachmias, V. T. (1990). Isolation of a 5-kilodalton actinsequestering peptide from human blood platelets. Proc. Natl. Acad. Sci. USA 87, 2536-2540.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2536-2540
    • Safer, D.R.1    Golla, R.2    Nachmias, V.T.3
  • 98
    • 0021677114 scopus 로고
    • Microinjection of actin-binding proteins and actin antibodies demonstrates involvement of nuclear actin in transcription of lampbrush chromosomes
    • Scheer, U., Hinssen, H., Franke, W. W. and Jockusch, B. M. (1984). Microinjection of actin-binding proteins and actin antibodies demonstrates involvement of nuclear actin in transcription of lampbrush chromosomes. Cell 39, 111-122.
    • (1984) Cell , vol.39 , pp. 111-122
    • Scheer, U.1    Hinssen, H.2    Franke, W.W.3    Jockusch, B.M.4
  • 101
    • 0037684765 scopus 로고    scopus 로고
    • The nucleoskeleton: lamins and actin are major players in essential nuclear functions
    • Shumaker, D. K., Kuczmarski, E. R. and Goldman, R. D. (2003). The nucleoskeleton: lamins and actin are major players in essential nuclear functions. Curr. Opin. Cell Biol. 15, 358-366.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 358-366
    • Shumaker, D.K.1    Kuczmarski, E.R.2    Goldman, R.D.3
  • 102
    • 0242641546 scopus 로고    scopus 로고
    • Exportin 6 a novel nuclear export receptor that is specific for profilin.actin complexes
    • Stüven, T., Hartmann, E. and Görlich, D. (2003). Exportin 6: a novel nuclear export receptor that is specific for profilin.actin complexes. EMBO J. 22, 5928-5940.
    • (2003) EMBO J , vol.22 , pp. 5928-5940
    • Stüven, T.1    Hartmann, E.2    Görlich, D.3
  • 103
    • 0142211212 scopus 로고    scopus 로고
    • Translocation of N-WASP by nuclear localization and export signals into the nucleus modulates expression of HSP90
    • Suetsugu, S. and Takenawa, T. J. (2003). Translocation of N-WASP by nuclear localization and export signals into the nucleus modulates expression of HSP90. J. Biol. Chem. 278, 42515-42523.
    • (2003) J. Biol. Chem. , vol.278 , pp. 42515-42523
    • Suetsugu, S.1    Takenawa, T.J.2
  • 104
    • 0030006284 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization
    • Symons, M., Derry, J. M., Karlak, B., Jiang, S., Lemahieu, V., Mccormick, F., Francke, U. and Abo, A. (1996). Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization. Cell 84, 723-734.
    • (1996) Cell , vol.84 , pp. 723-734
    • Symons, M.1    Derry, J.M.2    Karlak, B.3    Jiang, S.4    Lemahieu, V.5    Mccormick, F.6    Francke, U.7    Abo, A.8
  • 106
    • 0037016718 scopus 로고    scopus 로고
    • The rat homologue of Wiskott-Aldrich syndrome protein (WASP)-interacting protein (WIP) associates with actin filaments, recruits N-WASP from the nucleus, and mediates mobilization of actin from stress fibers in favor of filopodia formation
    • Vetterkind, S., Miki, H., Takenawa, T., Klawitz, I., Scheidtmann, K. H. and Preuss, U. (2002). The rat homologue of Wiskott-Aldrich syndrome protein (WASP)-interacting protein (WIP) associates with actin filaments, recruits N-WASP from the nucleus, and mediates mobilization of actin from stress fibers in favor of filopodia formation. J. Biol. Chem. 277, 87-95.
    • (2002) J. Biol. Chem. , vol.277 , pp. 87-95
    • Vetterkind, S.1    Miki, H.2    Takenawa, T.3    Klawitz, I.4    Scheidtmann, K.H.5    Preuss, U.6
  • 107
    • 38849201066 scopus 로고    scopus 로고
    • BAF53 interacts with p53 and functions in p53-mediated p21-gene transcription
    • Wang, M., Gu, C., Qi, T., Tang, W., Wang, L., Wang, S. and Zeng, X. (2007). BAF53 interacts with p53 and functions in p53-mediated p21-gene transcription. J. Biochem. 142, 613-620.
    • (2007) J. Biochem. , vol.142 , pp. 613-620
    • Wang, M.1    Gu, C.2    Qi, T.3    Tang, W.4    Wang, L.5    Wang, S.6    Zeng, X.7
  • 108
    • 0022390903 scopus 로고
    • Exchange of actin subunits at the leading edge of living fibroblasts: possible role of treadmilling
    • Wang, Y. L. (1985). Exchange of actin subunits at the leading edge of living fibroblasts: possible role of treadmilling. J. Cell Biol. 101, 597-602.
    • (1985) J. Cell Biol. , vol.101 , pp. 597-602
    • Wang, Y.L.1
  • 109
    • 48249083745 scopus 로고    scopus 로고
    • mDia2 induces the actin scaffold for the contractile ring and stabilizes its position during cytokinesis in NIH 3T3 cells
    • Watanabe, S., Ando, Y., Yasuda, S., Hosoya, H., Watanabe, N., Ishizaki, T. and Narumiya, S. (2008). mDia2 induces the actin scaffold for the contractile ring and stabilizes its position during cytokinesis in NIH 3T3 cells. Mol. Biol. Cell 19, 2328-2338.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2328-2338
    • Watanabe, S.1    Ando, Y.2    Yasuda, S.3    Hosoya, H.4    Watanabe, N.5    Ishizaki, T.6    Narumiya, S.7
  • 110
    • 1542304700 scopus 로고    scopus 로고
    • Focal adhesion kinase regulation of N-WASP subcellular localization and function
    • Wu, X., Suetsugu, S., Cooper, L. A., Takenawa, T. and Guan, J. L. (2004). Focal adhesion kinase regulation of N-WASP subcellular localization and function. J. Biol. Chem. 279, 9565-9576.
    • (2004) J. Biol. Chem. , vol.279 , pp. 9565-9576
    • Wu, X.1    Suetsugu, S.2    Cooper, L.A.3    Takenawa, T.4    Guan, J.L.5
  • 111
    • 33745762947 scopus 로고    scopus 로고
    • Regulation of RNA-polymerase-II-dependent transcription by N-WASP and its nuclear-binding partners
    • Wu, X., Yoo, Y., Okuhama, N. N., Tucker, P. W., Liu, G. and Guan, J. L. (2006). Regulation of RNA-polymerase-II-dependent transcription by N-WASP and its nuclear-binding partners. Nat. Cell Biol. 8, 756-763.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 756-763
    • Wu, X.1    Yoo, Y.2    Okuhama, N.N.3    Tucker, P.W.4    Liu, G.5    Guan, J.L.6
  • 112
    • 37249003725 scopus 로고    scopus 로고
    • Novel roles of formin mDia2 in lamellipodia and filopodia formation in motile cells
    • Yang, C., Czech, L., Gerboth, S., Kojima, S., Scita, G. and Svitkina, T. (2007). Novel roles of formin mDia2 in lamellipodia and filopodia formation in motile cells. PLoS Biol. 5, e317.
    • (2007) PLoS Biol , vol.5
    • Yang, C.1    Czech, L.2    Gerboth, S.3    Kojima, S.4    Scita, G.5    Svitkina, T.6
  • 113
    • 34250844333 scopus 로고    scopus 로고
    • SNX9 couples actin assembly to phosphoinositide signals and is required for membrane remodeling during endocytosis
    • Yarar, D., Waterman-Storer, C. M. and Schmid, S. L. (2007). SNX9 couples actin assembly to phosphoinositide signals and is required for membrane remodeling during endocytosis. Dev. Cell 13, 43-56.
    • (2007) Dev. Cell , vol.13 , pp. 43-56
    • Yarar, D.1    Waterman-Storer, C.M.2    Schmid, S.L.3
  • 115
    • 34147105329 scopus 로고    scopus 로고
    • A novel role of the actin-nucleating Arp2/3 complex in the regulation of RNA polymerase ii-dependent transcription
    • Yoo, Y., Wu, X. and Guan, J.-L. (2007). A novel role of the actin-nucleating Arp2/3 complex in the regulation of RNA polymerase ii-dependent transcription. J. Biol. Chem. 282, 7616-7623.
    • (2007) J. Biol. Chem. , vol.282 , pp. 7616-7623
    • Yoo, Y.1    Wu, X.2    Guan, J.-L.3
  • 116
    • 77951231123 scopus 로고    scopus 로고
    • Gas7 functions with N-WASP to regulate the neurite outgrowth of hippocampal neurons
    • You, J. J. and Lin-Chao, S. (2010). Gas7 functions with N-WASP to regulate the neurite outgrowth of hippocampal neurons. J. Biol. Chem. 285, 11652-11666.
    • (2010) J. Biol. Chem. , vol.285 , pp. 11652-11666
    • You, J.J.1    Lin-Chao, S.2
  • 117
    • 0033740339 scopus 로고    scopus 로고
    • Phosphorylation near nuclear localization signal regulates nuclear import of adenomatous polyposis coli protein
    • Zhang, F., White, R. L. and Neufeld, K. L. (2000). Phosphorylation near nuclear localization signal regulates nuclear import of adenomatous polyposis coli protein. Proc. Natl. Acad. Sci. USA 97, 12577-12582.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12577-12582
    • Zhang, F.1    White, R.L.2    Neufeld, K.L.3
  • 118
    • 0035167598 scopus 로고    scopus 로고
    • Cell density and phosphorylation control the subcellular localization of adenomatous polyposis coli protein
    • Zhang, F., White, R. L. and Neufeld, K. L. (2001). Cell density and phosphorylation control the subcellular localization of adenomatous polyposis coli protein. Mol. Cell. Biol. 21, 8143-8156.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 8143-8156
    • Zhang, F.1    White, R.L.2    Neufeld, K.L.3
  • 121
    • 84857852663 scopus 로고    scopus 로고
    • Actin binding to WH2 domains regulates nuclear import of the multifunctional actin regulator JMY
    • Zuchero, J. B., Belin, B. and Dyche Mullins, R. (2012). Actin binding to WH2 domains regulates nuclear import of the multifunctional actin regulator JMY. Mol Biol. Cell 23, 853-863.
    • (2012) Mol Biol. Cell , vol.23 , pp. 853-863
    • Zuchero, J.B.1    Belin, B.2    Dyche Mullins, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.