메뉴 건너뛰기




Volumn 24, Issue 7, 2013, Pages 982-994

Visualization of actin filaments and monomers in somatic cell nuclei

Author keywords

[No Author keywords available]

Indexed keywords

MONOMER;

EID: 84875456639     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E12-09-0685     Document Type: Article
Times cited : (128)

References (51)
  • 1
    • 0032533444 scopus 로고    scopus 로고
    • Structural comparisons of calponin homology domains: Implications for actin binding
    • Bañuelos S, Saraste M, Djinovic' Carugo K (1998). Structural comparisons of calponin homology domains: implications for actin binding. Structure 6, 1419-1431. (Pubitemid 28541885)
    • (1998) Structure , vol.6 , Issue.11 , pp. 1419-1431
    • Banuelos, S.1    Saraste, M.2    Carugo, K.D.3
  • 2
    • 33644747345 scopus 로고    scopus 로고
    • A selective block of nuclear actin export stabilizes the giant nuclei of Xenopus oocytes
    • DOI 10.1038/ncb1357, PII N1357
    • Bohnsack MT, Stüven T, Kuhn C, Cordes VC, Gorlich D (2006). A selective block of nuclear actin export stabilizes the giant nuclei of Xenopus oocytes. Nat Cell Biol 8, 257-263. (Pubitemid 43336067)
    • (2006) Nature Cell Biology , vol.8 , Issue.3 , pp. 257-263
    • Bohnsack, M.T.1    Stuven, T.2    Kuhn, C.3    Cordes, V.C.4    Gorlich, D.5
  • 3
    • 33846453991 scopus 로고    scopus 로고
    • A receptors in growth cones detected by a speed correlation index
    • DOI 10.1529/biophysj.106.094524
    • Bouzigues C, Dahan M (2007). Transient directed motions of GABAA receptors in growth cones detected by a speed correlation index. Biophys J 92, 654-660. (Pubitemid 46145797)
    • (2007) Biophysical Journal , vol.92 , Issue.2 , pp. 654-660
    • Bouzigues, C.1    Dahan, M.2
  • 4
    • 79952723337 scopus 로고    scopus 로고
    • Active liquid-like behavior of nucleoli determines their size and shape in Xenopus laevis oocytes
    • Brangwynne CP, Mitchison TJ, Hyman AA (2011). Active liquid-like behavior of nucleoli determines their size and shape in Xenopus laevis oocytes. Proc Natl Acad Sci USA 108, 4334-4339.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 4334-4339
    • Brangwynne, C.P.1    Mitchison, T.J.2    Hyman, A.A.3
  • 5
    • 35649027944 scopus 로고    scopus 로고
    • Versatile fluorescent probes for actin filaments based on the actin-binding domain of utrophin
    • DOI 10.1002/cm.20226
    • Burkel BM, Von Dassow G, Bement WM (2007). Versatile fluorescent probes for actin filaments based on the actin-binding domain of utrophin. Cell Motil. Cytoskeleton 64, 822-832. (Pubitemid 350035031)
    • (2007) Cell Motility and the Cytoskeleton , vol.64 , Issue.11 , pp. 822-832
    • Burkel, B.M.1    Von Dassow, G.2    Bement, W.M.3
  • 6
    • 33845792555 scopus 로고    scopus 로고
    • CellProfiler: Image analysis software for identifying and quantifying cell phenotypes
    • Carpenter AE et al. (2006). CellProfiler: image analysis software for identifying and quantifying cell phenotypes. Genome Biol 7, R100.
    • (2006) Genome Biol , vol.7
    • Carpenter, A.E.1
  • 7
    • 0017716157 scopus 로고
    • Diffusible and bound actin in nuclei of Xenopus laevis oocytes
    • Clark T, Merriam R (1977). Diffusible and bound actin in nuclei of Xenopus laevis oocytes. Cell 12, 881-891.
    • (1977) Cell , vol.12 , pp. 881-891
    • Clark, T.1    Merriam, R.2
  • 8
    • 0018601589 scopus 로고
    • An actin filament matrix in hand-isolated nuclei of X. laevis oocytes
    • Clark T, Rosenbaum J (1979). An actin filament matrix in hand-isolated nuclei of X. laevis oocytes. Cell 18, 1101-1108. (Pubitemid 10172649)
    • (1979) Cell , vol.18 , Issue.4 , pp. 1101-1108
    • Clark, T.G.1    Rosenbaum, J.L.2
  • 9
    • 80054046064 scopus 로고    scopus 로고
    • Dynamic remodeling of the actin cytoskeleton by FMNL1γ is required for structural maintenance of the Golgi complex
    • Colón-Franco JM, Gomez TS, Billadeau DD (2011). Dynamic remodeling of the actin cytoskeleton by FMNL1γ is required for structural maintenance of the Golgi complex. J Cell Sci 124, 3118-3126.
    • (2011) J Cell Sci , vol.124 , pp. 3118-3126
    • Colón-Franco, J.M.1    Gomez, T.S.2    Billadeau, D.D.3
  • 10
    • 80455168204 scopus 로고    scopus 로고
    • Nuclear actin and myosins: Life without filaments
    • de Lanerolle P, Serebryannyy L (2011). Nuclear actin and myosins: life without filaments. Nat Cell Biol 13, 1282-1288.
    • (2011) Nat Cell Biol , vol.13 , pp. 1282-1288
    • De Lanerolle, P.1    Serebryannyy, L.2
  • 13
    • 44449139885 scopus 로고    scopus 로고
    • Chromatin remodelling and actin reorganization
    • Farrants AO (2008). Chromatin remodelling and actin reorganization. FEBS Lett 585, 2041-2050.
    • (2008) FEBS Lett , vol.585 , pp. 2041-2050
    • Farrants, A.O.1
  • 14
    • 1242316973 scopus 로고    scopus 로고
    • An actin-myosin complex on actively transcribing genes
    • DOI 10.1016/j.yexcr.2003.10.028
    • Fomproix N, Percipalle P (2004). An actin-myosin complex on actively transcribing genes. Exp Cell Res 294, 140-148. (Pubitemid 38229788)
    • (2004) Experimental Cell Research , vol.294 , Issue.1 , pp. 140-148
    • Fomproix, N.1    Percipalle, P.2
  • 16
    • 77951879206 scopus 로고    scopus 로고
    • Examining the contents of isolated Xenopus germinal vesicles
    • Gall JG, Wu Z (2010). Examining the contents of isolated Xenopus germinal vesicles. Methods 51, 45-51.
    • (2010) Methods , vol.51 , pp. 45-51
    • Gall, J.G.1    Wu, Z.2
  • 17
    • 43449111772 scopus 로고    scopus 로고
    • Modulation of RNA Polymerase Assembly Dynamics in Transcriptional Regulation
    • DOI 10.1016/j.molcel.2008.04.021, PII S1097276508003237
    • Gorski S, Snyder S, John S, Grummt I, Misteli T (2008). Modulation of RNA polymerase assembly dynamics in transcriptional regulation. Mol Cell 30, 486-497. (Pubitemid 351672375)
    • (2008) Molecular Cell , vol.30 , Issue.4 , pp. 486-497
    • Gorski, S.A.1    Snyder, S.K.2    John, S.3    Grummt, I.4    Misteli, T.5
  • 20
    • 79951780039 scopus 로고    scopus 로고
    • Coronin 2A mediates actin-dependent de-repression of inflammatory response genes
    • Huang W et al. (2011). Coronin 2A mediates actin-dependent de-repression of inflammatory response genes. Nature 470, 414-418.
    • (2011) Nature , vol.470 , pp. 414-418
    • Huang, W.1
  • 21
    • 0026550804 scopus 로고
    • The KKRKK sequence is involved in head-shock induced nuclear translocation of the 18-kDa actin-binding protein, cofilin
    • Iida K, Matsumoto S, Yahara I (1992). The KKRKK sequence is involved in head-shock induced nuclear translocation of the 18-kDa actin-binding protein, cofilin. Cell Struct Funct 17, 39-46.
    • (1992) Cell Struct Funct , vol.17 , pp. 39-46
    • Iida, K.1    Matsumoto, S.2    Yahara, I.3
  • 23
    • 0033572690 scopus 로고    scopus 로고
    • Crystal structure of the actin-binding region of utrophin reveals a head-to-tail dimer
    • DOI 10.1016/S0969-2126(00)88344-6
    • Keep NH, Winder SJ, Moores CA, Walke S, Norwood FL, Kendrick-Jones J (1999). Crystal structure of the actin-binding region of utrophin reveals a head-to-tail dimer. Structure 7, 1539-1546. (Pubitemid 30007239)
    • (1999) Structure , vol.7 , Issue.12 , pp. 1539-1546
    • Keep, N.H.1    Winder, S.J.2    Moores, C.A.3    Walke, S.4    Norwood, F.L.M.5    Kendrick-Jones, J.6
  • 24
    • 3042777656 scopus 로고    scopus 로고
    • Actin-and protien-4.1-containing filaments link nuclear pore complexes to subnuclear organelles in Xenopus oocyte nuclei
    • DOI 10.1242/jcs.01098
    • Kiseleva E, Drummond SP, Goldberg MW, Rutherford SA, Allen TD, Wilson KL (2004). Actin- and protein-4.1-containing filaments link nuclear pore complexes to subnuclear organelles in Xenopus oocyte nuclei. J Cell Sci 117, 2481-2490. (Pubitemid 38877844)
    • (2004) Journal of Cell Science , vol.117 , Issue.12 , pp. 2481-2490
    • Kiseleva, E.1    Drummond, S.P.2    Goldberg, M.W.3    Rutherford, S.A.4    Allen, T.D.5    Wilson, K.L.6
  • 26
    • 77951159377 scopus 로고    scopus 로고
    • Molecular mechanisms underlying nucleoplasmic shuttling of actinin-4
    • Kumeta M, Yoshimura SH, Harata M, Takeyasu K (2010). Molecular mechanisms underlying nucleoplasmic shuttling of actinin-4. J Cell Sci 123, 1020-1031.
    • (2010) J Cell Sci , vol.123 , pp. 1020-1031
    • Kumeta, M.1    Yoshimura, S.H.2    Harata, M.3    Takeyasu, K.4
  • 27
    • 3142661809 scopus 로고    scopus 로고
    • Rapid inhibition of cancer cell growth induced by lentiviral delivery and expression of mutant-template telomerase RNA and anti-telomerase short-interfering RNA
    • DOI 10.1158/0008-5472.CAN-04-0953
    • Li S, Rosenberg JE, Donjacour AA, Botchkina IL, Hom YK, Cunha GR, Blackburn EH (2004). Rapid inhibition of cancer cell growth induced by lentiviral delivery and expression of mutant-template telomerase RNA and Anti-telomerase short-interfering RNA. Cancer Res 64, 4833-40. (Pubitemid 38924527)
    • (2004) Cancer Research , vol.64 , Issue.14 , pp. 4833-4840
    • Li, S.1    Rosenberg, J.E.2    Donjacour, A.A.3    Botchkina, I.L.4    Hom, Y.K.5    Cunha, G.R.6    Blackburn, E.H.7
  • 29
    • 32644451623 scopus 로고    scopus 로고
    • Nucleoplasmic β-actin exists in a dynamic equilibrium between low-mobility polymeric species and rapidly diffusing populations
    • DOI 10.1083/jcb.200507101
    • McDonald D, Carrero G, Andrin C, de Vries G, Hendzel MJ (2006). Nucleoplasmic b-actin exists in a dynamic equilibrium between low-mobility polymeric species and rapidly diffusing populations. J Cell Biol 172, 541-552. (Pubitemid 43243875)
    • (2006) Journal of Cell Biology , vol.172 , Issue.4 , pp. 541-552
    • McDonald, D.1    Carrero, G.2    Andrin, C.3    De Vries, G.4    Hendzel, M.J.5
  • 31
    • 57149087850 scopus 로고    scopus 로고
    • Molecular basis for G-actin binding to RPEL motifs from the serum response factor coactivator MAL
    • Mouilleron S, Guettler S, Langer CA, Treisman R, McDonald NQ (2008). Molecular basis for G-actin binding to RPEL motifs from the serum response factor coactivator MAL. EMBO J 27, 3198-208.
    • (2008) EMBO J , vol.27 , pp. 3198-3208
    • Mouilleron, S.1    Guettler, S.2    Langer, C.A.3    Treisman, R.4    McDonald, N.Q.5
  • 32
    • 0037515668 scopus 로고    scopus 로고
    • Latrunculin B or ATP depletion induces cofilin-dependent translocation of actin into nuclei of mast cells
    • DOI 10.1074/jbc.M206393200
    • Pendleton A, Pope B, Weeds A, Koffer A (2003). Latrunculin B or ATP depletion induces cofilin-dependent translocation of actin into nuclei of mast cells. J Biol Chem 278, 14394-14400. (Pubitemid 36799991)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.16 , pp. 14394-14400
    • Pendleton, A.1    Pope, B.2    Weeds, A.3    Koffer, A.4
  • 36
    • 46249118002 scopus 로고    scopus 로고
    • Lifeact: A versatile marker to visualize F-actin
    • Riedl J et al. (2008). Lifeact: a versatile marker to visualize F-actin. Nat Meth 5, 606-607.
    • (2008) Nat Meth , vol.5 , pp. 606-607
    • Riedl, J.1
  • 37
    • 0029163176 scopus 로고
    • Single-particle tracking: Effects of corrals
    • Saxton MJ (1995). Single-particle tracking: effects of corrals. Biophys J 69, 389-98.
    • (1995) Biophys J , vol.69 , pp. 389-398
    • Saxton, M.J.1
  • 38
    • 0021677114 scopus 로고
    • Microinjection of actin-binding proteins and actin antibodies demonstrates involvement of nuclear actin in transcription of lampbrush chromosomes
    • Scheer U, Hinssen S, Franke WW, Jockusch BM (1984). Microinjection of actin-binding proteins and actin antibodies demonstrates involvement of nuclear actin in transcription of lampbrush chromosomes. Cell 39, 111-112.
    • (1984) Cell , vol.39 , pp. 111-112
    • Scheer, U.1    Hinssen, S.2    Franke, W.W.3    Jockusch, B.M.4
  • 39
    • 28944449940 scopus 로고    scopus 로고
    • Conformation-specific antibodies reveal distinct actin structures in the nucleus and the cytoplasm
    • DOI 10.1016/j.jsb.2005.09.003, PII S1047847705001930
    • Schoenenberger CA, Buchmeier S, Boerries M, Sütterlin R, Aebi U, Jockusch BM (2005). Conformation-specific antibodies reveal distinct actin structures in the nucleus and in the cytoplasm. J Struct Biol 152, 157-168. (Pubitemid 41785513)
    • (2005) Journal of Structural Biology , vol.152 , Issue.3 , pp. 157-168
    • Schoenenberger, C.-A.1    Buchmeier, S.2    Boerries, M.3    Sutterlin, R.4    Aebi, U.5    Jockusch, B.M.6
  • 40
    • 0032796310 scopus 로고    scopus 로고
    • Annealing accounts for the length of actin filaments formed by spontaneous polymerization
    • Sept D, Xu J, Pollard TD, McCammon JA (1999). Annealing accounts for the length of actin filaments formed by spontaneous polymerization. Biophys J 77, 2911-2919.
    • (1999) Biophys J , vol.77 , pp. 2911-2919
    • Sept, D.1    Xu, J.2    Pollard, T.D.3    McCammon, J.A.4
  • 41
    • 58049195492 scopus 로고    scopus 로고
    • The A- and B-type nuclear lamin networks: Microdomains involved in chromatin organization and transcription
    • Shimi T et al. (2008). The A- and B-type nuclear lamin networks: microdomains involved in chromatin organization and transcription. Genes Dev 22, 3409-3421.
    • (2008) Genes Dev , vol.22 , pp. 3409-3421
    • Shimi, T.1
  • 42
    • 0031720742 scopus 로고    scopus 로고
    • A factor required for nonsense-mediated mRNA decay in yeast is exported from the nucleus to the cytoplasm by a nuclear export signal sequence
    • Shirley RL, Lelivelt MJ, Schenkman LR, Dahlseid JN, Culbertson MR (1998). A factor required for nonsense-mediated mRNA decay in yeast is exported from the nucleus to the cytoplasm by a nuclear export signal sequence. J Cell Sci 111, 3129-3143. (Pubitemid 28532424)
    • (1998) Journal of Cell Science , vol.111 , Issue.21 , pp. 3129-3143
    • Shirley, R.L.1    Lelivelt, M.J.2    Schenkman, L.R.3    Dahlseid, J.N.4    Culbertson, M.R.5
  • 44
    • 42149142178 scopus 로고    scopus 로고
    • Micro-Manager: Open source software for light microscope imaging
    • Stuurman N, Amodaj N, Vale RD (2007). Micro-Manager: open source software for light microscope imaging. Microscopy Today 15, 42-43.
    • (2007) Microscopy Today , vol.15 , pp. 42-43
    • Stuurman, N.1    Amodaj, N.2    Vale, R.D.3
  • 45
    • 0242641546 scopus 로고    scopus 로고
    • Exportin 6: A novel nuclear export receptor that is specific for profilin-actin complexes
    • DOI 10.1093/emboj/cdg565
    • Stüven T, Hartmann E, Görlich D (2003). Exportin 6: a novel nuclear export receptor that is specific for profiling-actin complexes. EMBO J 22, 5928-5940. (Pubitemid 37408828)
    • (2003) EMBO Journal , vol.22 , Issue.21 , pp. 5928-5940
    • Stuven, T.1    Hartmann, E.2    Gorlich, D.3
  • 46
    • 77953494844 scopus 로고    scopus 로고
    • Bacterial chromosomal loci move subdiffusively through a viscoelastic cytoplasm
    • Weber SC, Spakowitz AJ, Theriot JA (2010a). Bacterial chromosomal loci move subdiffusively through a viscoelastic cytoplasm. Phys Rev Lett 104, 238102.
    • (2010) Phys Rev Lett , vol.104 , pp. 238102
    • Weber, S.C.1    Spakowitz, A.J.2    Theriot, J.A.3
  • 49
    • 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, Tucker PW, Liu G, Guan 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.3    Tucker, P.W.4    Liu, G.5    Guan, L.6
  • 50
    • 38949127670 scopus 로고    scopus 로고
    • Nuclear myosin I acts in concert with polymeric actin to drive RNA polymerase I transcription
    • DOI 10.1101/gad.455908
    • Ye J, Zhao J, Hoffmann-Rohrer U, Grummt I (2008). Nuclear myosin I acts in concert with polymeric actin to drive RNA polymerase I transcription. Genes Dev 22, 322-330. (Pubitemid 351214274)
    • (2008) Genes and Development , vol.22 , Issue.3 , pp. 322-330
    • Ye, J.1    Zhao, J.2    Hoffmann-Rohrer, U.3    Grummt, I.4
  • 51
    • 0032567080 scopus 로고    scopus 로고
    • Rapid and phosphoinositol-dependent binding of the SWI/SNF-like BAF complex to chromatin after T-lymphocyte receptor signaling
    • Zhao K, Wang W, Rando OJ, Xue Y, Swiderek K, Kuo A, Crabtree GR (1998). Rapid and phosphoinositol-dependent binding of the SWI/SNF-like BAF complex to chromatin after T-lymphocyte receptor signaling. Cell 95, 625-638.
    • (1998) Cell , vol.95 , pp. 625-638
    • Zhao, K.1    Wang, W.2    Rando, O.J.3    Xue, Y.4    Swiderek, K.5    Kuo, A.6    Crabtree, G.R.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.