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Volumn 14, Issue 11, 2013, Pages 693-697

To be or not to be assembled: Progressing into nuclear actin filaments

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; SCAFFOLD PROTEIN;

EID: 84886314384     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm3681     Document Type: Article
Times cited : (93)

References (46)
  • 1
    • 28944449940 scopus 로고    scopus 로고
    • Conformation-specific antibodies reveal distinct actin structures in the nucleus and the cytoplasm
    • Schoenenberger, C. A. et al. Conformation-specific antibodies reveal distinct actin structures in the nucleus and the cytoplasm. J. Struct. Biol. 152, 157-168 (2005).
    • (2005) J. Struct. Biol. , vol.152 , pp. 157-168
    • Schoenenberger, C.A.1
  • 2
    • 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. & Jockusch, B. M. Microinjection of actin-binding proteins and actin antibodies demonstrates involvement of nuclear actin in transcription of lampbrush chromosomes. Cell 39, 111-122(1984).
    • (1984) Cell , vol.39 , pp. 111-122
    • Scheer, U.1    Hinssen, H.2    Franke, W.W.3    Jockusch, B.M.4
  • 3
    • 0021513584 scopus 로고
    • Is actin a transcription initiation factor for RNA polymerase B?
    • Egly, J. M., Miyamoto, N. G., Moncollin, V. & Chambon, P. Is actin a transcription initiation factor for RNA polymerase B? EMBO J. 3, 2363-2371 (1984).
    • (1984) EMBO J. , vol.3 , pp. 2363-2371
    • Egly, J.M.1    Miyamoto, N.G.2    Moncollin, V.3    Chambon, P.4
  • 4
    • 85052276775 scopus 로고    scopus 로고
    • Co-transcriptional nuclear actin dynamics
    • Percipalle, P. Co-transcriptional nuclear actin dynamics. Nucleus 4, 43-52 (2013).
    • (2013) Nucleus , vol.4 , pp. 43-52
    • Percipalle, P.1
  • 5
    • 84883456432 scopus 로고    scopus 로고
    • Transcriptional regulation and nuclear reprogramming: Roles of nuclear actin and actin-binding proteins
    • Miyamoto, K. & Gurdon, J. B. Transcriptional regulation and nuclear reprogramming: roles of nuclear actin and actin-binding proteins. Cell. Mol. Life Sci. 70, 3289-3302 (2012).
    • (2012) Cell. Mol. Life Sci. , vol.70 , pp. 3289-3302
    • Miyamoto, K.1    Gurdon, J.B.2
  • 6
    • 80455168204 scopus 로고    scopus 로고
    • Nuclear actin and myosins: Life without filaments
    • de Lanerolle, P. & Serebryannyy, L. Nuclear actin and myosins: life without filaments. Nature Cell Biol. 13, 1282-1288 (2011).
    • (2011) Nature Cell Biol. , vol.13 , pp. 1282-1288
    • De Lanerolle, P.1    Serebryannyy, L.2
  • 7
    • 34250849566 scopus 로고    scopus 로고
    • Nuclear actin regulates dynamic subcellular localization and activity of the SRF cofactor MAL
    • Vartiainen, M. K., Guettler, S., Larijani, B. & Treisman, R. Nuclear actin regulates dynamic subcellular localization and activity of the SRF cofactor MAL. Science 316, 1749-1752 (2007).
    • (2007) Science , vol.316 , pp. 1749-1752
    • Vartiainen, M.K.1    Guettler, S.2    Larijani, B.3    Treisman, R.4
  • 8
    • 53549100755 scopus 로고    scopus 로고
    • The histone acetyltransferase PCAF associates with actin and hnRNP U for RNA polymerase II transcription
    • Obrdlik, A. et al. The histone acetyltransferase PCAF associates with actin and hnRNP U for RNA polymerase II transcription. Mol. Cell. Biol. 28, 6342-6357 (2008).
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 6342-6357
    • Obrdlik, A.1
  • 9
    • 0037089149 scopus 로고    scopus 로고
    • Nuclear actin is associated with a specific subset of hnRNP A/B-type proteins
    • Percipalle, P. et al. Nuclear actin is associated with a specific subset of hnRNP A/B-type proteins. Nucleic Acid. Res. 30, 1725-1734 (2002).
    • (2002) Nucleic Acid. Res. , vol.30 , pp. 1725-1734
    • Percipalle, P.1
  • 10
    • 0037637576 scopus 로고    scopus 로고
    • An actin-ribonucleoprotein interaction is involved in transcription by RNA polymerase II
    • Percipalle, P. et al. An actin-ribonucleoprotein interaction is involved in transcription by RNA polymerase II. Proc. Nat. Acad. Sci. USA 100, 6475-6480 (2003).
    • (2003) Proc. Nat. Acad. Sci. USA , vol.100 , pp. 6475-6480
    • Percipalle, P.1
  • 11
    • 79955396454 scopus 로고    scopus 로고
    • G-actin participates in RNA polymerase II-dependent transcription elongation by recruiting positive transcription elongation factor b (P-TEFb)
    • Qi, T. et al. G-actin participates in RNA polymerase II-dependent transcription elongation by recruiting positive transcription elongation factor b (P-TEFb). J. Biol. Chem. 286, 15171-15181 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 15171-15181
    • Qi, T.1
  • 12
    • 79957907752 scopus 로고    scopus 로고
    • Structural biochemistry of nuclear actin-related proteins 4 and 8 reveals their interaction with actin
    • Fenn, S. et al. Structural biochemistry of nuclear actin-related proteins 4 and 8 reveals their interaction with actin. EMBO J. 30, 2153-2166 (2011).
    • (2011) EMBO J. , vol.30 , pp. 2153-2166
    • Fenn, S.1
  • 14
    • 32644451623 scopus 로고    scopus 로고
    • Nucleoplasmic β-actin exists in a dynamic equilibrium between low-mobility polymeric species and rapidly diffusing populations
    • McDonald, D., Carrero, G., Andrin, C., de Vries, G. & Hendzel, M. J. Nucleoplasmic β-actin exists in a dynamic equilibrium between low-mobility polymeric species and rapidly diffusing populations. J. Cell Biol. 172, 541-552 (2006).
    • (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
  • 15
    • 38949127670 scopus 로고    scopus 로고
    • Nuclear myosin i acts in concert with polymeric actin to drive RNA polymerase i transcription
    • Ye, J., Zhao, J., Hoffmann-Rohrer, U. & Grummt, I. Nuclear myosin I acts in concert with polymeric actin to drive RNA polymerase I transcription. Genes Dev. 22, 322-330 (2008).
    • (2008) Genes Dev. , vol.22 , pp. 322-330
    • Ye, J.1    Zhao, J.2    Hoffmann-Rohrer, U.3    Grummt, I.4
  • 16
    • 58049208232 scopus 로고    scopus 로고
    • Enhancing nuclear receptor-induced transcription requires nuclear motor and LSD1-dependent gene networking in interchromatin granules
    • Hu, Q. et al. Enhancing nuclear receptor-induced transcription requires nuclear motor and LSD1-dependent gene networking in interchromatin granules. Proc. Natl Acad. Sci. USA 105, 19199-19204 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 19199-19204
    • Hu, Q.1
  • 17
    • 37249038708 scopus 로고    scopus 로고
    • Actin-dependent intranuclear repositioning of an active gene locus
    • Dundr, M. et al. Actin-dependent intranuclear repositioning of an active gene locus in vivo. J. Cell Biol. 179, 1095-1103 (2007).
    • (2007) Vivo. J. Cell Biol. , vol.179 , pp. 1095-1103
    • Dundr, M.1
  • 18
    • 33646021963 scopus 로고    scopus 로고
    • Long-range directional movement of an interphase chromosome site
    • Chuang, C. H. et al. Long-range directional movement of an interphase chromosome site. Curr. Biol. 16, 825-831 (2006).
    • (2006) Curr. Biol. , vol.16 , pp. 825-831
    • Chuang, C.H.1
  • 19
    • 0036170782 scopus 로고    scopus 로고
    • Metabolic-energy-dependent movement of PML bodies within the mammalian cell nucleus
    • Muratani, M. et al. Metabolic-energy-dependent movement of PML bodies within the mammalian cell nucleus. Nature Cell Biol. 4, 106-110 (2002).
    • (2002) Nature Cell Biol. , vol.4 , pp. 106-110
    • Muratani, M.1
  • 20
    • 84875998417 scopus 로고    scopus 로고
    • Nuclear myosin 1c facilitates the chromatin modifications required to activate rRNA gene transcription and cell cycle progression
    • Sarshad, A. et al. Nuclear myosin 1c facilitates the chromatin modifications required to activate rRNA gene transcription and cell cycle progression. PLoS Genet. 9, e1003397 (2013).
    • (2013) PLoS Genet. , vol.9
    • Sarshad, A.1
  • 21
    • 79951780039 scopus 로고    scopus 로고
    • Coronin 2A mediates actin-dependent de-repression of inflammatory response genes
    • Huang, W. et al. Coronin 2A mediates actin-dependent de-repression of inflammatory response genes. Nature 470, 414-418 (2011).
    • (2011) Nature , vol.470 , pp. 414-418
    • Huang, W.1
  • 22
    • 33745762947 scopus 로고    scopus 로고
    • Regulation of RNA-polymerase II-dependent transcription by N-WASP and its nuclear-binding partners
    • Wu, X. et al. Regulation of RNA-polymerase II-dependent transcription by N-WASP and its nuclear-binding partners. Nature Cell Biol. 8, 756-763 (2006).
    • (2006) Nature Cell Biol. , vol.8 , pp. 756-763
    • Wu, X.1
  • 23
    • 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. & Guan, J. L. 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).
    • (2007) J. Biol. Chem. , vol.282 , pp. 7616-7623
    • Yoo, Y.1    Wu, X.2    Guan, J.L.3
  • 24
    • 79952637148 scopus 로고    scopus 로고
    • The F-actin severing protein cofilin-1 is required for RNA polymerase II transcription elongation
    • Obrdlik, A. & Percipalle, P. The F-actin severing protein cofilin-1 is required for RNA polymerase II transcription elongation Nucleus 2, 72-79 (2011).
    • (2011) Nucleus , vol.2 , pp. 72-79
    • Obrdlik, A.1    Percipalle, P.2
  • 25
    • 33644747345 scopus 로고    scopus 로고
    • A selective block of nuclear actin export stabilizes the giant nuclei of Xenopus oocytes
    • Bohnsack, M. T., Stuven, T., Kuhn, C., Cordes, V. C. & Gorlich, D. A selective block of nuclear actin export stabilizes the giant nuclei of Xenopus oocytes. Nature Cell Biol. 8, 257-263 (2006).
    • (2006) Nature Cell Biol. , vol.8 , pp. 257-263
    • Bohnsack, M.T.1    Stuven, T.2    Kuhn, C.3    Cordes, V.C.4    Gorlich, D.5
  • 26
    • 33646073458 scopus 로고    scopus 로고
    • Exporting actin
    • Gall, J. G. Exporting actin. Nature Cell Biol. 8, 205-207 (2006).
    • (2006) Nature Cell Biol. , vol.8 , pp. 205-207
    • Gall, J.G.1
  • 27
    • 84880193973 scopus 로고    scopus 로고
    • The nuclear F-actin interactome of Xenopus oocytes reveals an actin-bundling kinesin that is essential for meiotic cytokinesis
    • Samwer, M. et al. The nuclear F-actin interactome of Xenopus oocytes reveals an actin-bundling kinesin that is essential for meiotic cytokinesis. EMBO J.32, 1886-1902 (2013).
    • (2013) EMBO J. , vol.32 , pp. 1886-1902
    • Samwer, M.1
  • 28
    • 79955683477 scopus 로고    scopus 로고
    • Nuclear actin polymerization is required for transcriptional reprogramming of Oct4 by oocytes
    • Miyamoto, K., Pasque, V., Jullien, J. & Gurdon, J. B. Nuclear actin polymerization is required for transcriptional reprogramming of Oct4 by oocytes. Genes Dev. 25, 946-958 (2011).
    • (2011) Genes Dev. , vol.25 , pp. 946-958
    • Miyamoto, K.1    Pasque, V.2    Jullien, J.3    Gurdon, J.B.4
  • 29
    • 23844466646 scopus 로고    scopus 로고
    • A contractile nuclear actin network drives chromosome congression in oocytes
    • Lenart, P. et al. A contractile nuclear actin network drives chromosome congression in oocytes. Nature 436, 812-818 (2005).
    • (2005) Nature , vol.436 , pp. 812-818
    • Lenart, P.1
  • 30
    • 0028833396 scopus 로고
    • Utrophin actin binding domain: Analysis of actin binding and cellular targeting
    • Winder, S. J. et al. Utrophin actin binding domain: analysis of actin binding and cellular targeting. J. Cell Sci. 108, 63-71 (1995).
    • (1995) J. Cell Sci. , vol.108 , pp. 63-71
    • Winder, S.J.1
  • 31
    • 35649027944 scopus 로고    scopus 로고
    • Versatile fluorescent probes for actin filaments based on the actin-binding domain of utrophin
    • Burkel, B. M., von Dassow, G. & Bement, W. M. Versatile fluorescent probes for actin filaments based on the actin-binding domain of utrophin. Cell. Motil. Cytoskeleton 64, 822-832 (2007).
    • (2007) Cell. Motil. Cytoskeleton , vol.64 , pp. 822-832
    • Burkel, B.M.1    Von Dassow, G.2    Bement, W.M.3
  • 32
    • 84856133266 scopus 로고    scopus 로고
    • An actin-dependent mechanism for long-range vesicle transport
    • Schuh, M. An actin-dependent mechanism for long-range vesicle transport. Nature Cell Biol. 13, 1431-1436 (2011).
    • (2011) Nature Cell Biol. , vol.13 , pp. 1431-1436
    • Schuh, M.1
  • 33
    • 84875456639 scopus 로고    scopus 로고
    • Visualization of actin filaments and monomers in somatic cell nuclei
    • Belin, B. J., Cimini, B. A., Blackburn, E. H. & Mullins, R. D. Visualization of actin filaments and monomers in somatic cell nuclei. Mol. Biol. Cell 24, 982-994 (2013).
    • (2013) Mol. Biol. Cell , vol.24 , pp. 982-994
    • Belin, B.J.1    Cimini, B.A.2    Blackburn, E.H.3    Mullins, R.D.4
  • 34
    • 84877742076 scopus 로고    scopus 로고
    • Nuclear actin network assembly by formins regulates the SRF coactivator MAL
    • Baarlink, C., Wang, H. & Grosse, R. Nuclear actin network assembly by formins regulates the SRF coactivator MAL. Science 340, 864-867 (2013).
    • (2013) Science , vol.340 , pp. 864-867
    • Baarlink, C.1    Wang, H.2    Grosse, R.3
  • 35
    • 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
  • 36
    • 44449142302 scopus 로고    scopus 로고
    • Nuclear actin dynamics - From form to function
    • Vartiainen, M. K. Nuclear actin dynamics - from form to function. FEBS Lett. 582, 2033-2040 (2008).
    • (2008) FEBS Lett. , vol.582 , pp. 2033-2040
    • Vartiainen, M.K.1
  • 37
    • 84869105145 scopus 로고    scopus 로고
    • Actin nucleators in the nucleus: An emerging theme
    • Weston, L., Coutts, A. S. & La Thangue, N. B. Actin nucleators in the nucleus: an emerging theme. J. Cell Sci. 125, 3519-3527 (2012).
    • (2012) J. Cell Sci. , vol.125 , pp. 3519-3527
    • Weston, L.1    Coutts, A.S.2    La Thangue, N.B.3
  • 38
    • 17844390892 scopus 로고    scopus 로고
    • Evolution of the gelsolin family of actin-binding proteins as novel transcriptional coactivators
    • Archer, S. K., Claudianos, C. & Campbell, H. D. Evolution of the gelsolin family of actin-binding proteins as novel transcriptional coactivators. Bioessays 27, 388-396 (2005).
    • (2005) Bioessays , vol.27 , pp. 388-396
    • Archer, S.K.1    Claudianos, C.2    Campbell, H.D.3
  • 40
    • 84880159982 scopus 로고    scopus 로고
    • Stimulation of in vivo nuclear transport dynamics of actin and its co-factors IQGAP1 and Rac1 in response to DNA replication stress
    • Johnson, M. A., Sharma, M., Mok, M. T. & Henderson, B. R. Stimulation of in vivo nuclear transport dynamics of actin and its co-factors IQGAP1 and Rac1 in response to DNA replication stress. Biochim. Biophys. Acta 1833, 2334-2347 (2013).
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 2334-2347
    • Johnson, M.A.1    Sharma, M.2    Mok, M.T.3    Henderson, B.R.4
  • 41
    • 77957678443 scopus 로고    scopus 로고
    • LINC complexes in health and disease
    • Mejat, A. & Misteli, T. LINC complexes in health and disease. Nucleus 1, 40-52 (2010).
    • (2010) Nucleus , vol.1 , pp. 40-52
    • Mejat, A.1    Misteli, T.2
  • 42
    • 77956588049 scopus 로고    scopus 로고
    • Direct actin binding to A- and B-type lamin tails and actin filament bundling by the lamin A tail
    • Simon, D. N., Zastrow, M. S. & Wilson, K. L. Direct actin binding to A- and B-type lamin tails and actin filament bundling by the lamin A tail. Nucleus 1, 264-272 (2010).
    • (2010) Nucleus , vol.1 , pp. 264-272
    • Simon, D.N.1    Zastrow, M.S.2    Wilson, K.L.3
  • 43
    • 19344378383 scopus 로고    scopus 로고
    • Emerin caps the pointed end of actin filaments: Evidence for an actin cortical network at the nuclear inner membrane
    • Holaska, J. M., Kowalski, A. K. & Wilson, K. L. Emerin caps the pointed end of actin filaments: evidence for an actin cortical network at the nuclear inner membrane. PLoS Biol. 2, E231 (2004).
    • (2004) PLoS Biol. , vol.2
    • Holaska, J.M.1    Kowalski, A.K.2    Wilson, K.L.3
  • 44
    • 84878116428 scopus 로고    scopus 로고
    • Lamin A/C and emerin regulate MKL1-SRF activity by modulating actin dynamics
    • Ho, C. Y., Jaalouk, D. E., Vartiainen, M. K. & Lammerding, J. Lamin A/C and emerin regulate MKL1-SRF activity by modulating actin dynamics. Nature 497, 507-511 (2013).
    • (2013) Nature , vol.497 , pp. 507-511
    • Ho, C.Y.1    Jaalouk, D.E.2    Vartiainen, M.K.3    Lammerding, J.4
  • 45
    • 37849015440 scopus 로고    scopus 로고
    • RPEL motifs link the serum response factor cofactor MAL but not myocardin to Rho signaling via actin binding
    • Guettler, S., Vartiainen, M. K., Miralles, F., Larijani, B. & Treisman, R. RPEL motifs link the serum response factor cofactor MAL but not myocardin to Rho signaling via actin binding. Mol. Cell. Biol. 28, 732-742 (2008).
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 732-742
    • Guettler, S.1    Vartiainen, M.K.2    Miralles, F.3    Larijani, B.4    Treisman, R.5
  • 46
    • 46249118002 scopus 로고    scopus 로고
    • Lifeact: A versatile marker to visualize F-actin
    • Riedl, J. et al. Lifeact: a versatile marker to visualize F-actin. Nature Methods 5, 605-607 (2008).
    • (2008) Nature Methods , vol.5 , pp. 605-607
    • Riedl, J.1


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