메뉴 건너뛰기




Volumn 272, Issue C, 2008, Pages 107-147

Chapter 3 Transcriptional Control of Gene Expression by Actin and Myosin

Author keywords

Chromatin regulation; Gene expression; Molecular motors; Nuclear actin; Nuclear myosin; Nuclear structure; rRNA biogenesis; Transcription

Indexed keywords

ACTIN; DNA DIRECTED RNA POLYMERASE; MYOSIN; MYOSIN ADENOSINE TRIPHOSPHATASE; RIBONUCLEOPROTEIN; RIBOSOME RNA; RNA POLYMERASE II; MESSENGER RNA; MOLECULAR MOTOR;

EID: 58049173935     PISSN: 19376448     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1937-6448(08)01603-1     Document Type: Review
Times cited : (42)

References (116)
  • 2
    • 0023025373 scopus 로고
    • A myosin heavy chain-like polypeptide is associated with the nuclear envelope in higher eukaryotic cells
    • Berrios M., and Fisher P.A. A myosin heavy chain-like polypeptide is associated with the nuclear envelope in higher eukaryotic cells. J. Cell Biol. 103 (1986) 711-724
    • (1986) J. Cell Biol. , vol.103 , pp. 711-724
    • Berrios, M.1    Fisher, P.A.2
  • 3
    • 0025961833 scopus 로고
    • Localization of a myosin heavy chain-like polypeptide to Drosophila nuclear pore complex
    • Berrios M., Fisher P.A., and Matz E.C. Localization of a myosin heavy chain-like polypeptide to Drosophila nuclear pore complex. Proc. Natl. Acad. Sci. USA 88 (1991) 219-223
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 219-223
    • Berrios, M.1    Fisher, P.A.2    Matz, E.C.3
  • 4
    • 0033602146 scopus 로고    scopus 로고
    • Self-regulated polymerization of the actin-related protein Arp1
    • Bingham J.B., and Schroer T.A. Self-regulated polymerization of the actin-related protein Arp1. Curr. Biol. 9 (1999) 223-226
    • (1999) Curr. Biol. , vol.9 , pp. 223-226
    • Bingham, J.B.1    Schroer, T.A.2
  • 5
    • 33748415010 scopus 로고    scopus 로고
    • A mechanism for coordinating chromatin modification and preinitiation complex assembly
    • Black J.C., Choi J.E., Lombardo S.R., and Carey M. A mechanism for coordinating chromatin modification and preinitiation complex assembly. Mol. Cell 23 (2006) 809-818
    • (2006) Mol. Cell , vol.23 , pp. 809-818
    • Black, J.C.1    Choi, J.E.2    Lombardo, S.R.3    Carey, M.4
  • 7
    • 15744397041 scopus 로고    scopus 로고
    • Chromatin remodeling complexes: Strength in diversity, precision through specialization
    • Cairns B.R. Chromatin remodeling complexes: Strength in diversity, precision through specialization. Curr. Opin. Genet. Dev. 15 (2005) 185-190
    • (2005) Curr. Opin. Genet. Dev. , vol.15 , pp. 185-190
    • Cairns, B.R.1
  • 8
    • 0032214123 scopus 로고    scopus 로고
    • Two actin-related proteins are shared functional components of the chromatin-remodeling complexes RSC and SWI/SNF
    • Cairns B.R., Erdjument-Bromage H., Tempst P., Winston F., and Kornberg R.D. Two actin-related proteins are shared functional components of the chromatin-remodeling complexes RSC and SWI/SNF. Mol. Cell 2 (1998) 639-651
    • (1998) Mol. Cell , vol.2 , pp. 639-651
    • Cairns, B.R.1    Erdjument-Bromage, H.2    Tempst, P.3    Winston, F.4    Kornberg, R.D.5
  • 9
    • 33845529654 scopus 로고    scopus 로고
    • Myosin16b: The COOH-tail region directs localization to the nucleus and overexpression delays S-phase progression
    • Cameron R.S., Liu C., Mixon A.S., Pihkala J.P., Rahn R.J., and Cameron P.L. Myosin16b: The COOH-tail region directs localization to the nucleus and overexpression delays S-phase progression. Cell Motil. Cytoskeleton 64 (2007) 19-48
    • (2007) Cell Motil. Cytoskeleton , vol.64 , pp. 19-48
    • Cameron, R.S.1    Liu, C.2    Mixon, A.S.3    Pihkala, J.P.4    Rahn, R.J.5    Cameron, P.L.6
  • 10
    • 33745197326 scopus 로고    scopus 로고
    • The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear proteins in transcription
    • Cavellan E., Asp P., Percipalle P., and Östlund Farrants A.K. The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear proteins in transcription. J. Biol. Chem. 281 (2006) 16264-16271
    • (2006) J. Biol. Chem. , vol.281 , pp. 16264-16271
    • Cavellan, E.1    Asp, P.2    Percipalle, P.3    Östlund Farrants, A.K.4
  • 12
    • 33845583159 scopus 로고    scopus 로고
    • Small ribosomal subunits associate with nuclear myosin and actin in transit to the nuclear pores
    • Cisterna B., Necchi D., Prosperi E., and Biggiogera M. Small ribosomal subunits associate with nuclear myosin and actin in transit to the nuclear pores. FASEB J. 20 (2006) 1901-1903
    • (2006) FASEB J. , vol.20 , pp. 1901-1903
    • Cisterna, B.1    Necchi, D.2    Prosperi, E.3    Biggiogera, M.4
  • 13
    • 0017716157 scopus 로고
    • Diffusible and bound actin nuclei of Xenopus laevis oocytes
    • Clark T.G., and Merriam R.W. Diffusible and bound actin nuclei of Xenopus laevis oocytes. Cell 12 (1977) 883-891
    • (1977) Cell , vol.12 , pp. 883-891
    • Clark, T.G.1    Merriam, R.W.2
  • 14
    • 1242296369 scopus 로고    scopus 로고
    • Mechanisms of RNA polymerase I transcription
    • Comai L. Mechanisms of RNA polymerase I transcription. Adv. Protein Chem. 67 (2004) 123-155
    • (2004) Adv. Protein Chem. , vol.67 , pp. 123-155
    • Comai, L.1
  • 15
    • 0017198257 scopus 로고
    • Fine structure of the heterochromatin of the kangaroo rat dipidomys ordii, and examination of the possible role of actin and myosin in heterochromatin condensation
    • Comings D.E., and Okada T.A. Fine structure of the heterochromatin of the kangaroo rat dipidomys ordii, and examination of the possible role of actin and myosin in heterochromatin condensation. J. Cell Sci. 21 (1976) 465-477
    • (1976) J. Cell Sci. , vol.21 , pp. 465-477
    • Comings, D.E.1    Okada, T.A.2
  • 16
    • 1542358189 scopus 로고    scopus 로고
    • Multiple roles for ISWI in transcription, chromosome organization and DNA replication
    • Corona D.F., and Tamkun J.W. Multiple roles for ISWI in transcription, chromosome organization and DNA replication. Biochim. Biophys. Acta. 1677 (2004) 113-119
    • (2004) Biochim. Biophys. Acta. , vol.1677 , pp. 113-119
    • Corona, D.F.1    Tamkun, J.W.2
  • 17
    • 0035316574 scopus 로고    scopus 로고
    • Chromosome territories, nuclear architecture and gene regulation in mammalian cells
    • Cremer T., and Cremer C. Chromosome territories, nuclear architecture and gene regulation in mammalian cells. Nat. Rev. Gen. 2 (2001) 292-301
    • (2001) Nat. Rev. Gen. , vol.2 , pp. 292-301
    • Cremer, T.1    Cremer, C.2
  • 18
    • 0030984264 scopus 로고    scopus 로고
    • A look at messenger RNP moving through the nuclear pore
    • Daneholt B. A look at messenger RNP moving through the nuclear pore. Cell 88 (1997) 585-588
    • (1997) Cell , vol.88 , pp. 585-588
    • Daneholt, B.1
  • 19
    • 0035912782 scopus 로고    scopus 로고
    • Assembly and transport of a premessenger RNP particle
    • Daneholt D. Assembly and transport of a premessenger RNP particle. Proc. Natl. Acad. Sci. USA 98 (2001) 7012-7017
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7012-7017
    • Daneholt, D.1
  • 22
    • 0343220267 scopus 로고
    • Major non-histone proteins of rat liver chromatin: Preliminary identification of myosin, actin, tubulin and tropomyosin
    • Douvas A.S., harrington C.A., and Bonner J. Major non-histone proteins of rat liver chromatin: Preliminary identification of myosin, actin, tubulin and tropomyosin. Proc. Natl. Acad. Sci. USA 72 (1975) 3902-3906
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 3902-3906
    • Douvas, A.S.1    harrington, C.A.2    Bonner, J.3
  • 24
    • 0021513584 scopus 로고
    • Is actin a transcription initiation factor for RNA polymerase B?
    • Egly J.M., Miyamoto N.G., Moncollin V., and Chambon P. Is actin a transcription initiation factor for RNA polymerase B?. EMBO J. 3 (1984) 2363-2371
    • (1984) EMBO J. , vol.3 , pp. 2363-2371
    • Egly, J.M.1    Miyamoto, N.G.2    Moncollin, V.3    Chambon, P.4
  • 25
    • 1242316973 scopus 로고    scopus 로고
    • An actin-myosin complex on actively transcribing genes
    • Fomproix N., and Percipalle P. An actin-myosin complex on actively transcribing genes. Exp. Cell Res. 294 (2004) 140-148
    • (2004) Exp. Cell Res. , vol.294 , pp. 140-148
    • Fomproix, N.1    Percipalle, P.2
  • 26
    • 34249307315 scopus 로고    scopus 로고
    • Nuclear organization of the genome and the potential for gene regulation
    • Fraser P., and Bickmore W. Nuclear organization of the genome and the potential for gene regulation. Nature 447 (2007) 413-417
    • (2007) Nature , vol.447 , pp. 413-417
    • Fraser, P.1    Bickmore, W.2
  • 29
    • 10444232746 scopus 로고    scopus 로고
    • Chromatin organization in the mammalian nucleus
    • Gilbert N., Gilchrist S., and Bickmore W.A. Chromatin organization in the mammalian nucleus. Int. Rev. Cytol. 242 (2005) 283-336
    • (2005) Int. Rev. Cytol. , vol.242 , pp. 283-336
    • Gilbert, N.1    Gilchrist, S.2    Bickmore, W.A.3
  • 31
    • 0019423975 scopus 로고
    • Involvement of contractile proteins in the changes in consistency of oocyte nucleoplasm of the newt Pleurodeles waltlii
    • Gounon P., and Karsenti E. Involvement of contractile proteins in the changes in consistency of oocyte nucleoplasm of the newt Pleurodeles waltlii. J. Cell Biol. 88 (1981) 410-421
    • (1981) J. Cell Biol. , vol.88 , pp. 410-421
    • Gounon, P.1    Karsenti, E.2
  • 32
    • 0038506040 scopus 로고    scopus 로고
    • Life on a planet of its own: Regulation of RNA polymerase I transcription in the nucleolus
    • Grummt I. Life on a planet of its own: Regulation of RNA polymerase I transcription in the nucleolus. Genes Dev. 17 (2003) 1691-1702
    • (2003) Genes Dev. , vol.17 , pp. 1691-1702
    • Grummt, I.1
  • 33
    • 33644852058 scopus 로고    scopus 로고
    • Actin and myosin as transcription factors
    • Grummt I. Actin and myosin as transcription factors. Curr. Opin. Genet Dev. 16 (2006) 191-196
    • (2006) Curr. Opin. Genet Dev. , vol.16 , pp. 191-196
    • Grummt, I.1
  • 34
    • 0030882497 scopus 로고    scopus 로고
    • Interaction of AU-rich sequence binding proteins with actin: Possible involvement of the actin cytoskeleton in lymphokine mRNA turnover
    • Henics T., Nagy E., and Szekeres-Bartho J. Interaction of AU-rich sequence binding proteins with actin: Possible involvement of the actin cytoskeleton in lymphokine mRNA turnover. J. Cell. Physiol. 173 (1997) 19-27
    • (1997) J. Cell. Physiol. , vol.173 , pp. 19-27
    • Henics, T.1    Nagy, E.2    Szekeres-Bartho, J.3
  • 35
    • 0033766762 scopus 로고    scopus 로고
    • A myosin family tree
    • Hodge T., and Cope M.J. A myosin family tree. J. Cell Sci. 113 (2000) 3353-3354
    • (2000) J. Cell Sci. , vol.113 , pp. 3353-3354
    • Hodge, T.1    Cope, M.J.2
  • 38
    • 33750542350 scopus 로고    scopus 로고
    • Nuclear myosin I is necessary for the formation of the first phosphodiester bond during transcription initiation by RNA polymerase II
    • Hofmann W.A., Vargas G.M., Ramchandran R., Stojiljkovic L., Goodrich J.A., and de Lanerolle P. Nuclear myosin I is necessary for the formation of the first phosphodiester bond during transcription initiation by RNA polymerase II. J. Cell Biochem. 99 (2006) 1001-1009
    • (2006) J. Cell Biochem. , vol.99 , pp. 1001-1009
    • Hofmann, W.A.1    Vargas, G.M.2    Ramchandran, R.3    Stojiljkovic, L.4    Goodrich, J.A.5    de Lanerolle, P.6
  • 39
    • 34547642520 scopus 로고    scopus 로고
    • An emerin "proteome": Purification of distinct emerin-containing complexes from HeLa cells suggests molecular basis for diverse roles including gene regulation, mRNA splicing, signaling, mechanosensing, and nuclear architecture
    • Holaska J.M., and Wilson K.L. An emerin "proteome": Purification of distinct emerin-containing complexes from HeLa cells suggests molecular basis for diverse roles including gene regulation, mRNA splicing, signaling, mechanosensing, and nuclear architecture. Biochemistry 46 (2007) 8897-8908
    • (2007) Biochemistry , vol.46 , pp. 8897-8908
    • Holaska, J.M.1    Wilson, K.L.2
  • 40
    • 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., and 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 (2004) E231
    • (2004) PLoS Biol. , vol.2
    • Holaska, J.M.1    Kowalski, A.K.2    Wilson, K.L.3
  • 41
    • 10644294832 scopus 로고    scopus 로고
    • A role for beta-actin in RNA polymerase III transcription
    • Hu P., Wu S., and Hernandez N. A role for beta-actin in RNA polymerase III transcription. Genes Dev. 18 (2004) 3010-3015
    • (2004) Genes Dev. , vol.18 , pp. 3010-3015
    • Hu, P.1    Wu, S.2    Hernandez, N.3
  • 44
    • 33846415874 scopus 로고    scopus 로고
    • Nuclear myosin is ubiquitously expressed and evolutionary conserved in vertebrates
    • Kahle M., Pridalova J., Spacek M., Dzijak R., and Hozak P. Nuclear myosin is ubiquitously expressed and evolutionary conserved in vertebrates. Histochem. Cell Biol. 127 (2007) 139-148
    • (2007) Histochem. Cell Biol. , vol.127 , pp. 139-148
    • Kahle, M.1    Pridalova, J.2    Spacek, M.3    Dzijak, R.4    Hozak, P.5
  • 45
    • 2342497805 scopus 로고    scopus 로고
    • Intranuclear pre-mRNA trafficking in an insect model system
    • Kiesler E., and Visa N. Intranuclear pre-mRNA trafficking in an insect model system. Prog. Mol. Subcell. Biol. 35 (2004) 99-118
    • (2004) Prog. Mol. Subcell. Biol. , vol.35 , pp. 99-118
    • Kiesler, E.1    Visa, N.2
  • 46
    • 3042777656 scopus 로고    scopus 로고
    • Actin- and protein-4.1-containing filaments link nuclear pore complexes to subnuclear organelles in Xenopus oocyte nuclei
    • Kiseleva E., Drummond S.P., Goldberg M.W., Rutherford S.A., Allen T.D., and Wilson K.L. Actin- and protein-4.1-containing filaments link nuclear pore complexes to subnuclear organelles in Xenopus oocyte nuclei. J. Cell Sci. 117 (2004) 2481-2490
    • (2004) J. Cell Sci. , vol.117 , 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
  • 48
    • 34548801789 scopus 로고    scopus 로고
    • The molecular basis of eukaryotic transcription
    • Kornberg R.G. The molecular basis of eukaryotic transcription. Proc. Natl. Acad. Sci. USA 104 (2007) 12955-12961
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 12955-12961
    • Kornberg, R.G.1
  • 51
    • 0343683356 scopus 로고    scopus 로고
    • RNA polymerase I transcription on nucleosomal templates: TTF-I induces chromatin remodeling and relieves transcriptional repression
    • Längst G., Blank T.A., Becker P.B., and Grummt I. RNA polymerase I transcription on nucleosomal templates: TTF-I induces chromatin remodeling and relieves transcriptional repression. EMBO J. 16 (1997) 760-768
    • (1997) EMBO J. , vol.16 , pp. 760-768
    • Längst, G.1    Blank, T.A.2    Becker, P.B.3    Grummt, I.4
  • 52
    • 33947532026 scopus 로고    scopus 로고
    • Histone acetyl transferase complexes: One size doesn't fit all
    • Lee K.K., and Workman J.L. Histone acetyl transferase complexes: One size doesn't fit all. Nat. Rev. Mol. Cell Biol. 8 (2007) 284-295
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 284-295
    • Lee, K.K.1    Workman, J.L.2
  • 54
    • 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. Nucleoplasmic beta-actin exists in a dynamic equilibrium between low-mobility polymeric species and rapidly diffusing populations. J. Cell Biol. 172 (2006) 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
  • 56
    • 33646926758 scopus 로고    scopus 로고
    • Dynamic nucleosomes and gene transcription
    • Mellor J. Dynamic nucleosomes and gene transcription. TRENDS Genet. 22 (2006) 320-329
    • (2006) TRENDS Genet. , vol.22 , pp. 320-329
    • Mellor, J.1
  • 57
    • 0037314175 scopus 로고    scopus 로고
    • Sequential recruitment of HAT and SWI/SNF components to condensed chromatin by VP16
    • Memedula S., and Belmont A.S. Sequential recruitment of HAT and SWI/SNF components to condensed chromatin by VP16. Curr. Biol. 13 (2003) 241-246
    • (2003) Curr. Biol. , vol.13 , pp. 241-246
    • Memedula, S.1    Belmont, A.S.2
  • 58
    • 0142026447 scopus 로고    scopus 로고
    • Regulation of actin dynamics by WASP family proteins
    • Miki H., and Takenawa T. Regulation of actin dynamics by WASP family proteins. J. Biochem. 134 (2003) 309-313
    • (2003) J. Biochem. , vol.134 , pp. 309-313
    • Miki, H.1    Takenawa, T.2
  • 59
    • 0035298137 scopus 로고    scopus 로고
    • Molecular characterization of Ct-hrp65: Identification of two novel isoforms originated by alternative splicing
    • Miralles F., and Visa N. Molecular characterization of Ct-hrp65: Identification of two novel isoforms originated by alternative splicing. Exp. Cell Res. 264 (2001) 284-295
    • (2001) Exp. Cell Res. , vol.264 , pp. 284-295
    • Miralles, F.1    Visa, N.2
  • 60
    • 33646495978 scopus 로고    scopus 로고
    • Actin in transcription and transcription regulation
    • Miralles F., and Visa N. Actin in transcription and transcription regulation. Curr. Opin. Cell Biol. 18 (2006) 261-266
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 261-266
    • Miralles, F.1    Visa, N.2
  • 63
    • 53549100755 scopus 로고    scopus 로고
    • The histone acetyltransferase PCAF associates with actin and hnRNP U for RNA polymerase II transcription
    • Obrdlik A., Kukalev A., Louvet E., Östlund Farrants A.-K., Caputo L., and Percipalle P. The histone acetyltransferase PCAF associates with actin and hnRNP U for RNA polymerase II transcription. Mol. Cell. Biol. 28 (2008) 6342-6357
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 6342-6357
    • Obrdlik, A.1    Kukalev, A.2    Louvet, E.3    Östlund Farrants, A.-K.4    Caputo, L.5    Percipalle, P.6
  • 64
    • 34247606028 scopus 로고    scopus 로고
    • Myosin at work: Motor adaptation for a variety of cellular functions
    • O'Connell C.B., Tyska M.J., and Mooseker M.S. Myosin at work: Motor adaptation for a variety of cellular functions. Biochem. Biophys. Acta 1773 (2007) 615-630
    • (2007) Biochem. Biophys. Acta , vol.1773 , pp. 615-630
    • O'Connell, C.B.1    Tyska, M.J.2    Mooseker, M.S.3
  • 65
    • 0035997387 scopus 로고    scopus 로고
    • Nuclear actin and actin-related proteins in chromatin remodeling
    • Olave I.A., Reck-Peterson S.L., and Crabtree G.R. Nuclear actin and actin-related proteins in chromatin remodeling. Annu. Rev. Biochem. 71 (2002) 755-781
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 755-781
    • Olave, I.A.1    Reck-Peterson, S.L.2    Crabtree, G.R.3
  • 66
    • 44449139885 scopus 로고    scopus 로고
    • Chromatin remodelling and actin organization
    • Öslund Farrants A.-K. Chromatin remodelling and actin organization. FEBS Lett. 582 (2008) 2041-2050
    • (2008) FEBS Lett. , vol.582 , pp. 2041-2050
    • Öslund Farrants, A.-K.1
  • 67
  • 68
    • 0031736990 scopus 로고    scopus 로고
    • The Drosophila trithorax group proteins BRM, ASH1, and ASH2 are subunits of distinct protein complexes
    • Papoulas O., Beek S.J., Moseley S.L., McCallum C.M., Sarte M., Shearn A., and Tamkun J.W. The Drosophila trithorax group proteins BRM, ASH1, and ASH2 are subunits of distinct protein complexes. Development 125 (1998) 3955-3966
    • (1998) Development , vol.125 , pp. 3955-3966
    • Papoulas, O.1    Beek, S.J.2    Moseley, S.L.3    McCallum, C.M.4    Sarte, M.5    Shearn, A.6    Tamkun, J.W.7
  • 69
    • 41549114618 scopus 로고    scopus 로고
    • As functional actin comes into view, is it globular, filamentous, or both?
    • Pederson T. As functional actin comes into view, is it globular, filamentous, or both?. J. Cell. Biol. 180 (2008) 1061-1064
    • (2008) J. Cell. Biol. , vol.180 , pp. 1061-1064
    • Pederson, T.1
  • 70
    • 0036971460 scopus 로고    scopus 로고
    • Actin in the nucleus: What form and what for?
    • Pederson T., and Aebi U. Actin in the nucleus: What form and what for?. J. Struct. Biol. 140 (2002) 3-9
    • (2002) J. Struct. Biol. , vol.140 , pp. 3-9
    • Pederson, T.1    Aebi, U.2
  • 71
    • 27644506209 scopus 로고    scopus 로고
    • Nuclear actin extends, with no contraction in sight
    • Pederson T., and Aebi U. Nuclear actin extends, with no contraction in sight. Mol. Biol. Cell. 16 (2005) 5055-5060
    • (2005) Mol. Biol. Cell. , vol.16 , pp. 5055-5060
    • Pederson, T.1    Aebi, U.2
  • 72
    • 34248588469 scopus 로고    scopus 로고
    • Genetic connections of the actin cytoskeleton and beyond
    • Percipalle P. Genetic connections of the actin cytoskeleton and beyond. BioEssays 29 (2007) 407-411
    • (2007) BioEssays , vol.29 , pp. 407-411
    • Percipalle, P.1
  • 73
    • 33746279691 scopus 로고    scopus 로고
    • Chromatin remodeling and transcription: be-WICHed by nuclear myosin 1
    • Percipalle P., and Östlund Farrants A.K. Chromatin remodeling and transcription: be-WICHed by nuclear myosin 1. Curr. Opin. Cell Biol. 18 (2006) 267-274
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 267-274
    • Percipalle, P.1    Östlund Farrants, A.K.2
  • 74
    • 33645285000 scopus 로고    scopus 로고
    • Molecular functions of nuclear actin in transcription
    • Percipalle P., and Visa N. Molecular functions of nuclear actin in transcription. J. Cell Biol. 172 (2006) 967-971
    • (2006) J. Cell Biol. , vol.172 , pp. 967-971
    • Percipalle, P.1    Visa, N.2
  • 75
    • 0035795419 scopus 로고    scopus 로고
    • Actin bound to the heterogeneous nuclear ribonucleoprotein hrp36 is associated with Balbiani ring mRNA from the gene to polysomes
    • Percipalle P., Zhao J., Pope B., Weeds A., Lindberg U., and Daneholt B. Actin bound to the heterogeneous nuclear ribonucleoprotein hrp36 is associated with Balbiani ring mRNA from the gene to polysomes. J. Cell Biol. 153 (2001) 229-236
    • (2001) J. Cell Biol. , vol.153 , pp. 229-236
    • Percipalle, P.1    Zhao, J.2    Pope, B.3    Weeds, A.4    Lindberg, U.5    Daneholt, B.6
  • 81
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard T.D., and Borisy G.G. Cellular motility driven by assembly and disassembly of actin filaments. Cell 113 (2003) 453-465
    • (2003) Cell , vol.113 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 82
  • 83
    • 33750343214 scopus 로고    scopus 로고
    • Actin' together: Serum response factor, its cofactors and the link to signal transduction
    • Posern G., and Treisman R. Actin' together: Serum response factor, its cofactors and the link to signal transduction. TRENDS Cell Biol. 16 (2006) 588-596
    • (2006) TRENDS Cell Biol. , vol.16 , pp. 588-596
    • Posern, G.1    Treisman, R.2
  • 85
    • 51349125658 scopus 로고    scopus 로고
    • In cultured oligodendrocytes the A/B-type hnRNP CBF-A accompanies MBP mRNA bound to mRNA trafficking sequences
    • May 14, [Epub ahead of print], PMID 18480411**
    • Raju C.S., Göritz C., Nord Y., Hermanson O., Loper-Iglesias C., Castelo-Branco G., and Percipalle P. In cultured oligodendrocytes the A/B-type hnRNP CBF-A accompanies MBP mRNA bound to mRNA trafficking sequences. Mol. Biol. Cell (2008) May 14, [Epub ahead of print], PMID 18480411**
    • (2008) Mol. Biol. Cell
    • Raju, C.S.1    Göritz, C.2    Nord, Y.3    Hermanson, O.4    Loper-Iglesias, C.5    Castelo-Branco, G.6    Percipalle, P.7
  • 86
    • 0037022632 scopus 로고    scopus 로고
    • Phosphatidylinositol-dependent actin filament binding by the SWI/SNF-like BAF chromatin remodeling complex
    • Rando O.J., Zhao K., Janmey P., and Crabtree G.R. Phosphatidylinositol-dependent actin filament binding by the SWI/SNF-like BAF chromatin remodeling complex. Proc. Natl. Acad. Sci. USA 99 (2002) 2824-2829
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 2824-2829
    • Rando, O.J.1    Zhao, K.2    Janmey, P.3    Crabtree, G.R.4
  • 87
    • 0034695924 scopus 로고    scopus 로고
    • The yeast nuclear pore complex: Composition, architecture, and transport mechanisms
    • Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y., and Chait B.T. The yeast nuclear pore complex: Composition, architecture, and transport mechanisms. J. Cell Biol. 148 (2000) 635-651
    • (2000) J. Cell Biol. , vol.148 , pp. 635-651
    • Rout, M.P.1    Aitchison, J.D.2    Suprapto, A.3    Hjertaas, K.4    Zhao, Y.5    Chait, B.T.6
  • 88
    • 0018595534 scopus 로고
    • Intranuclear injection of anti-actin antibodies into Xenopus oocytes blocks chromosome condensation
    • Rungger D. Intranuclear injection of anti-actin antibodies into Xenopus oocytes blocks chromosome condensation. Nature 282 (1979) 320-321
    • (1979) Nature , vol.282 , pp. 320-321
    • Rungger, D.1
  • 89
    • 0032700750 scopus 로고    scopus 로고
    • Interaction of the universal mRNA-binding protein, p50, with actin: A possible link between mRNA and microfilaments
    • Ruzanov P.V., Evdokimova V.M., Korneeva N.L., Hershey J.W.B., and Ovchinnikov L.P. Interaction of the universal mRNA-binding protein, p50, with actin: A possible link between mRNA and microfilaments. J. Cell Sci. 112 (1999) 3487-3496
    • (1999) J. Cell Sci. , vol.112 , pp. 3487-3496
    • Ruzanov, P.V.1    Evdokimova, V.M.2    Korneeva, N.L.3    Hershey, J.W.B.4    Ovchinnikov, L.P.5
  • 90
    • 0016722297 scopus 로고
    • Presence of actin during chromosomal movement
    • Sanger J.W. Presence of actin during chromosomal movement. Proc. Natl. Acad. Sci. USA 72 (1975) 2451-2455
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 2451-2455
    • Sanger, J.W.1
  • 91
    • 0028304474 scopus 로고
    • Ultrastructural analysis of the dynactin complex: An actin-related protein is a component of a filament that resembles F-actin
    • Schafer D.A., Gill S.R., Cooper J.A., Heuser J.E., and Schroer T.A. Ultrastructural analysis of the dynactin complex: An actin-related protein is a component of a filament that resembles F-actin. J. Cell Biol. 126 (1994) 403-412
    • (1994) J. Cell Biol. , vol.126 , pp. 403-412
    • Schafer, D.A.1    Gill, S.R.2    Cooper, J.A.3    Heuser, J.E.4    Schroer, T.A.5
  • 92
    • 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. Microinjection of actin-binding proteins and actin antibodies demonstrates involvement of nuclear actin in transcription of lampbrush chromosomes. Cell 39 (1984) 111-122
    • (1984) Cell , vol.39 , pp. 111-122
    • Scheer, U.1    Hinssen, H.2    Franke, W.W.3    Jockusch, B.M.4
  • 93
    • 0022495720 scopus 로고
    • Nuclear actin and myosin as control elements in nucleocytoplasmic transport
    • Schindler M., and Jiang L.W. Nuclear actin and myosin as control elements in nucleocytoplasmic transport. J. Cell Biol. 102 (1986) 859-862
    • (1986) J. Cell Biol. , vol.102 , pp. 859-862
    • Schindler, M.1    Jiang, L.W.2
  • 95
    • 35148882905 scopus 로고    scopus 로고
    • The SWI/SNF complex is important for histone eviction during transcriptional activation and RNA polymerase II elongation in vivo
    • Schwabish M.A., and Struhl K. The SWI/SNF complex is important for histone eviction during transcriptional activation and RNA polymerase II elongation in vivo. Mol. Cell. Biol. 27 (2007) 6987-6995
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 6987-6995
    • Schwabish, M.A.1    Struhl, K.2
  • 97
    • 0037032415 scopus 로고    scopus 로고
    • PSF and p54(nrb)/NonO-multi-functional nuclear proteins
    • Shav-Tal Y., and Zipori X. PSF and p54(nrb)/NonO-multi-functional nuclear proteins. FEBS Lett. 531 (2002) 109-114
    • (2002) FEBS Lett. , vol.531 , pp. 109-114
    • Shav-Tal, Y.1    Zipori, X.2
  • 98
    • 0034601464 scopus 로고    scopus 로고
    • A chromatin remodeling complex involved in transcription and DNA processing
    • Shen X., Mizuguchi G., Hamiche A., and Wu C. A chromatin remodeling complex involved in transcription and DNA processing. Nature 406 (2000) 541-544
    • (2000) Nature , vol.406 , pp. 541-544
    • Shen, X.1    Mizuguchi, G.2    Hamiche, A.3    Wu, C.4
  • 99
    • 6344286164 scopus 로고    scopus 로고
    • ATP-dependnet nucleosome remodeling complexes: Enzymes tailored to deal with chromatin
    • Sif S. ATP-dependnet nucleosome remodeling complexes: Enzymes tailored to deal with chromatin. J. Cell. Biochem. 91 (2004) 1087-1098
    • (2004) J. Cell. Biochem. , vol.91 , pp. 1087-1098
    • Sif, S.1
  • 101
    • 23944495664 scopus 로고    scopus 로고
    • The growing pre-mRNA recruits actin and chromatin-modifying factors to transcriptionally active genes
    • Sjölinder M., Björk P., Soderberg E., Sabri N., Östlund Farrants A.K., and Visa N. The growing pre-mRNA recruits actin and chromatin-modifying factors to transcriptionally active genes. Genes Dev. 19 (2005) 1871-1884
    • (2005) Genes Dev. , vol.19 , pp. 1871-1884
    • Sjölinder, M.1    Björk, P.2    Soderberg, E.3    Sabri, N.4    Östlund Farrants, A.K.5    Visa, N.6
  • 102
    • 0030868980 scopus 로고    scopus 로고
    • Efficient mammalian protein synthesis requires an intact F-actin system
    • Stapulionis R., Kolli S., and Deutscher M.P. Efficient mammalian protein synthesis requires an intact F-actin system. J. Biol. Chem. 272 (1997) 24980-24986
    • (1997) J. Biol. Chem. , vol.272 , pp. 24980-24986
    • Stapulionis, R.1    Kolli, S.2    Deutscher, M.P.3
  • 103
    • 0034795562 scopus 로고    scopus 로고
    • Cytoskeleton-dependent transport and localization of mRNA
    • Stebbings H. Cytoskeleton-dependent transport and localization of mRNA. Int. Rev. Cyt. 211 (2001) 1-31
    • (2001) Int. Rev. Cyt. , vol.211 , pp. 1-31
    • Stebbings, H.1
  • 106
    • 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., and Treisman R. Nuclear actin regulates dynamic subcellular localization and activity of the SRF cofactor MAL. Science 316 (2007) 1749-1752
    • (2007) Science , vol.316 , pp. 1749-1752
    • Vartiainen, M.K.1    Guettler, S.2    Larijani, B.3    Treisman, R.4
  • 107
    • 33745738998 scopus 로고    scopus 로고
    • Actin's latest act: Polymerizing to facilitate transcription?
    • Vieu E., and Hernandez N. Actin's latest act: Polymerizing to facilitate transcription?. Nat. Cell Biol. 8 (2006) 650-651
    • (2006) Nat. Cell Biol. , vol.8 , pp. 650-651
    • Vieu, E.1    Hernandez, N.2
  • 108
    • 16844373309 scopus 로고    scopus 로고
    • Actin in transcription
    • Visa N. Actin in transcription. EMBO Rep. 6 (2005) 218-219
    • (2005) EMBO Rep. , vol.6 , pp. 218-219
    • Visa, N.1
  • 109
    • 0030034421 scopus 로고    scopus 로고
    • A pre-mRNA-binding protein accompanies the RNA from the gene through the nuclear pores and into polysomes
    • Visa N., Alzhanova-Ericsson A.T., Sun X., Kiseleva E., Björkroth B., Wurtz T., and Daneholt B. A pre-mRNA-binding protein accompanies the RNA from the gene through the nuclear pores and into polysomes. Cell 84 (1996) 253-264
    • (1996) Cell , vol.84 , pp. 253-264
    • Visa, N.1    Alzhanova-Ericsson, A.T.2    Sun, X.3    Kiseleva, E.4    Björkroth, B.5    Wurtz, T.6    Daneholt, B.7
  • 111
    • 33750325090 scopus 로고    scopus 로고
    • Actin-based modeling of a transcriptionally competent nuclear substructure induced by transcription inhibition
    • Wang I.F., Chang H.Y., and Shen C.K.J. Actin-based modeling of a transcriptionally competent nuclear substructure induced by transcription inhibition. Exp. Cell Res. 312 (2006) 3796-3807
    • (2006) Exp. Cell Res. , vol.312 , pp. 3796-3807
    • Wang, I.F.1    Chang, H.Y.2    Shen, C.K.J.3
  • 112
    • 11244281646 scopus 로고    scopus 로고
    • RNA polymerases I and III growth control and cancer
    • White R.J. RNA polymerases I and III growth control and cancer. Nat. Rev. Mol. Cell Biol. 6 (2005) 69-78
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 69-78
    • White, R.J.1
  • 113
    • 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. Regulation of RNA-polymerase-II-dependent transcription by N-WASP and its nuclear-binding partners. Nat. Cell Biol. 8 (2006) 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
  • 114
    • 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., and Grummt I. Nuclear myosin I acts in concert with polymeric actin to drive RNA polymerase I transcription. Genes Dev. 22 (2008) 322-330
    • (2008) Genes Dev. , vol.22 , pp. 322-330
    • Ye, J.1    Zhao, J.2    Hoffmann-Rohrer, U.3    Grummt, I.4
  • 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. A novel role of the actin-nucleating Arp2/3 complex in the regulation of RNA polymerase II-dependent transcription. J. Biol. Chem. 282 (2007) 7616-7623
    • (2007) J. Biol. Chem. , vol.282 , pp. 7616-7623
    • Yoo, Y.1    Wu, X.2    Guan, J.L.3
  • 116
    • 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 O.J., Xue Y., Swiderek K., Kuo A., and Crabtree G.R. Rapid and phosphoinositol-dependent binding of the SWI/SNF-like BAF complex to chromatin after T lymphocyte receptor signaling. Cell 95 (1998) 625-636
    • (1998) Cell , vol.95 , pp. 625-636
    • 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.