The F-actin severing protein cofilin-1 is required for RNA polymerase II transcription elongation

References

• Hofmann WA. Cell and molecular biology of nuclear actin. Int Rev Cell Mol Biol 2009; 273:219 - 263
   PubMed Web of Science ®Google Scholar
• Louvet E, Percipalle P. Actin and myosin in gene transcription. Int Rev Cell Mol Biol 2009; 272:107 - 147
   PubMed Web of Science ®Google Scholar
• Hofmann WA, Stojiljkovic L, Fuchsova B, Vargas GM, Mavrommatis E, Philimonenko V, et al. Actin is part of pre-initiation complexes and is necessary for transcription by RNA polymerase II. Nat Cell Biol 2004; 6:1094 - 1101
   PubMed Web of Science ®Google Scholar
• Kukalev A, Nord Y, Palmberg C, Bergman T, Percipalle P. Actin and hnRNP U cooperate for productive transcription by RNA polymerase II. Nat Struct Mol Biol 2005; 12:238 - 244
   PubMed Web of Science ®Google Scholar
• Obrdlik A, Kukalev A, Louvet E, Farrants AK, Caputo L, Percipalle P. The histone acetyltransferase PCAF associates with actin and hnRNP U for RNA polymerase II transcription. Mol Cell Biol 2008; 28:6342 - 6357
   PubMed Web of Science ®Google Scholar
• Percipalle P. The long journey of actin and actin-associated proteins from gene to polysomes. Cell Mol Life Sci 2009; 66:2151 - 2165
   PubMed Web of Science ®Google Scholar
• McDonald D, Carrero G, Andrin C, de Vries G, Hendzel MG. Nucleoplasmic beta-actin exists in a dynamic equilibrium between low-mobility polymeric species and rapidly diffusing populations. J Cell Biol 2006; 172:541 - 552
   PubMed Web of Science ®Google Scholar
• Wu X, Yoo Y, Okuhama NN, Tucker PW, Liu G, Guan JL. Regulation of RNApolymerase-II-dependent transcription by N-WASP and its nuclear-binding partners. Nat Cell Biol 2006; 8:756 - 763
   PubMed Web of Science ®Google Scholar
• Yoo Y, Wu X, Guan JL. A novel role of the actin-nucleating Arp2/3 complex in the regulation of RNA polymerase II-dependent transcription. J Biol Chem 2007; 282:7616 - 7623
   PubMedGoogle Scholar
• Jockusch BM, Schoenenberger CA, Stetefeld J, Aebi U. Tracking down the different forms of nuclear actin. Trends Cell Biol 2006; 16:391 - 396
   PubMed Web of Science ®Google Scholar
• Gieni RS, Hendzel MJ. Actin dynamics and functions in the interphase nucleus: moving toward an understanding of nuclear polymeric actin. Biochem Cell Biol 2009; 87:283 - 306
   PubMed Web of Science ®Google Scholar
• Visa N, Percipalle P. Nuclear functions of actin. Cold Spring Harb Perspect Biol 2010; http://dx.doi.org/10.1101/csh-perspect.a000620
   PubMed Web of Science ®Google Scholar
• Pollard TD, Cooper JA. Actin, a central player in cell shape and movement. Science 2009; 326:1208 - 1212
   PubMed Web of Science ®Google Scholar
• Vartiainen MK, Mustonen T, Mattila PK, Ojala PJ, Thesleff I, Partanen J, et al. The three mouse actin-depolymerizing factor/cofilins evolved to fulfill cell-type-specific requirements for actin dynamics. Mol Biol Cell 2002; 13:183
   PubMed Web of Science ®Google Scholar
• Dedova IV, Nikolaeva OP, Mikhailova VV, dos Remedios CG, Levitsky DI. Two opposite effects of cofilin on the thermal unfolding of F-actin: A differential scanning calorimetric study. Biophys Chem 2004; 110:119 - 128
   PubMed Web of Science ®Google Scholar
• Hotulainen P, Paunola E, Vartiainen MK, Lappalainen P. Actin-depolymerizing factor and cofilin-1 play overlapping roles in promoting rapid F-actin depolymerization in mammalian non-muscle cells. Mol Biol Cell 2005; 16:649 - 664
   PubMed Web of Science ®Google Scholar
• Yap CT, Simpson TI, Pratt T, Price DJ, Maciver SK. The motility of glioblastoma tumour cells is modulated by intracellular cofilin expression in a concentration-dependent manner. Cell Motil Cytoskeleton 2005; 60:153 - 165
   PubMed Web of Science ®Google Scholar
• Andrianantoandro E, Pollard TD. Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin. Mol Cell 2006; 24:13 - 23
   PubMed Web of Science ®Google Scholar
• Bobkov AA, Muhlrad A, Pavlov DA, Kokabi K, Yilmaz A, Reisler E. Cooperative effects of cofilin (ADF) on actin structure suggest allosteric mechanism of cofilin function. J Mol Biol 2006; 356:325 - 334
   PubMed Web of Science ®Google Scholar
• Pavlov D, Muhlrad A, Cooper J, Wear M, Reisler E. Actin filament severing by cofilin. J Mol Biol 2007; 365:1350 - 1358
   PubMed Web of Science ®Google Scholar
• Pendleton A, Pope B, Weeds A, Koffer A. Latrunculin B or ATP depletion induces cofilin-dependent translocation of actin into nuclei of mast cells. J Biol Chem 2003; 278:14394 - 14400
   PubMed Web of Science ®Google Scholar
• Ye J, Zhao J, Hoffmann-Rohrer U, Grummt I. Nuclear myosin 1 acts in concert with polymeric actin to drive RNA polymerase I transcription. Genes & Dev 2008; 22:322 - 330
   PubMed Web of Science ®Google Scholar
• Schoenenberger CA, Buchmeier S, Boerries M, Sütterlin R, Aebi U, Jockusch BM. Conformation-specific antibodies reveal distinct actin structures in the nucleus and the cytoplasm. J Struct Biol 2005; 152:157 - 168
   PubMed Web of Science ®Google Scholar
• Goddette DW, Frieden C. Actin polymerization. The mechanism of action of cytochalasin D. J Biol Chem 1986; 261:15974 - 15980
   PubMed Web of Science ®Google Scholar
• Cooper JA. Effects of cytochalasin and phalloidin on actin. J Cell Biol 1987; 105:1473 - 1478
   PubMed Web of Science ®Google Scholar
• Bubb MR, Spector I, Beyer BB, Fosen KM. Effects of jasplakinolide on the kinetics of actin polymerization. J Biol Chem 2000; 275:5163 - 5170
   PubMed Web of Science ®Google Scholar
• Morton WM, Ayscough KR, McLaughlin PJ. Latrunculin alters the actin-monomer subunit interface to prevent polymerization. Nat Cell Biol 2000; 2:376 - 378
   PubMed Web of Science ®Google Scholar
• Paavilainen VO, Bertling E, Falck S, Lappalainen P. Regulation of cytoskeletal dynamics by actin-monomer-binding proteins. Trends Cell Biol 2004; 14:386 - 394
   PubMed Web of Science ®Google Scholar
• Berger SL. The complex language of chromatin regulation during transcription. Nature 2007; 44:7407 - 7412
   Google Scholar
• Mitchell JA, Fraser P. Transcription factories are nuclear subcompartments that remain in the absence of transcription. Genes Dev 2008; 22:20 - 25
   PubMed Web of Science ®Google Scholar