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Commentary

Formin-mediated epigenetic maintenance of centromere identity

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Pages 245-250 | Received 15 Jun 2016, Accepted 15 Jul 2016, Published online: 09 Aug 2016

References

  • Cleveland DW, Mao Y, Sullivan KF. Centromeres and Kinetochores: From epigenetics to mitotic checkpoint signaling. Cell 2003; 112:407-21; PMID:12600307; https://doi.org/10.1016/S0092-8674(03)00115-6
  • Jansen LET, Black BE, Foltz DR, Cleveland DW. Propagation of centromeric chromatin requires exit from mitosis. J Cell Biol 2007; 176:795-805; PMID:17339380; https://doi.org/10.1083/jcb.200701066
  • Fujita Y, Hayashi T, Kiyomitsu T, Toyoda Y, Kokubu A, Obuse C, et al. Priming of centromere for CENP-A recruitment by human hMis18α, hMis18β, and M18BP1. Dev Cell 2007; 12:17-30; PMID:17199038; https://doi.org/10.1016/j.devcel.2006.11.002
  • Maddox PS, Hyndman F, Monen J, Oegema K, Desai A. Functional genomics identifies a Myb domain–containing protein family required for assembly of CENP-A chromatin. J Cell Biol 2007; 176:757-63; PMID:17339379; https://doi.org/10.1083/jcb.200701065
  • Dunleavy EM, Roche D, Tagami H, Lacoste N, Ray-Gallet D, Nakamura Y, Daigo Y, Nakatani Y, Almouzni-Pettinotti G. HJURP Is a cell-cycle-dependent maintenance and deposition factor of CENP-A at centromeres. Cell 2009; 137:485-97; PMID:19410545; https://doi.org/10.1016/j.cell.2009.02.040
  • Foltz DR, Jansen LET, Bailey AO, Yates Iii JR, Bassett EA, Wood S, Black BE, Cleveland DW. Centromere-specific assembly of CENP-A nucleosomes is mediated by HJURP. Cell 2009; 137:472-84; PMID:19410544; https://doi.org/10.1016/j.cell.2009.02.039
  • McKinley Kara L, Cheeseman Iain M. Polo-like Kinase 1 Licenses CENP-A Deposition at Centromeres. Cell 2014; 158:397-411; PMID:25036634; https://doi.org/10.1016/j.cell.2014.06.016
  • Ridley AJ. Rho GTPase signalling in cell migration. Curr Opin Cell Biol 2015; 36:103-12; PMID:26363959; https://doi.org/10.1016/j.ceb.2015.08.005
  • Schaefer A, Reinhard NR, Hordijk PL. Toward understanding RhoGTPase specificity: structure, function and local activation. Small GTPases 2014; 5:6; PMID:25483298; https://doi.org/10.4161/21541248.2014.968004
  • Dubash AD, Guilluy C, Srougi MC, Boulter E, Burridge K, Garcia-Mata R. The small GTPase RhoA localizes to the nucleus and is activated by Net1 and DNA damage signals. PloS one 2011; 6:e17380; PMID:21390328; https://doi.org/10.1371/journal.pone.0017380
  • Srougi MC, Burridge K. The nuclear guanine nucleotide exchange factors Ect2 and Net1 regulate RhoB-mediated cell death after DNA damage. PloS one 2011; 6:e17108; PMID:21373644; https://doi.org/10.1371/journal.pone.0017108
  • Sandrock K, Bielek H, Schradi K, Schmidt G, Klugbauer N. The nuclear import of the small GTPase Rac1 is mediated by the direct interaction with karyopherin alpha2. Traffic 2010; 11:198-209; PMID:19961560; https://doi.org/10.1111/j.1600-0854.2009.01015.x
  • Cha K, Sen P, Raghunayakula S, Zhang XD. The cellular distribution of RanGAP1 is regulated by CRM1-mediated nuclear export in mammalian cells. PloS one 2015; 10:e0141309.
  • Chalamalasetty RB, Hummer S, Nigg EA, Sillje HH. Influence of human Ect2 depletion and overexpression on cleavage furrow formation and abscission. J Cell Sci 2006; 119:3008-19; PMID:16803869; https://doi.org/10.1242/jcs.03032
  • Lagana A, Dorn JF, De Rop V, Ladouceur AM, Maddox AS, Maddox PS. A small GTPase molecular switch regulates epigenetic centromere maintenance by stabilizing newly incorporated CENP-A. Nat Cell Biol 2010; 12:1186-93; PMID:21102442; https://doi.org/10.1038/ncb2129
  • Goode BL, Eck MJ. Mechanism and function of formins in the control of actin assembly. Ann Rev Biochem 2007; 76:593-627; PMID:17373907; https://doi.org/10.1146/annurev.biochem.75.103004.142647
  • Bartolini F, Moseley JB, Schmoranzer J, Cassimeris L, Goode BL, Gundersen GG. The formin mDia2 stabilizes microtubules independently of its actin nucleation activity. J Cell Biol 2008; 181:523-36; PMID:18458159; https://doi.org/10.1083/jcb.200709029
  • Alberts AS, Bouquin N, Johnston LH, Treisman R. Analysis of RhoA-binding proteins reveals an interaction domain conserved in heterotrimeric G protein beta subunits and the yeast response regulator protein Skn7. J Biol Chem 1998; 273:8616-22; PMID:9535835; https://doi.org/10.1074/jbc.273.15.8616
  • Gasman S, Kalaidzidis Y, Zerial M. RhoD regulates endosome dynamics through Diaphanous-related Formin and Src tyrosine kinase. Nat Cell Biol 2003; 5:195-204; PMID:12577064; https://doi.org/10.1038/ncb935
  • Ji P, Jayapal SR, Lodish HF. Enucleation of cultured mouse fetal erythroblasts requires Rac GTPases and mDia2. Nat Cell Biol 2008; 10:314-21; PMID:18264091; https://doi.org/10.1038/ncb1693
  • Lammers M, Meyer S, Kuhlmann D, Wittinghofer A. Specificity of interactions between mDia isoforms and Rho proteins. J Biol Chem 2008; 283:35236-46; PMID:18829452; https://doi.org/10.1074/jbc.M805634200
  • Palazzo AF, Cook TA, Alberts AS, Gundersen GG. mDia mediates Rho-regulated formation and orientation of stable microtubules. Nat Cell Biol 2001; 3:723-9; PMID:11483957; https://doi.org/10.1038/35087035
  • Peng J, Wallar BJ, Flanders A, Swiatek PJ, Alberts AS. Disruption of the diaphanous-related formin Drf1 gene encoding mDia1 reveals a role for Drf3 as an effector for Cdc42. Curr Biol 2003; 13:534-45; PMID:12676083; https://doi.org/10.1016/S0960-9822(03)00170-2
  • Wallar BJ, Deward AD, Resau JH, Alberts AS. RhoB and the mammalian Diaphanous-related formin mDia2 in endosome trafficking. Exp Cell Res 2007; 313:560-71; PMID:17198702; https://doi.org/10.1016/j.yexcr.2006.10.033
  • Watanabe N, Kato T, Fujita A, Ishizaki T, Narumiya S. Cooperation between mDia1 and ROCK in Rho-induced actin reorganization. Nat Cell Biol 1999; 1:136-43; PMID:10559899; https://doi.org/10.1038/11056
  • Watanabe N, Madaule P, Reid T, Ishizaki T, Watanabe G, Kakizuka A, Saito Y, Nakao K, Jockusch BM, Narumiya S. p140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin. Embo J 1997; 16:3044-56; PMID:9214622; https://doi.org/10.1093/emboj/16.11.3044
  • Yasuda S, Oceguera-Yanez F, Kato T, Okamoto M, Yonemura S, Terada Y, Ishizaki T, Narumiya S. Cdc42 and mDia3 regulate microtubule attachment to kinetochores. Nature 2004; 428:767-71; PMID:15085137; http://dx.doi.org/10.1038/nature02452
  • Cheng L, Zhang J, Ahmad S, Rozier L, Yu H, Deng H, Mao Y. Aurora B regulates formin mDia3 in achieving metaphase chromosome alignment. Dev Cell 2011; 20:342-52; PMID:21397845; https://doi.org/10.1016/j.devcel.2011.01.008
  • Liu C, Chuang J-Z, Sung C-H, Mao Y. A dynein independent role of Tctex-1 at the kinetochore. Cell Cycle 2015; 14:1379-88; PMID:25928583; https://doi.org/10.1080/15384101.2014.1000217
  • Liu C, Mao Y. Diaphanous formin mDia2 regulates CENP-A levels at centromeres. J Cell Biol 2016; 213:415-24; PMID:27185834; https://doi.org/10.1083/jcb.201512034
  • Miki T, Okawa K, Sekimoto T, Yoneda Y, Watanabe S, Ishizaki T, Narumiya S. mDia2 shuttles between the nucleus and the cytoplasm through the importin-α/β- and CRM1-mediated nuclear transport mechanism. J Biol Chem 2009; 284:5753-62; PMID:19117945; http://dx.doi.org/10.1074/jbc.M806191200
  • Chesarone MA, DuPage AG, Goode BL. Unleashing formins to remodel the actin and microtubule cytoskeletons. Nat Rev Mol Cell Biol 2010; 11:62-74; PMID:19997130; https://doi.org/10.1038/nrm2816
  • Bartolini F, Gundersen GG. Formins and microtubules. Biochim Biophys Acta 2010; 1803:164-73; PMID:19631698; https://doi.org/10.1016/j.bbamcr.2009.07.006
  • Mao Y. FORMIN a link between kinetochores and microtubule ends. Trends Cell Biol 2011; 21:625-9; PMID:21920754; https://doi.org/10.1016/j.tcb.2011.08.005
  • Goode BL, Eck MJ. Mechanism and function of formins in the control of actin assembly. Ann Rev Biochem 2007; 76:593-627; PMID:17373907; https://doi.org/10.1146/annurev.biochem.75.103004.142647
  • Baarlink C, Wang H, Grosse R. Nuclear Actin Network Assembly by Formins Regulates the SRF Coactivator MAL. Science 2013; PMID:23558171
  • Plessner M, Melak M, Chinchilla P, Baarlink C, Grosse R. Nuclear F-actin formation and reorganization upon cell spreading. J Biol Chem 2015; PMID:25759381
  • Belin BJ, Lee T, Mullins RD. DNA damage induces nuclear actin filament assembly by Formin-2 and Spire-1/2 that promotes efficient DNA repair. eLife 2015; 4:e07735; PMID:AMBIGUOUS
  • Silva Mariana CC, Bodor Dani L, Stellfox Madison E, Martins Nuno MC, Hochegger H, Foltz Daniel R, Jansen LE. Cdk activity couples epigenetic centromere inheritance to cell cycle progression. Dev Cell 2012; 22:52-63; PMID:22169070; https://doi.org/10.1016/j.devcel.2011.10.014
  • Barnhart MC, Kuich PHJL, Stellfox ME, Ward JA, Bassett EA, Black BE, Foltz DR. HJURP is a CENP-A chromatin assembly factor sufficient to form a functional de novo kinetochore. J Cell Biol 2011; 194:229-43; PMID:21768289; https://doi.org/10.1083/jcb.201012017

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