메뉴 건너뛰기




Volumn 4, Issue AUGUST2015, 2015, Pages

DNA damage induces nuclear actin filament assembly by formin-2 and spire-1/2 that promotes efficient DNA repair

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; FORMIN 2; GREEN FLUORESCENT PROTEIN; KARYOPHERIN; MESYLIC ACID; NUCLEAR PROTEIN; PHALLOIDIN; SPIRE 1; SPIRE 2; UNCLASSIFIED DRUG; ZINOSTATIN; ACTIN BINDING PROTEIN; FORMIN 2, HUMAN; SPIRE-1 PROTEIN, HUMAN; SPIRE-2 PROTEIN, HUMAN;

EID: 84941927563     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.07735     Document Type: Article
Times cited : (179)

References (59)
  • 2
    • 84877742076 scopus 로고    scopus 로고
    • Nuclear actin network assembly by formins regulates the SRF coactivator MAL
    • Baarlink C, Wang H, Grosse R. 2013. Nuclear actin network assembly by formins regulates the SRF coactivator MAL. Science 340:864–867. doi: 10.1126/science.1235038.
    • (2013) Science , vol.340 , pp. 864-867
    • Baarlink, C.1    Wang, H.2    Grosse, R.3
  • 4
    • 84897524426 scopus 로고    scopus 로고
    • What we talk about when we talk about nuclear actin
    • Belin BJ, Mullins RD. 2013. What we talk about when we talk about nuclear actin. Nucleus 4:291–297. doi: 10.4161/nucl.25960.
    • (2013) Nucleus , vol.4 , pp. 291-297
    • Belin, B.J.1    Mullins, R.D.2
  • 5
    • 85017151534 scopus 로고    scopus 로고
    • Comparative analysis of tools for live cell imaging of actin network architecture
    • Belin BJ, Goins LM, Mullins RD. 2015. Comparative analysis of tools for live cell imaging of actin network architecture. BioArchitecture 1–14. doi: 10.1080/19490992.2014.1047714.
    • (2015) Bioarchitecture , pp. 1-14
    • Belin, B.J.1    Goins, L.M.2    Mullins, R.D.3
  • 6
    • 84860657462 scopus 로고    scopus 로고
    • Incorporation of cofilin into rods depends on disulfide intermolecular bonds: Implications for actin regulation and neurodegenerative disease
    • Bernstein BW, Shaw AE, Minamide LS, Pak CW, Bamburg JR. 2012. Incorporation of cofilin into rods depends on disulfide intermolecular bonds: implications for actin regulation and neurodegenerative disease. The Journal of Neuroscience 32:6670–6681. doi: 10.1523/JNEUROSCI.6020-11.2012.
    • (2012) The Journal of Neuroscience , vol.32 , pp. 6670-6681
    • Bernstein, B.W.1    Shaw, A.E.2    Minamide, L.S.3    Pak, C.W.4    Bamburg, J.R.5
  • 7
    • 33644747345 scopus 로고    scopus 로고
    • A selective block of nuclear actin export stabilizes the giant nuclei of Xenopus oocytes
    • Bohnsack MT, Stuven T, Kuhn C, Cordes VC, Gorlich D. 2006. A selective block of nuclear actin export stabilizes the giant nuclei of Xenopus oocytes. Nature Cell Biology 8:257–263. doi: 10.1038/ncb1357.
    • (2006) Nature Cell Biology , vol.8 , pp. 257-263
    • Bohnsack, M.T.1    Stuven, T.2    Kuhn, C.3    Cordes, V.C.4    Gorlich, D.5
  • 8
    • 84924709811 scopus 로고    scopus 로고
    • Regulation of the formin cappuccino is critical for polarity of Drosophila oocytes
    • Bor B, Bois JS, Quinlan ME. 2015. Regulation of the formin cappuccino is critical for polarity of Drosophila oocytes. Cytoskeleton 72:1–15. doi: 10.1002/cm.21205.
    • (2015) Cytoskeleton , vol.72 , pp. 1-15
    • Bor, B.1    Bois, J.S.2    Quinlan, M.E.3
  • 9
    • 84867152062 scopus 로고    scopus 로고
    • Autoinhibition of the formin Cappuccino in the absence of canonical autoinhibitory domains
    • Bor B, Vizcarra CL, Phillips ML, Quinlan ME. 2012. Autoinhibition of the formin Cappuccino in the absence of canonical autoinhibitory domains. Molecular Biology of the Cell 23:3801–3813. doi: 10.1091/mbc.E12-04-0288.
    • (2012) Molecular Biology of the Cell , vol.23 , pp. 3801-3813
    • Bor, B.1    Vizcarra, C.L.2    Phillips, M.L.3    Quinlan, M.E.4
  • 10
    • 84855842282 scopus 로고    scopus 로고
    • Formins filter modified actin subunits during processive elongation
    • Chen Q, Nag S T D. 2012. Formins filter modified actin subunits during processive elongation. Journal of Structural Biology 177:32–39. doi: 10.1016/j.jsb.2011.10.005.
    • (2012) Journal of Structural Biology , vol.177 , pp. 32-39
    • Chen, Q.1    Nag, S.2
  • 11
    • 57049132043 scopus 로고    scopus 로고
    • 53BP1 promotes non-homologous end joining of telomeres by increasing chromatin mobility
    • Dimitrova N, Chen YC, Spector DL, de Lange T. 2008. 53BP1 promotes non-homologous end joining of telomeres by increasing chromatin mobility. Nature 456:524–528. doi: 10.1038/nature07433.
    • (2008) Nature , vol.456 , pp. 524-528
    • Dimitrova, N.1    Chen, Y.C.2    Spector, D.L.3    De Lange, T.4
  • 12
    • 84855607470 scopus 로고    scopus 로고
    • The ATM protein kinase and cellular redox signaling: Beyond the DNA damage response
    • Ditch S, Paull TT. 2012. The ATM protein kinase and cellular redox signaling: beyond the DNA damage response. Trends in Biochemical Sciences 37:15–22. doi: 10.1016/j.tibs.2011.10.002.
    • (2012) Trends in Biochemical Sciences , vol.37 , pp. 15-22
    • Ditch, S.1    Paull, T.T.2
  • 14
    • 34247239350 scopus 로고    scopus 로고
    • Conserved actin cysteine residues are oxidative stress sensors that can regulate cell death in yeast
    • Farah ME, Amberg DC. 2007. Conserved actin cysteine residues are oxidative stress sensors that can regulate cell death in yeast. Molecular Biology of the Cell 18:1359–1365. doi: 10.1091/mbc.E06-08-0718.
    • (2007) Molecular Biology of the Cell , vol.18 , pp. 1359-1365
    • Farah, M.E.1    Amberg, D.C.2
  • 15
    • 79959351431 scopus 로고    scopus 로고
    • Diverse protective roles of the actin cytoskeleton during oxidative stress
    • Farah ME, Sirotkin V, Haarer B, Kakhniashvili D, Amberg DC. 2011. Diverse protective roles of the actin cytoskeleton during oxidative stress. Cytoskeleton 68:340–354. doi: 10.1002/cm.20516.
    • (2011) Cytoskeleton , vol.68 , pp. 340-354
    • Farah, M.E.1    Sirotkin, V.2    Haarer, B.3    Kakhniashvili, D.4    Amberg, D.C.5
  • 16
    • 44449139885 scopus 로고    scopus 로고
    • Chromatin remodelling and actin reorganization
    • Farrants AO. 2008. Chromatin remodelling and actin reorganization. FEBS Letters 585:2041–2050. doi: 10.1016/j.febslet.2008.04.032.
    • (2008) FEBS Letters , vol.585 , pp. 2041-2050
    • Farrants, A.O.1
  • 17
    • 84885179258 scopus 로고    scopus 로고
    • A nuclear F-actin scaffold stabilizes ribonucleoprotein droplets against gravity in large cells
    • Feric M, Brangwynne CP. 2013. A nuclear F-actin scaffold stabilizes ribonucleoprotein droplets against gravity in large cells. Nature Cell Biology 15:1253–1259. doi: 10.1038/ncb2830.
    • (2013) Nature Cell Biology , vol.15 , pp. 1253-1259
    • Feric, M.1    Brangwynne, C.P.2
  • 18
    • 0017834489 scopus 로고
    • Intranuclear actin bundles induced by dimethyl sulfoxide in interphase nucleus of Dictyostelium
    • Fukui Y. 1978. Intranuclear actin bundles induced by dimethyl sulfoxide in interphase nucleus of Dictyostelium. The Journal of Cell Biology 76:146–157. doi: 10.1083/jcb.76.1.146.
    • (1978) The Journal of Cell Biology , vol.76 , pp. 146-157
    • Fukui, Y.1
  • 19
    • 0018881934 scopus 로고
    • Dynamics of nuclear actin bundle induction by dimethyl sulfoxide and factors affecting its development
    • Fukui Y, Katsumaru H. 1980. Dynamics of nuclear actin bundle induction by dimethyl sulfoxide and factors affecting its development. The Journal of Cell Biology 84:131–140. doi: 10.1083/jcb.84.1.131.
    • (1980) The Journal of Cell Biology , vol.84 , pp. 131-140
    • Fukui, Y.1    Katsumaru, H.2
  • 21
    • 0014033467 scopus 로고
    • Isolation and characterization of plasmodium actin
    • Hatano S, Oosawa F. 1966. Isolation and characterization of plasmodium actin. Biochimica et Biophysica Acta 127:488–498. doi: 10.1016/0304-4165(66)90402-8.
    • (1966) Biochimica Et Biophysica Acta , vol.127 , pp. 488-498
    • Hatano, S.1    Oosawa, F.2
  • 22
    • 84923781513 scopus 로고    scopus 로고
    • Lansford R. 2014. Generation and analysis of lentivirus expressing a 2A peptide-linked bicistronic fluorescent construct
    • Huss D, Lansford R. 2014. generation and analysis of lentivirus expressing a 2A peptide-linked bicistronic fluorescent construct. Cold Spring Harbor Protocols 2014:1290–1311. doi: 10.1101/pdb.prot081422.
    • (2014) Cold Spring Harbor Protocols , pp. 1290-1311
    • Huss, D.1
  • 23
    • 0026550804 scopus 로고
    • The KKRKK sequence is involved in heat 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 heat shock-induced nuclear translocation of the 18-kDa actin-binding protein, cofilin. Cell Structure and Function 17:39–46. doi: 10.1247/csf.17.39.
    • (1992) Cell Structure and Function , vol.17 , pp. 39-46
    • Iida, K.1    Matsumoto, S.2    Yahara, I.3
  • 24
    • 84863482471 scopus 로고    scopus 로고
    • Biophysical mechanism of T-cell receptor triggering in a reconstituted system
    • James JR, Vale RD. 2012. Biophysical mechanism of T-cell receptor triggering in a reconstituted system. Nature 487:64–69. doi: 10.1038/nature11220.
    • (2012) Nature , vol.487 , pp. 64-69
    • James, J.R.1    Vale, R.D.2
  • 26
    • 66349108700 scopus 로고    scopus 로고
    • Reactive oxygen species regulate a slingshot-cofilin activation pathway
    • Kim JS, Huang TY, Bokoch GM. 2009. Reactive oxygen species regulate a slingshot-cofilin activation pathway. Molecular Biology of the Cell 20:2650–2660. doi: 10.1091/mbc.E09-02-0131.
    • (2009) Molecular Biology of the Cell , vol.20 , pp. 2650-2660
    • Kim, J.S.1    Huang, T.Y.2    Bokoch, G.M.3
  • 27
    • 67649845784 scopus 로고    scopus 로고
    • Systematic identification of cell cycle-dependent yeast nucleocytoplasmic shuttling proteins by prediction of composite motifs
    • Kosugi S, Hasebe M, Tomita M, Yanagawa H. 2009. Systematic identification of cell cycle-dependent yeast nucleocytoplasmic shuttling proteins by prediction of composite motifs. Proceedings of the National Academy of Sciences of USA 106:10171–10176. doi: 10.1073/pnas.0900604106.
    • (2009) Proceedings of the National Academy of Sciences of USA , vol.106 , pp. 10171-10176
    • Kosugi, S.1    Hasebe, M.2    Tomita, M.3    Yanagawa, H.4
  • 28
    • 23844466646 scopus 로고    scopus 로고
    • A contractile nuclear actin network drives chromosome congression in oocytes
    • Lenart P, Bacher CP, Daigle N, Hand AR, Eils R, Terasaki M, Ellenberg J. 2005. A contractile nuclear actin network drives chromosome congression in oocytes. Nature 436:812–818. doi: 10.1038/nature03810.
    • (2005) Nature , vol.436 , pp. 812-818
    • Lenart, P.1    Bacher, C.P.2    Daigle, N.3    Hand, A.R.4    Eils, R.5    Terasaki, M.6    Ellenberg, J.7
  • 30
    • 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
    • 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 Research 64:4833–4840. doi: 10.1158/0008-5472.CAN-04-0953.
    • (2004) Cancer Research , vol.64 , 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
  • 31
    • 49749114828 scopus 로고    scopus 로고
    • Development of a family of redox-sensitive green fluorescent protein indicators for use in relatively oxidizing subcellular environments
    • Lohman JR, Remington SJ. 2008. Development of a family of redox-sensitive green fluorescent protein indicators for use in relatively oxidizing subcellular environments. Biochemistry 47:8678–8688. doi: 10.1021/bi800498g.
    • (2008) Biochemistry , vol.47 , pp. 8678-8688
    • Lohman, J.R.1    Remington, S.J.2
  • 33
    • 1842339879 scopus 로고    scopus 로고
    • Reprogramming of telomerase by expression of mutant telomerase RNA template in human cells leads to altered telomeres that correlate with reduced cell viability
    • Marusic L, Anton M, Tidy A, Wang P, Villeponteau B, Bacchetti S. 1997. Reprogramming of telomerase by expression of mutant telomerase RNA template in human cells leads to altered telomeres that correlate with reduced cell viability. Molecular and Cellular Biology 17:6394–6401.
    • (1997) Molecular and Cellular Biology , vol.17 , pp. 6394-6401
    • Marusic, L.1    Anton, M.2    Tidy, A.3    Wang, P.4    Villeponteau, B.5    Bacchetti, S.6
  • 35
    • 56349087407 scopus 로고    scopus 로고
    • Real-time redox measurements during endoplasmic reticulum stress reveal interlinked protein folding functions
    • Merksamer PI, Trusina A, Papa FR. 2008. Real-time redox measurements during endoplasmic reticulum stress reveal interlinked protein folding functions. Cell 135:933–947. doi: 10.1016/j.cell.2008.10.011.
    • (2008) Cell , vol.135 , pp. 933-947
    • Merksamer, P.I.1    Trusina, A.2    Papa, F.R.3
  • 36
    • 84886751857 scopus 로고    scopus 로고
    • DNA in motion during double-strand break repair
    • Mine-Hattab J, Rothstein R. 2013. DNA in motion during double-strand break repair. Trends in Cell Biology 23:529–536. doi: 10.1016/j.tcb.2013.05.006.
    • (2013) Trends in Cell Biology , vol.23 , pp. 529-536
    • Mine-Hattab, J.1    Rothstein, R.2
  • 38
    • 84902584011 scopus 로고    scopus 로고
    • An Arp2/3 nucleated F-actin shell fragments nuclear membranes at nuclear envelope breakdown in starfish oocytes
    • Mori M, Somogyi K, Kondo H, Monnier N, Falk HJ, Machado P, Bathe M, Nedelec F, Lenart P. 2014. An Arp2/3 nucleated F-actin shell fragments nuclear membranes at nuclear envelope breakdown in starfish oocytes. Current Biology 24:1421–1428. doi: 10.1016/j.cub.2014.05.019.
    • (2014) Current Biology , vol.24 , pp. 1421-1428
    • Mori, M.1    Somogyi, K.2    Kondo, H.3    Monnier, N.4    Falk, H.J.5    Machado, P.6    Bathe, M.7    Nedelec, F.8    Lenart, P.9
  • 39
    • 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. The EMBO Journal 27:3198–3208. doi: 10.1038/emboj.2008.235.
    • (2008) The EMBO Journal , vol.27 , pp. 3198-3208
    • Mouilleron, S.1    Guettler, S.2    Langer, C.A.3    Treisman, R.4    McDonald, N.Q.5
  • 40
    • 84869136860 scopus 로고    scopus 로고
    • Cofilin nuclear-cytoplasmic shuttling affects cofilin-actin rod formation during stress
    • Munsie LN, Desmond CR, Truant R. 2012. Cofilin nuclear-cytoplasmic shuttling affects cofilin-actin rod formation during stress. Journal of Cell Science 125:3977–3988. doi: 10.1242/jcs.097667.
    • (2012) Journal of Cell Science , vol.125 , pp. 3977-3988
    • Munsie, L.N.1    Desmond, C.R.2    Truant, R.3
  • 41
    • 0036971460 scopus 로고    scopus 로고
    • Actin in the nucleus: What form and what for?
    • Pederson T, Aebi U. 2002. Actin in the nucleus: what form and what for? Journal of Structural Biology 140:3–9. doi: 10.1016/S1047-8477(02)00528-2.
    • (2002) Journal of Structural Biology , vol.140 , pp. 3-9
    • Pederson, T.1    Aebi, U.2
  • 42
    • 0037515668 scopus 로고    scopus 로고
    • Latrunculin B or ATP depletion induces cofilin-dependent translocation of actin into nuclei of mast cells
    • 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. The Journal of Biological Chemistry 278:14394–14400. doi: 10.1074/jbc.M206393200.
    • (2003) The Journal of Biological Chemistry , vol.278 , pp. 14394-14400
    • Pendleton, A.1    Pope, B.2    Weeds, A.3    Koffer, A.4
  • 45
    • 13444292982 scopus 로고    scopus 로고
    • Drosophila Spire is an actin nucleation factor
    • Quinlan ME, Heuser JE, Kerkhoff E, Mullins RD. 2005. Drosophila Spire is an actin nucleation factor. Nature 433:382–388. doi: 10.1038/nature03241.
    • (2005) Nature , vol.433 , pp. 382-388
    • Quinlan, M.E.1    Heuser, J.E.2    Kerkhoff, E.3    Mullins, R.D.4
  • 48
    • 0035813147 scopus 로고    scopus 로고
    • Inositol 1,4,5-trisphosphate 3-kinase A associates with F-actin and dendritic spines via its N terminus
    • Schell MJ, Erneux C, Irvine RF. 2001. Inositol 1,4,5-trisphosphate 3-kinase A associates with F-actin and dendritic spines via its N terminus. The Journal of Biological Chemistry 276:37537–37546. doi: 10.1074/jbc.M104101200.
    • (2001) The Journal of Biological Chemistry , vol.276 , pp. 37537-37546
    • Schell, M.J.1    Erneux, C.2    Irvine, R.F.3
  • 49
    • 84856133266 scopus 로고    scopus 로고
    • An actin-dependent mechanism for long-range vesicle transport
    • Schuh M. 2011. An actin-dependent mechanism for long-range vesicle transport. Nature Cell Biology 13:1431–1436. doi: 10.1038/ncb2353.
    • (2011) Nature Cell Biology , vol.13 , pp. 1431-1436
    • Schuh, M.1
  • 50
    • 57649245603 scopus 로고    scopus 로고
    • A new model for asymmetric spindle positioning in mouse oocytes
    • Schuh M, Ellenberg J. 2008. A new model for asymmetric spindle positioning in mouse oocytes. Current Biology 18:1986–1992. doi: 10.1016/j.cub.2008.11.022.
    • (2008) Current Biology , vol.18 , pp. 1986-1992
    • Schuh, M.1    Ellenberg, J.2
  • 51
    • 48549084245 scopus 로고    scopus 로고
    • ATM mediates cytotoxicity of a mutant telomerase RNA in human cancer cells
    • Stohr BA, Blackburn EH. 2008. ATM mediates cytotoxicity of a mutant telomerase RNA in human cancer cells. Cancer Research 68:5309–5317. doi: 10.1158/0008-5472.CAN-08-0504.
    • (2008) Cancer Research , vol.68 , pp. 5309-5317
    • Stohr, B.A.1    Blackburn, E.H.2
  • 53
    • 0242641546 scopus 로고    scopus 로고
    • Exportin 6: A novel nuclear export receptor that is specific for profiling actin complexes
    • Stuven T, Hartmann E, Gorlich D. 2003. Exportin 6: a novel nuclear export receptor that is specific for profiling actin complexes. The EMBO Journal 22:5928–5940.
    • (2003) The EMBO Journal , vol.22 , pp. 5928-5940
    • Stuven, T.1    Hartmann, E.2    Gorlich, D.3
  • 54
    • 34250849566 scopus 로고    scopus 로고
    • Nuclear actin regulates dynamic subcellular localization and activity of the SRF cofactor MAL
    • Vartiainen MK, Guettler S, Larijani B, Treisman R. 2007. Nuclear actin regulates dynamic subcellular localization and activity of the SRF cofactor MAL. Science 316:1749–1752. doi: 10.1126/science.1141084.
    • (2007) Science , vol.316 , pp. 1749-1752
    • Vartiainen, M.K.1    Guettler, S.2    Larijani, B.3    Treisman, R.4
  • 56
    • 84876864559 scopus 로고    scopus 로고
    • Identification and functional characterization of FMN2, a regulator of the cyclin-dependent kinase inhibitorp21
    • Yamada K, Ono M, Perkins ND, Rocha S, Lamond AI. 2013a. Identification and functional characterization of FMN2, a regulator of the cyclin-dependent kinase inhibitorp21. Molecular Cell 49:922–933. doi: 10.1016/j.molcel.2012.12.023.
    • (2013) Molecular Cell , vol.49 , pp. 922-933
    • Yamada, K.1    Ono, M.2    Perkins, N.D.3    Rocha, S.4    Lamond, A.I.5
  • 57
    • 84881501068 scopus 로고    scopus 로고
    • FMN2 is a novel regulator of the cyclin-dependent kinase inhibitor p21
    • Yamada K, Ono M, Bensaddek D, Lamond AI, Rocha S. 2013b. FMN2 is a novel regulator of the cyclin-dependent kinase inhibitor p21. Cell Cycle 12:2348–2354. doi: 10.4161/cc.25511.
    • (2013) Cell Cycle , vol.12 , pp. 2348-2354
    • Yamada, K.1    Ono, M.2    Bensaddek, D.3    Lamond, A.I.4    Rocha, S.5
  • 58
    • 84882424327 scopus 로고    scopus 로고
    • Formation of cofilin-actin rods following cucurbitacin-Binduced actin aggregation depends on Slingshot homolog1-mediated cofilin hyperactivation
    • Zhang YT, Ouyang DY, Xu LH, Zha QB, He XH. 2013. Formation of cofilin-actin rods following cucurbitacin-Binduced actin aggregation depends on Slingshot homolog1-mediated cofilin hyperactivation. Journal of Cellular Biochemistry 114(10):2415–2429. doi: 10.1002/jcb.24587.
    • (2013) Journal of Cellular Biochemistry , vol.114 , Issue.10 , pp. 2415-2429
    • Zhang, Y.T.1    Ouyang, D.Y.2    Xu, L.H.3    Zha, Q.B.4    He, X.H.5
  • 59
    • 84857852663 scopus 로고    scopus 로고
    • Actin binding to WH2 domains regulates nuclear import of the multifunctional actin regulator JMY
    • Zuchero JB, Belin B, Mullins RD. 2012. Actin binding to WH2 domains regulates nuclear import of the multifunctional actin regulator JMY. Molecular Biology of the Cell 23:853–863. doi: 10.1091/mbc.E11-12-0992.
    • (2012) Molecular Biology of the Cell , vol.23 , pp. 853-863
    • Zuchero, J.B.1    Belin, B.2    Mullins, R.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.