메뉴 건너뛰기




Volumn 318, Issue 18, 2012, Pages 2365-2376

Nucleolar exit of RNF8 and BRCA1 in response to DNA damage

Author keywords

BRCA1; DNA damage; Nucleolus; RNF8

Indexed keywords

BRCA1 PROTEIN; DNA; FORKHEAD ASSOCIATED PROTEIN; RIBOSOME PROTEIN; RING FINGER PROTEIN; RNF8 PROTEIN; RPSA PROTEIN; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 84865305782     PISSN: 00144827     EISSN: 10902422     Source Type: Journal    
DOI: 10.1016/j.yexcr.2012.07.003     Document Type: Article
Times cited : (25)

References (41)
  • 1
    • 78649336706 scopus 로고    scopus 로고
    • The DNA damage response: making it safe to play with knives
    • Ciccia A., Elledge S.J. The DNA damage response: making it safe to play with knives. Mol. Cell 2010, 40:179-204.
    • (2010) Mol. Cell , vol.40 , pp. 179-204
    • Ciccia, A.1    Elledge, S.J.2
  • 2
    • 36749022214 scopus 로고    scopus 로고
    • The DNA damage response: ten years after
    • Harper J.W., Elledge S.J. The DNA damage response: ten years after. Mol. Cell 2007, 28:739-745.
    • (2007) Mol. Cell , vol.28 , pp. 739-745
    • Harper, J.W.1    Elledge, S.J.2
  • 3
    • 79952235291 scopus 로고    scopus 로고
    • Dynamics of DNA damage response proteins at DNA breaks: a focus on protein modifications
    • Polo S.E., Jackson S.P. Dynamics of DNA damage response proteins at DNA breaks: a focus on protein modifications. Genes Dev. 2011, 25:409-433.
    • (2011) Genes Dev. , vol.25 , pp. 409-433
    • Polo, S.E.1    Jackson, S.P.2
  • 5
    • 36249031962 scopus 로고    scopus 로고
    • RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly
    • Huen M.S., Grant R., Manke I., Minn K., Yu X., Yaffe M.B., Chen J. RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly. Cell 2007, 131:901-914.
    • (2007) Cell , vol.131 , pp. 901-914
    • Huen, M.S.1    Grant, R.2    Manke, I.3    Minn, K.4    Yu, X.5    Yaffe, M.B.6    Chen, J.7
  • 7
    • 36248966246 scopus 로고    scopus 로고
    • RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins
    • Mailand N., Bekker-Jensen S., Faustrup H., Melander F., Bartek J., Lukas C., Lukas J. RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins. Cell 2007, 131:887-900.
    • (2007) Cell , vol.131 , pp. 887-900
    • Mailand, N.1    Bekker-Jensen, S.2    Faustrup, H.3    Melander, F.4    Bartek, J.5    Lukas, C.6    Lukas, J.7
  • 8
    • 36749025467 scopus 로고    scopus 로고
    • S.J. Rnf8 ubiquitin/Rnf8 ubiquitin ligases control foci formation of the Rap80/Abraxas/Brca1/Brcc36 complex in response to DNA damage
    • B. Wang, S.J. Rnf8 ubiquitin/Rnf8 ubiquitin ligases control foci formation of the Rap80/Abraxas/Brca1/Brcc36 complex in response to DNA damage, Proc. Nat. Acad. Sci. U. S. A. 104 (2007) 20759-20763.
    • (2007) Proc. Nat. Acad. Sci. U. S. A. , vol.104 , pp. 20759-20763
    • Wang, B.1
  • 12
    • 66849138419 scopus 로고    scopus 로고
    • Solving the RIDDLE of 53BP1 recruitment to sites of damage
    • Stewart G.S. Solving the RIDDLE of 53BP1 recruitment to sites of damage. Cell Cycle 2009, 8:1532-1538.
    • (2009) Cell Cycle , vol.8 , pp. 1532-1538
    • Stewart, G.S.1
  • 16
  • 17
    • 75949124023 scopus 로고    scopus 로고
    • Assembly of checkpoint and repair machineries at DNA damage sites
    • Huen M.S., Chen J. Assembly of checkpoint and repair machineries at DNA damage sites. Trends Biochem. Sci. 2009, 35:101-108.
    • (2009) Trends Biochem. Sci. , vol.35 , pp. 101-108
    • Huen, M.S.1    Chen, J.2
  • 19
    • 39849092543 scopus 로고    scopus 로고
    • Regulation of mitotic exit by the RNF8 ubiquitin ligase
    • Plans V., Guerra-Rebollo M., Thomson T.M. Regulation of mitotic exit by the RNF8 ubiquitin ligase. Oncogene 2008, 27:1355-1365.
    • (2008) Oncogene , vol.27 , pp. 1355-1365
    • Plans, V.1    Guerra-Rebollo, M.2    Thomson, T.M.3
  • 20
    • 33144459648 scopus 로고    scopus 로고
    • The RING finger protein RNF8 recruits UBC13 for lysine 63-based self polyubiquitylation
    • Plans V., Scheper J., Soler M., Loukili N., Okano Y., Thomson T.M. The RING finger protein RNF8 recruits UBC13 for lysine 63-based self polyubiquitylation. J. Cell. Biochem. 2006, 97:572-582.
    • (2006) J. Cell. Biochem. , vol.97 , pp. 572-582
    • Plans, V.1    Scheper, J.2    Soler, M.3    Loukili, N.4    Okano, Y.5    Thomson, T.M.6
  • 23
    • 70449084692 scopus 로고    scopus 로고
    • Efficient protection and isolation of ubiquitylated proteins using tandem ubiquitin-binding entities
    • Hjerpe R., Aillet F., Lopitz-Otsoa F., Lang V., England P., Rodriguez M.S. Efficient protection and isolation of ubiquitylated proteins using tandem ubiquitin-binding entities. EMBO Rep. 2009, 10:1250-1258.
    • (2009) EMBO Rep. , vol.10 , pp. 1250-1258
    • Hjerpe, R.1    Aillet, F.2    Lopitz-Otsoa, F.3    Lang, V.4    England, P.5    Rodriguez, M.S.6
  • 24
    • 11244269445 scopus 로고    scopus 로고
    • The CDK regulates repair of double-strand breaks by homologous recombination during the cell cycle
    • Aylon Y., Liefshitz B., Kupiec M. The CDK regulates repair of double-strand breaks by homologous recombination during the cell cycle. EMBO J. 2004, 23:4868-4875.
    • (2004) EMBO J. , vol.23 , pp. 4868-4875
    • Aylon, Y.1    Liefshitz, B.2    Kupiec, M.3
  • 25
    • 77449086623 scopus 로고    scopus 로고
    • DNA resection in eukaryotes: deciding how to fix the break
    • Huertas P. DNA resection in eukaryotes: deciding how to fix the break. Nat. Struct. Mol. Biol. 2010, 17:11-16.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 11-16
    • Huertas, P.1
  • 29
    • 33845286542 scopus 로고    scopus 로고
    • BRCA1 foci in normal S-phase nuclei are linked to interphase centromeres and replication of pericentric heterochromatin
    • Pageau G.J., Lawrence J.B. BRCA1 foci in normal S-phase nuclei are linked to interphase centromeres and replication of pericentric heterochromatin. J. Cell Biol. 2006, 175:693-701.
    • (2006) J. Cell Biol. , vol.175 , pp. 693-701
    • Pageau, G.J.1    Lawrence, J.B.2
  • 30
    • 84861800872 scopus 로고    scopus 로고
    • Three-dimensional imaging reveals the spatial separation of gammaH2AX-MDC1-53BP1 and RNF8-RNF168-BRCA1-A complexes at ionizing radiation-induced foci
    • Mok M.T., Henderson B.R. Three-dimensional imaging reveals the spatial separation of gammaH2AX-MDC1-53BP1 and RNF8-RNF168-BRCA1-A complexes at ionizing radiation-induced foci. Radiother. Oncol. 2012, 103:415-420.
    • (2012) Radiother. Oncol. , vol.103 , pp. 415-420
    • Mok, M.T.1    Henderson, B.R.2
  • 32
    • 78649375395 scopus 로고    scopus 로고
    • Translational regulation of gene expression during conditions of cell stress
    • Spriggs K.A., Bushell M., Willis A.E. Translational regulation of gene expression during conditions of cell stress. Mol. Cell 2010, 40:228-237.
    • (2010) Mol. Cell , vol.40 , pp. 228-237
    • Spriggs, K.A.1    Bushell, M.2    Willis, A.E.3
  • 34
    • 0026554288 scopus 로고
    • A 33-kDa polypeptide with homology to the laminin receptor: component of translation machinery
    • Auth D., Brawerman G. A 33-kDa polypeptide with homology to the laminin receptor: component of translation machinery. Proc. Natl. Acad. Sci. U S A 1992, 89:4368-4372.
    • (1992) Proc. Natl. Acad. Sci. U S A , vol.89 , pp. 4368-4372
    • Auth, D.1    Brawerman, G.2
  • 36
    • 41249088465 scopus 로고    scopus 로고
    • Crystal structure of the human laminin receptor precursor
    • Jamieson K.V., Wu J., Hubbard S.R., Meruelo D. Crystal structure of the human laminin receptor precursor. J. Biol. Chem. 2008, 283:3002-3005.
    • (2008) J. Biol. Chem. , vol.283 , pp. 3002-3005
    • Jamieson, K.V.1    Wu, J.2    Hubbard, S.R.3    Meruelo, D.4
  • 37
    • 78650418551 scopus 로고    scopus 로고
    • Structure-guided identification of a laminin binding site on the laminin receptor precursor
    • Jamieson K.V., Hubbard S.R., Meruelo D. Structure-guided identification of a laminin binding site on the laminin receptor precursor. J. Mol. Biol. 2010, 405:24-32.
    • (2010) J. Mol. Biol. , vol.405 , pp. 24-32
    • Jamieson, K.V.1    Hubbard, S.R.2    Meruelo, D.3
  • 38
    • 78650414544 scopus 로고    scopus 로고
    • Extraribosomal functions associated with the C terminus of the 37/67kDa laminin receptor are required for maintaining cell viability
    • Scheiman J., Jamieson K.V., Ziello J., Tseng J.C., Meruelo D. Extraribosomal functions associated with the C terminus of the 37/67kDa laminin receptor are required for maintaining cell viability. Cell Death Diff. 2010, 1:e42.
    • (2010) Cell Death Diff. , vol.1
    • Scheiman, J.1    Jamieson, K.V.2    Ziello, J.3    Tseng, J.C.4    Meruelo, D.5
  • 39
    • 79251569266 scopus 로고    scopus 로고
    • Interactions between laminin receptor and the cytoskeleton during translation and cell motility
    • Venticinque L., Jamieson K.V., Meruelo D. Interactions between laminin receptor and the cytoskeleton during translation and cell motility. PLoS One 2011, 6:e15895.
    • (2011) PLoS One , vol.6
    • Venticinque, L.1    Jamieson, K.V.2    Meruelo, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.