메뉴 건너뛰기




Volumn 288, Issue 27, 2013, Pages 19604-19613

Identification and functional characterization of a ku-binding motif in aprataxin polynucleotide kinase/phosphatase-like factor (APLF)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID MOTIFS; DIRECT INTERACTIONS; FORKHEAD-ASSOCIATED DOMAIN; FUNCTIONAL CHARACTERIZATION; FUNCTIONAL REQUIREMENT; NONHOMOLOGOUS END JOINING; NUCLEAR LOCALIZATION SIGNAL; PHYSICAL INTERACTIONS;

EID: 84880049843     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.440388     Document Type: Article
Times cited : (36)

References (38)
  • 1
    • 70350504453 scopus 로고    scopus 로고
    • The DNA damage response in human biology and disease
    • Jackson, S. P., and Bartek, J. (2009) The DNA damage response in human biology and disease. Nature 461, 1071-1078
    • (2009) Nature , vol.461 , pp. 1071-1078
    • Jackson, S.P.1    Bartek, J.2
  • 2
    • 79952235291 scopus 로고    scopus 로고
    • Denamics of DNA damage response proteins at DNA breaks: A focus on protein modifications
    • Polo, S. E., and Jackson, S. P. (2011) Dynamics of DNA damage response proteins at DNA breaks: a focus on protein modifications. Genes Dev. 25, 409-433
    • (2011) Genes Dev , vol.25 , pp. 409-433
    • Polo, S.E.1    Jackson, S.P.2
  • 3
    • 77955841149 scopus 로고    scopus 로고
    • Collaboration and competition between DNA double-strand break repair pathways
    • Kass, E. M., and Jasin, M. (2010) Collaboration and competition between DNA double-strand break repair pathways. FEBS Lett. 584, 3703-3708
    • (2010) FEBS Lett , vol.584 , pp. 3703-3708
    • Kass, E.M.1    Jasin, M.2
  • 4
    • 4544362838 scopus 로고    scopus 로고
    • The mechanism of non-homologous end-joining: A synopsis of synapsis
    • Weterings, E., and van Gent, D. C. (2004) The mechanism of non-homologous end-joining: a synopsis of synapsis. DNA Repair 3, 1425-1435
    • (2004) DNA Repair , vol.3 , pp. 1425-1435
    • Weterings, E.1    Van Gent, D.C.2
  • 5
    • 0040077747 scopus 로고    scopus 로고
    • Dimerization, translocation and localization of Ku70 and Ku80 proteins
    • Koike, M. (2002) Dimerization, translocation and localization of Ku70 and Ku80 proteins. J. Radiat. Res. 43, 223-236
    • (2002) J. Radiat. Res , vol.43 , pp. 223-236
    • Koike, M.1
  • 6
    • 0033198709 scopus 로고    scopus 로고
    • Mapping of protein-protein interactions within the DNA-dependent protein kinase complex
    • Gell, D., and Jackson, S. P. (1999) Mapping of protein-protein interactions within the DNA-dependent protein kinase complex. Nucleic Acids Res. 27, 3494-3502
    • (1999) Nucleic Acids Res , vol.27 , pp. 3494-3502
    • Gell, D.1    Jackson, S.P.2
  • 7
    • 2342565902 scopus 로고    scopus 로고
    • A means to a DNA end: The many roles of Ku
    • Downs, J. A., and Jackson, S. P. (2004) A means to a DNA end: the many roles of Ku. Nat. Rev. Mol. Cell Biol. 5, 367-378
    • (2004) Nat. Rev. Mol. Cell Biol , vol.5 , pp. 367-378
    • Downs, J.A.1    Jackson, S.P.2
  • 8
    • 0029740571 scopus 로고    scopus 로고
    • Protein-protein and protein-DNA interaction regions within the DNA end-binding protein Ku70-Ku86
    • Wu, X., and Lieber, M. R. (1996) Protein-protein and protein-DNA interaction regions within the DNA end-binding protein Ku70-Ku86. Mol. Cell. Biol. 16, 5186-5193
    • (1996) Mol. Cell. Biol , vol.16 , pp. 5186-5193
    • Wu, X.1    Lieber, M.R.2
  • 9
    • 0036714151 scopus 로고    scopus 로고
    • Displacement of DNA-PKcs from DNA ends by the Werner syndrome protein
    • Li, B., and Comai, L. (2002) Displacement of DNA-PKcs from DNA ends by the Werner syndrome protein. Nucleic Acids Res. 30, 3653-3661
    • (2002) Nucleic Acids Res , vol.30 , pp. 3653-3661
    • Li, B.1    Comai, L.2
  • 10
    • 0035851181 scopus 로고    scopus 로고
    • Werner syndrome protein is regulated and phosphorylated by DNA-dependent protein kinase
    • Yannone, S. M., Roy, S., Chan, D. W., Murphy, M. B., Huang, S., Campisi, J., and Chen, D. J. (2001) Werner syndrome protein is regulated and phosphorylated by DNA-dependent protein kinase. J. Biol. Chem. 276, 38242-38248
    • (2001) J. Biol. Chem , vol.276 , pp. 38242-38248
    • Yannone, S.M.1    Roy, S.2    Chan, D.W.3    Murphy, M.B.4    Huang, S.5    Campisi, J.6    Chen, D.J.7
  • 11
    • 0035971076 scopus 로고    scopus 로고
    • Requirements for the nucleolytic processing of DNA ends by the Werner syndrome protein-Ku70/80 complex
    • Li, B., and Comai, L. (2001) Requirements for the nucleolytic processing of DNA ends by the Werner syndrome protein-Ku70/80 complex. J. Biol. Chem. 276, 9896-9902
    • (2001) J. Biol. Chem , vol.276 , pp. 9896-9902
    • Li, B.1    Comai, L.2
  • 12
    • 0032518680 scopus 로고    scopus 로고
    • Ku protein stimulates DNA end joining by mammalian DNA ligases: A direct role for Ku in repair of DNA double-strand breaks
    • Ramsden, D. A., and Gellert, M. (1998) Ku protein stimulates DNA end joining by mammalian DNA ligases: a direct role for Ku in repair of DNA double-strand breaks. EMBO J. 17, 609-614
    • (1998) EMBO J. , vol.17 , pp. 609-614
    • Ramsden, D.A.1    Gellert, M.2
  • 14
    • 0034714199 scopus 로고    scopus 로고
    • Interactions of theDNAligase IV-XRCC4 complex withDNAends and the DNA-dependent protein kinase
    • Chen, L., Trujillo, K., Sung, P., and Tomkinson, A. E. (2000) Interactions of theDNAligase IV-XRCC4 complex withDNAends and the DNA-dependent protein kinase. J. Biol. Chem. 275, 26196-26205
    • (2000) J. Biol. Chem , vol.275 , pp. 26196-26205
    • Chen, L.1    Trujillo, K.2    Sung, P.3    Tomkinson, A.E.4
  • 15
    • 31044432090 scopus 로고    scopus 로고
    • XLF interacts with the XRCC4-DNA ligase IV complex to promote DNA nonhomologous endjoining
    • Ahnesorg, P., Smith, P., and Jackson, S. P. (2006) XLF interacts with the XRCC4-DNA ligase IV complex to promote DNA nonhomologous endjoining. Cell 124, 301-313
    • (2006) Cell , vol.124 , pp. 301-313
    • Ahnesorg, P.1    Smith, P.2    Jackson, S.P.3
  • 18
    • 37549023517 scopus 로고    scopus 로고
    • APLF (C2orf13) facilitates nonhomologous end-joining and undergoes ATM-dependent hyperphosphorylation following ionizing radiation
    • Macrae, C. J., McCulloch, R. D., Ylanko, J., Durocher, D., and Koch, C. A. (2008) APLF (C2orf13) facilitates nonhomologous end-joining and undergoes ATM-dependent hyperphosphorylation following ionizing radiation. DNA Repair (Amst.) 7, 292-302
    • (2008) DNA Repair (Amst.) , vol.7 , pp. 292-302
    • MacRae, C.J.1    McCulloch, R.D.2    Ylanko, J.3    Durocher, D.4    Koch, C.A.5
  • 19
    • 34247245102 scopus 로고    scopus 로고
    • A novel human AP endonuclease with conserved zincfinger-like motifs involved in DNA strand break responses
    • Kanno, S., Kuzuoka, H., Sasao, S., Hong, Z., Lan, L., Nakajima, S., and Yasui, A. (2007) A novel human AP endonuclease with conserved zincfinger-like motifs involved in DNA strand break responses. EMBO J. 26, 2094-2103
    • (2007) EMBO J. , vol.26 , pp. 2094-2103
    • Kanno, S.1    Kuzuoka, H.2    Sasao, S.3    Hong, Z.4    Lan, L.5    Nakajima, S.6    Yasui, A.7
  • 20
    • 34248157719 scopus 로고    scopus 로고
    • APLF (C2orf13) is a novel human protein involved in the cellular response to chromosomal DNA strand breaks
    • Iles, N., Rulten, S., El-Khamisy, S. F., and Caldecott, K. W. (2007) APLF (C2orf13) is a novel human protein involved in the cellular response to chromosomal DNA strand breaks. Mol. Cell. Biol. 27, 3793-3803
    • (2007) Mol. Cell. Biol , vol.27 , pp. 3793-3803
    • Iles, N.1    Rulten, S.2    El-Khamisy, S.F.3    Caldecott, K.W.4
  • 22
    • 0037428228 scopus 로고    scopus 로고
    • DNA single-strand break repair and spinocerebellar ataxia
    • Caldecott, K. W. (2003) DNA single-strand break repair and spinocerebellar ataxia. Cell 112, 7-10
    • (2003) Cell , vol.112 , pp. 7-10
    • Caldecott, K.W.1
  • 25
    • 38049064044 scopus 로고    scopus 로고
    • Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint proteins
    • Ahel, I., Ahel, D., Matsusaka, T., Clark, A. J., Pines, J., Boulton, S. J., and West, S. C. (2008) Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint proteins. Nature 451, 81-85
    • (2008) Nature , vol.451 , pp. 81-85
    • Ahel, I.1    Ahel, D.2    Matsusaka, T.3    Clark, A.J.4    Pines, J.5    Boulton, S.J.6    West, S.C.7
  • 26
    • 47049104588 scopus 로고    scopus 로고
    • APLF (C2orf13) is a novel component of poly(ADP-ribose) signaling in mammalian cells
    • Rulten, S. L., Cortes-Ledesma, F., Guo, L., Iles, N. J., and Caldecott, K. W. (2008) APLF (C2orf13) is a novel component of poly(ADP-ribose) signaling in mammalian cells. Mol. Cell. Biol. 28, 4620-4628
    • (2008) Mol. Cell. Biol , vol.28 , pp. 4620-4628
    • Rulten, S.L.1    Cortes-Ledesma, F.2    Guo, L.3    Iles, N.J.4    Caldecott, K.W.5
  • 27
    • 77952716489 scopus 로고    scopus 로고
    • Structure and identification of ADP-ribose recognition motifs of APLF and role in the DNA damage response
    • Li, G. Y., McCulloch, R. D., Fenton, A. L., Cheung, M., Meng, L., Ikura, M., and Koch, C. A. (2010) Structure and identification of ADP-ribose recognition motifs of APLF and role in the DNA damage response. Proc. Natl. Acad. Sci. U.S.A. 107, 9129-9134
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 9129-9134
    • Li, G.Y.1    McCulloch, R.D.2    Fenton, A.L.3    Cheung, M.4    Meng, L.5    Ikura, M.6    Koch, C.A.7
  • 28
    • 0039115156 scopus 로고    scopus 로고
    • Transport into and out of the cell nucleus
    • Görlich, D. (1998) Transport into and out of the cell nucleus. EMBO J. 17, 2721-2727
    • (1998) EMBO J. , vol.17 , pp. 2721-2727
    • Görlich, D.1
  • 29
    • 68549085409 scopus 로고    scopus 로고
    • Importins and beyond: Non-conventional nuclear transport mechanisms
    • Wagstaff, K. M., and Jans, D. A. (2009) Importins and beyond: non-conventional nuclear transport mechanisms. Traffic 10, 1188-1198
    • (2009) Traffic , vol.10 , pp. 1188-1198
    • Wagstaff, K.M.1    Jans, D.A.2
  • 33
    • 0037102588 scopus 로고    scopus 로고
    • Ku heterodimer binds to both ends of the Werner protein and functional interaction occurs at the Werner N terminus
    • Karmakar, P., Snowden, C. M., Ramsden, D. A., and Bohr, V. A. (2002) Ku heterodimer binds to both ends of the Werner protein and functional interaction occurs at the Werner N terminus. Nucleic Acids Res. 30, 3583-3591
    • (2002) Nucleic Acids Res , vol.30 , pp. 3583-3591
    • Karmakar, P.1    Snowden, C.M.2    Ramsden, D.A.3    Bohr, V.A.4
  • 34
    • 79952573454 scopus 로고    scopus 로고
    • Functional significance of the interaction with Ku in DNA double-strand break recognition of XLF
    • Yano, K., Morotomi-Yano, K., Lee, K. J., and Chen, D. J. (2011) Functional significance of the interaction with Ku in DNA double-strand break recognition of XLF. FEBS Lett. 585, 841-846
    • (2011) FEBS Lett , vol.585 , pp. 841-846
    • Yano, K.1    Morotomi-Yano, K.2    Lee, K.J.3    Chen, D.J.4
  • 35
    • 4344649442 scopus 로고    scopus 로고
    • The Werner syndrome protein at the crossroads of DNA repair and apoptosis
    • Comai, L., and Li, B. (2004) The Werner syndrome protein at the crossroads of DNA repair and apoptosis. Mech. Ageing Dev. 125, 521-528
    • (2004) Mech. Ageing Dev , vol.125 , pp. 521-528
    • Comai, L.1    Li, B.2
  • 36
    • 0035312713 scopus 로고    scopus 로고
    • Different dynamics in nuclear entry of subunits of the repair/transcription factor TFIIH
    • Santagati, F., Botta, E., Stefanini, M., and Pedrini, A. M. (2001) Different dynamics in nuclear entry of subunits of the repair/transcription factor TFIIH. Nucleic Acids Res.29, 1574-1581
    • (2001) Nucleic Acids Res , vol.29 , pp. 1574-1581
    • Santagati, F.1    Botta, E.2    Stefanini, M.3    Pedrini, A.M.4
  • 37
    • 67349110815 scopus 로고    scopus 로고
    • Nuclear translocation contributes to regulation of DNA excision repair activities
    • Knudsen, N. Ø., Andersen, S. D., Lützen, A., Nielsen, F. C., and Rasmussen, L. J. (2009) Nuclear translocation contributes to regulation of DNA excision repair activities. DNA Repair 8, 682-689
    • (2009) DNA Repair , vol.8 , pp. 682-689
    • Knudsen N.Ø1    Andersen, S.D.2    Lützen, A.3    Nielsen, F.C.4    Rasmussen, L.J.5
  • 38
    • 33646117239 scopus 로고    scopus 로고
    • Spatial organization of the mammalian genome surveillance machinery in response to DNA strand breaks
    • Bekker-Jensen, S., Lukas, C., Kitagawa, R., Melander, F., Kastan, M. B., Bartek, J., and Lukas, J. (2006) Spatial organization of the mammalian genome surveillance machinery in response to DNA strand breaks. J. Cell Biol. 173, 195-206
    • (2006) J. Cell Biol , vol.173 , pp. 195-206
    • Bekker-Jensen, S.1    Lukas, C.2    Kitagawa, R.3    Melander, F.4    Kastan, M.B.5    Bartek, J.6    Lukas, J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.