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Volumn 16, Issue 6, 2004, Pages 629-633

The DNA damage response: Sensing and signaling

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; ATM PROTEIN; ATR PROTEIN; DNA; PROTEIN KINASE; UNCLASSIFIED DRUG;

EID: 7744243520     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2004.09.005     Document Type: Review
Times cited : (166)

References (47)
  • 1
    • 0036531901 scopus 로고    scopus 로고
    • A unified view of the DNA-damage checkpoint
    • J. Melo, and D. Toczyski A unified view of the DNA-damage checkpoint Curr Opin Cell Biol 14 2002 237 245
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 237-245
    • Melo, J.1    Toczyski, D.2
  • 2
    • 0036906303 scopus 로고    scopus 로고
    • Checkpoint signalling: Focusing on 53BP1
    • R.T. Abraham Checkpoint signalling: focusing on 53BP1 Nat Cell Biol 4 2002 E277 E279
    • (2002) Nat Cell Biol , vol.4
    • Abraham, R.T.1
  • 3
    • 0038613469 scopus 로고    scopus 로고
    • Checkpoint mediators: Relaying signals from DNA strand breaks
    • C.E. Canman Checkpoint mediators: relaying signals from DNA strand breaks Curr Biol 13 2003 R488 R490
    • (2003) Curr Biol , vol.13
    • Canman, C.E.1
  • 4
    • 0035449355 scopus 로고    scopus 로고
    • Cell cycle checkpoint signaling through the ATM and ATR kinases
    • R.T. Abraham Cell cycle checkpoint signaling through the ATM and ATR kinases Genes Dev 15 2001 2177 2196
    • (2001) Genes Dev , vol.15 , pp. 2177-2196
    • Abraham, R.T.1
  • 5
    • 0842287638 scopus 로고    scopus 로고
    • DNA damage tumor suppressor genes and genomic instability
    • N. Motoyama, and K. Naka DNA damage tumor suppressor genes and genomic instability Curr Opin Genet Dev 14 2004 11 16
    • (2004) Curr Opin Genet Dev , vol.14 , pp. 11-16
    • Motoyama, N.1    Naka, K.2
  • 6
    • 0037472924 scopus 로고    scopus 로고
    • DNA damage activates ATM through intermolecular autophosphorylation and dimer dissociation
    • C.J. Bakkenist, and M.B. Kastan DNA damage activates ATM through intermolecular autophosphorylation and dimer dissociation Nature 421 2003 499 506 This study shows that in unchallenged cells ATM exists as an inactive dimer. The presence of a very small number of double-strand breaks or global alterations in chromatin structure induces ATM autophosphorylation on serine 1981. Autophosphorylation triggers dissociation of the dimer and allows active monomers to phosphorylate other substrates.
    • (2003) Nature , vol.421 , pp. 499-506
    • Bakkenist, C.J.1    Kastan, M.B.2
  • 7
    • 1642499359 scopus 로고    scopus 로고
    • Quaternary structure of ATR and effects of ATRIP and replication protein a on its DNA binding and kinase activities
    • K. Unsal-Kacmaz, and A. Sancar Quaternary structure of ATR and effects of ATRIP and replication protein A on its DNA binding and kinase activities Mol Cell Biol 24 2004 1292 1300
    • (2004) Mol Cell Biol , vol.24 , pp. 1292-1300
    • Unsal-Kacmaz, K.1    Sancar, A.2
  • 9
    • 0037341599 scopus 로고    scopus 로고
    • Distinct spatiotemporal dynamics of mammalian checkpoint regulators induced by DNA damage
    • C. Lukas, J. Falck, J. Bartkova, J. Bartek, and J. Lukas Distinct spatiotemporal dynamics of mammalian checkpoint regulators induced by DNA damage Nat Cell Biol 5 2003 255 260
    • (2003) Nat Cell Biol , vol.5 , pp. 255-260
    • Lukas, C.1    Falck, J.2    Bartkova, J.3    Bartek, J.4    Lukas, J.5
  • 10
    • 2942687831 scopus 로고    scopus 로고
    • Phosphorylation of SMC1 is a critical downstream event in the ATM-NBS1-BRCA1 pathway
    • R. Kitagawa, C.J. Bakkenist, P.J. McKinnon, and M.B. Kastan Phosphorylation of SMC1 is a critical downstream event in the ATM-NBS1-BRCA1 pathway Genes Dev 18 2004 1423 1438
    • (2004) Genes Dev , vol.18 , pp. 1423-1438
    • Kitagawa, R.1    Bakkenist, C.J.2    McKinnon, P.J.3    Kastan, M.B.4
  • 12
    • 0032721091 scopus 로고    scopus 로고
    • The Mre11-Rad50-Xrs2 protein complex facilitates homologous recombination-based double-strand break repair in Saccharomyces cerevisiae
    • D.A. Bressan, B.K. Baxter, and J.H. Petrini The Mre11-Rad50-Xrs2 protein complex facilitates homologous recombination-based double-strand break repair in Saccharomyces cerevisiae Mol Cell Biol 19 1999 7681 7687
    • (1999) Mol Cell Biol , vol.19 , pp. 7681-7687
    • Bressan, D.A.1    Baxter, B.K.2    Petrini, J.H.3
  • 13
    • 0142011461 scopus 로고    scopus 로고
    • The cellular response to DNA double-strand breaks: Defining the sensors and mediators
    • J.H. Petrini, and T.H. Stracker The cellular response to DNA double-strand breaks: defining the sensors and mediators Trends Cell Biol 13 2003 458 462
    • (2003) Trends Cell Biol , vol.13 , pp. 458-462
    • Petrini, J.H.1    Stracker, T.H.2
  • 18
    • 0034749425 scopus 로고    scopus 로고
    • DNA damage-dependent nuclear dynamics of the Mre11 complex
    • O.K. Mirzoeva, and J.H. Petrini DNA damage-dependent nuclear dynamics of the Mre11 complex Mol Cell Biol 21 2001 281 288
    • (2001) Mol Cell Biol , vol.21 , pp. 281-288
    • Mirzoeva, O.K.1    Petrini, J.H.2
  • 20
    • 2442444916 scopus 로고    scopus 로고
    • Distinct functional domains of Nbs1 modulate the timing and magnitude of ATM activation after low doses of ionizing radiation
    • Z. Horejsi, J. Falck, C.J. Bakkenist, M.B. Kastan, J. Lukas, and J. Bartek Distinct functional domains of Nbs1 modulate the timing and magnitude of ATM activation after low doses of ionizing radiation Oncogene 23 2004 3122 3127
    • (2004) Oncogene , vol.23 , pp. 3122-3127
    • Horejsi, Z.1    Falck, J.2    Bakkenist, C.J.3    Kastan, M.B.4    Lukas, J.5    Bartek, J.6
  • 22
    • 0036276388 scopus 로고    scopus 로고
    • The Mre11 complex: At the crossroads of DNA repair and checkpoint signalling
    • D. D'Amours, and S.P. Jackson The Mre11 complex: at the crossroads of DNA repair and checkpoint signalling Nat Rev Mol Cell Biol 3 2002 317 327
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 317-327
    • D'Amours, D.1    Jackson, S.P.2
  • 23
    • 0035941021 scopus 로고    scopus 로고
    • ATR and ATRIP: Partners in checkpoint signaling
    • D. Cortez, S. Guntuku, J. Qin, and S.J. Elledge ATR and ATRIP: partners in checkpoint signaling Science 294 2001 1713 1716
    • (2001) Science , vol.294 , pp. 1713-1716
    • Cortez, D.1    Guntuku, S.2    Qin, J.3    Elledge, S.J.4
  • 24
    • 0037567268 scopus 로고    scopus 로고
    • Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes
    • L. Zou, and S.J. Elledge Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes Science 300 2003 1542 1548 This work provides evidence of a very simple and conserved mechanism by which a normal intermediate of DNA replication, recombination and repair, ssDNA, contributes to the ATR checkpoint activation. By recruiting kinases and substrates to ssDNA, RPA could activate the checkpoint without altering the specific activity of ATR.
    • (2003) Science , vol.300 , pp. 1542-1548
    • Zou, L.1    Elledge, S.J.2
  • 25
    • 3242670803 scopus 로고    scopus 로고
    • ATR and ATM regulate the timing of DNA replication origin firing
    • D. Shechter, V. Costanzo, and J. Gautier ATR and ATM regulate the timing of DNA replication origin firing Nat Cell Biol 6 2004 648 655
    • (2004) Nat Cell Biol , vol.6 , pp. 648-655
    • Shechter, D.1    Costanzo, V.2    Gautier, J.3
  • 26
    • 3242887431 scopus 로고    scopus 로고
    • Dial 9-1-1 for DNA damage: The Rad9-Hus1-Rad1 (9-1-1) clamp complex
    • E.R. Parrilla-Castellar, S.J. Arlander, and L. Karnitz Dial 9-1-1 for DNA damage: the Rad9-Hus1-Rad1 (9-1-1) clamp complex DNA Repair (Amst) 3 2004 1009 1014
    • (2004) DNA Repair (Amst) , vol.3 , pp. 1009-1014
    • Parrilla-Castellar, E.R.1    Arlander, S.J.2    Karnitz, L.3
  • 27
    • 0037224965 scopus 로고    scopus 로고
    • Checkpoint activation regulates mutagenic translesion synthesis
    • M. Kai, and T.S. Wang Checkpoint activation regulates mutagenic translesion synthesis Genes Dev 17 2003 64 76
    • (2003) Genes Dev , vol.17 , pp. 64-76
    • Kai, M.1    Wang, T.S.2
  • 28
    • 0037039165 scopus 로고    scopus 로고
    • Hus1 acts upstream of chk1 in a mammalian DNA damage response pathway
    • R.S. Weiss, S. Matsuoka, S.J. Elledge, and P. Leder Hus1 acts upstream of chk1 in a mammalian DNA damage response pathway Curr Biol 12 2002 73 77
    • (2002) Curr Biol , vol.12 , pp. 73-77
    • Weiss, R.S.1    Matsuoka, S.2    Elledge, S.J.3    Leder, P.4
  • 29
    • 0037080675 scopus 로고    scopus 로고
    • Regulation of ATR substrate selection by Rad17-dependent loading of Rad9 complexes onto chromatin
    • L. Zou, D. Cortez, and S.J. Elledge Regulation of ATR substrate selection by Rad17-dependent loading of Rad9 complexes onto chromatin Genes Dev 16 2002 198 208
    • (2002) Genes Dev , vol.16 , pp. 198-208
    • Zou, L.1    Cortez, D.2    Elledge, S.J.3
  • 30
    • 4243156107 scopus 로고    scopus 로고
    • Biochemical characterization of DNA damage checkpoint complexes: Clamp loader and clamp complexes with specificity for 5′ recessed DNA
    • V. Ellison, and B. Stillman Biochemical characterization of DNA damage checkpoint complexes: clamp loader and clamp complexes with specificity for 5′ recessed DNA PLoS Biol 1 2003 E33
    • (2003) PLoS Biol , vol.1
    • Ellison, V.1    Stillman, B.2
  • 32
    • 0142240342 scopus 로고    scopus 로고
    • BRCT repeats as phosphopeptide-binding modules involved in protein targeting
    • ••] took different approaches to demonstrate that BRCT domains are phospho-specific binding modules and that their function within the DNA damage depends on their ability to facilitate regulated protein-protein interactions.
    • (2003) Science , vol.302 , pp. 636-639
    • Manke, I.A.1    Lowery, D.M.2    Nguyen, A.3    Yaffe, M.B.4
  • 33
    • 3042793923 scopus 로고    scopus 로고
    • Histone H2A phosphorylation controls Crb2 recruitment at DNA breaks, maintains checkpoint arrest, and influences DNA repair in fission yeast
    • T.M. Nakamura, L.L. Du, C. Redon, and P. Russell Histone H2A phosphorylation controls Crb2 recruitment at DNA breaks, maintains checkpoint arrest, and influences DNA repair in fission yeast Mol Cell Biol 24 2004 6215 6230
    • (2004) Mol Cell Biol , vol.24 , pp. 6215-6230
    • Nakamura, T.M.1    Du, L.L.2    Redon, C.3    Russell, P.4
  • 35
    • 0038143321 scopus 로고    scopus 로고
    • Accumulation of checkpoint protein 53BP1 at DNA breaks involves its binding to phosphorylated histone H2AX
    • I.M. Ward, K. Minn, K.G. Jorda, and J. Chen Accumulation of checkpoint protein 53BP1 at DNA breaks involves its binding to phosphorylated histone H2AX J Biol Chem 278 2003 19579 19582
    • (2003) J Biol Chem , vol.278 , pp. 19579-19582
    • Ward, I.M.1    Minn, K.2    Jorda, K.G.3    Chen, J.4
  • 36
    • 0034700511 scopus 로고    scopus 로고
    • A role for Saccharomyces cerevisiae histone H2A in DNA repair
    • J.A. Downs, N.F. Lowndes, and S.P. Jackson A role for Saccharomyces cerevisiae histone H2A in DNA repair Nature 408 2000 1001 1004
    • (2000) Nature , vol.408 , pp. 1001-1004
    • Downs, J.A.1    Lowndes, N.F.2    Jackson, S.P.3
  • 38
    • 0038506000 scopus 로고    scopus 로고
    • Mrc1 is a replication fork component whose phosphorylation in response to DNA replication stress activates Rad53
    • A.J. Osborn, and S.J. Elledge Mrc1 is a replication fork component whose phosphorylation in response to DNA replication stress activates Rad53 Genes Dev 17 2003 1755 1767
    • (2003) Genes Dev , vol.17 , pp. 1755-1767
    • Osborn, A.J.1    Elledge, S.J.2
  • 39
    • 0042865938 scopus 로고    scopus 로고
    • S-phase checkpoint proteins Tof1 and Mrc1 form a stable replication-pausing complex
    • Y. Katou, Y. Kanoh, M. Bando, H. Noguchi, H. Tanaka, T. Ashikari, K. Sugimoto, and K. Shirahige S-phase checkpoint proteins Tof1 and Mrc1 form a stable replication-pausing complex Nature 424 2003 1078 1083 These authors made use of chromatin immunoprecipitation to show that the checkpoint mediator proteins Mrc1 and Tof1, but not the checkpoint kinase Rad53, are required to maintain stable replication complexes at replication forks.
    • (2003) Nature , vol.424 , pp. 1078-1083
    • Katou, Y.1    Kanoh, Y.2    Bando, M.3    Noguchi, H.4    Tanaka, H.5    Ashikari, T.6    Sugimoto, K.7    Shirahige, K.8
  • 40
    • 0037291130 scopus 로고    scopus 로고
    • Claspin, a Chk1-regulatory protein, monitors DNA replication on chromatin independently of RPA, ATR, and Rad17
    • J. Lee, A. Kumagai, and W.G. Dunphy Claspin, a Chk1-regulatory protein, monitors DNA replication on chromatin independently of RPA, ATR, and Rad17 Mol Cell 11 2003 329 340
    • (2003) Mol Cell , vol.11 , pp. 329-340
    • Lee, J.1    Kumagai, A.2    Dunphy, W.G.3
  • 41
    • 0242579867 scopus 로고    scopus 로고
    • Replication checkpoint protein Mrc1 is regulated by Rad3 and Tel1 in fission yeast
    • H. Zhao, K. Tanaka, E. Nogochi, C. Nogochi, and P. Russell Replication checkpoint protein Mrc1 is regulated by Rad3 and Tel1 in fission yeast Mol Cell Biol 23 2003 8395 8403
    • (2003) Mol Cell Biol , vol.23 , pp. 8395-8403
    • Zhao, H.1    Tanaka, K.2    Nogochi, E.3    Nogochi, C.4    Russell, P.5
  • 42
    • 0031034628 scopus 로고    scopus 로고
    • Cdc2 tyrosine phosphorylation is required for the DNA damage checkpoint in fission yeast
    • N. Rhind, B. Furnari, and P. Russell Cdc2 tyrosine phosphorylation is required for the DNA damage checkpoint in fission yeast Genes Dev 11 1997 504 511
    • (1997) Genes Dev , vol.11 , pp. 504-511
    • Rhind, N.1    Furnari, B.2    Russell, P.3
  • 43
    • 0031835956 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of Cdc2 required for the replication checkpoint in Schizosaccharomyces pombe
    • N. Rhind, and P. Russell Tyrosine phosphorylation of Cdc2 required for the replication checkpoint in Schizosaccharomyces pombe Mol Cel Biol 18 1998 3782 3787
    • (1998) Mol Cel Biol , vol.18 , pp. 3782-3787
    • Rhind, N.1    Russell, P.2
  • 44
    • 4444268809 scopus 로고    scopus 로고
    • Chk1, but not Chk2, inhibits Cdc25 phosphatases by a novel common mechanism
    • K. Uto, D. Inoue, K. Shimuta, N. Nakajo, and N. Sagata Chk1, but not Chk2, inhibits Cdc25 phosphatases by a novel common mechanism EMBO J 23 2004 3386 3396 This study shows that Chk1, but not Chk2, phosphorylates Xenopus Cdc25A at a C-terminal site (threonine-504) and inhibits it from interacting with CDK-cyclin complexes in vitro. Neither degradation of Cdc25A nor interaction with 14-3-3 proteins at the threonine-504 site, are required for the checkpoint regulation of Cdc25A by Chk1.
    • (2004) EMBO J , vol.23 , pp. 3386-3396
    • Uto, K.1    Inoue, D.2    Shimuta, K.3    Nakajo, N.4    Sagata, N.5
  • 45
    • 0142027900 scopus 로고    scopus 로고
    • Chk1 kinase negatively regulates mitotic function of Cdc25A phosphatase through 14-3-3 binding
    • M.S. Chen, C.E. Ryan, and H. Piwnica-Worms Chk1 kinase negatively regulates mitotic function of Cdc25A phosphatase through 14-3-3 binding Mol Cell Biol 23 2003 7488 7497
    • (2003) Mol Cell Biol , vol.23 , pp. 7488-7497
    • Chen, M.S.1    Ryan, C.E.2    Piwnica-Worms, H.3
  • 47
    • 0035182579 scopus 로고    scopus 로고
    • Nuclear exclusion of Cdc25 is not required for DNA damage checkpoint in fission yeast
    • A. Lopez-Girona, J. Kanoh, and P. Russell Nuclear exclusion of Cdc25 is not required for DNA damage checkpoint in fission yeast Curr Biol 11 2001 50 54
    • (2001) Curr Biol , vol.11 , pp. 50-54
    • Lopez-Girona, A.1    Kanoh, J.2    Russell, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.