메뉴 건너뛰기




Volumn 37, Issue 9, 2005, Pages 953-957

The BRIP1 helicase functions independently of BRCA1 in the Fanconi anemia pathway for DNA crosslink repair

Author keywords

[No Author keywords available]

Indexed keywords

BRCA1 PROTEIN; HELICASE; BRIP1 PROTEIN, HUMAN; CISPLATIN; CROSS LINKING REAGENT; DNA BINDING PROTEIN; FANCD2 PROTEIN, HUMAN; FANCONI ANEMIA GROUP D2 PROTEIN; MITOMYCIN; NUCLEAR PROTEIN; RNA HELICASE; SMALL INTERFERING RNA; UBIQUITIN;

EID: 25144503943     PISSN: 10614036     EISSN: 15461718     Source Type: Journal    
DOI: 10.1038/ng1627     Document Type: Article
Times cited : (172)

References (28)
  • 1
    • 20644461718 scopus 로고    scopus 로고
    • BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function
    • Cantor, S.B. et al. BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function. Cell 105, 149-160 (2001).
    • (2001) Cell , vol.105 , pp. 149-160
    • Cantor, S.B.1
  • 2
    • 0142147272 scopus 로고    scopus 로고
    • The BRCT domain is a phospho-protein binding domain
    • Yu, X., Chini, C.C., He, M., Mer, G. & Chen, J. The BRCT domain is a phospho-protein binding domain. Science 302, 639-642 (2003).
    • (2003) Science , vol.302 , pp. 639-642
    • Yu, X.1    Chini, C.C.2    He, M.3    Mer, G.4    Chen, J.5
  • 3
    • 1442281478 scopus 로고    scopus 로고
    • The BRCA1-associated protein BACH1 is a DNA helicase targeted by clinically relevant inactivating mutations
    • Cantor, S. et al. The BRCA1-associated protein BACH1 is a DNA helicase targeted by clinically relevant inactivating mutations. Proc. Natl. Acad. Sci. USA 101, 2357-2362 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2357-2362
    • Cantor, S.1
  • 4
    • 2542490186 scopus 로고    scopus 로고
    • Structural basis of phosphopeptide recognition by the BRCT domain of BRCA1
    • Williams, R.S., Lee, M.S., Hau, D.D. & Glover, J.N. Structural basis of phosphopeptide recognition by the BRCT domain of BRCA1. Nat. Struct. Mol. Biol. 11, 519-525 (2004).
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 519-525
    • Williams, R.S.1    Lee, M.S.2    Hau, D.D.3    Glover, J.N.4
  • 5
    • 2542489188 scopus 로고    scopus 로고
    • Structure and mechanism of BRCA1 BRCT domain recognition of phosphorylated BACH1 with implications for cancer
    • Clapperton, J.A. et al. Structure and mechanism of BRCA1 BRCT domain recognition of phosphorylated BACH1 with implications for cancer. Nat. Struct. Mol. Biol. 11, 512-518 (2004).
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 512-518
    • Clapperton, J.A.1
  • 6
    • 3142608985 scopus 로고    scopus 로고
    • Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains
    • Botuyan, M.V. et al. Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains. Structure (Camb.) 12, 1137-1146 (2004).
    • (2004) Structure (Camb.) , vol.12 , pp. 1137-1146
    • Botuyan, M.V.1
  • 7
    • 6344264992 scopus 로고    scopus 로고
    • DNA damage-induced cell cycle checkpoint control requires CtlP, a phosphorylation-dependent binding partner of BRCA1 C-terminal domains
    • Yu, X. & Chen, J. DNA damage-induced cell cycle checkpoint control requires CtlP, a phosphorylation-dependent binding partner of BRCA1 C-terminal domains. Mol. Cell. Biol. 24, 9478-9486 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 9478-9486
    • Yu, X.1    Chen, J.2
  • 8
    • 0142240342 scopus 로고    scopus 로고
    • BRCT repeats as phosphopeptide-binding modules involved in protein targeting
    • Manke, I.A., Lowery, D.M., Nguyen, A. & Yaffe, M.B. BRCT repeats as phosphopeptide-binding modules involved in protein targeting. Science 302, 636-639 (2003).
    • (2003) Science , vol.302 , pp. 636-639
    • Manke, I.A.1    Lowery, D.M.2    Nguyen, A.3    Yaffe, M.B.4
  • 9
    • 2342484423 scopus 로고    scopus 로고
    • Structure of the BRCT repeats of BRCA1 bound to a BACH1 phosphopeptide: Implications for signaling
    • Shiozaki, E.N., Gu, L., Yan, N. & Shi, Y. Structure of the BRCT repeats of BRCA1 bound to a BACH1 phosphopeptide: implications for signaling. Mol. Cell 14, 405-412 (2004).
    • (2004) Mol. Cell , vol.14 , pp. 405-412
    • Shiozaki, E.N.1    Gu, L.2    Yan, N.3    Shi, Y.4
  • 11
    • 0033569684 scopus 로고    scopus 로고
    • XRCC3 promotes homology-directed repair of DNA damage in mammalian cells
    • Pierce, A.J., Johnson, R.D., Thompson, L.H. & Jasin, M. XRCC3 promotes homology-directed repair of DNA damage in mammalian cells. Genes Dev. 13, 2633-2638 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 2633-2638
    • Pierce, A.J.1    Johnson, R.D.2    Thompson, L.H.3    Jasin, M.4
  • 12
    • 0036510163 scopus 로고    scopus 로고
    • BRCA1 regulates the G2/M checkpoint by activating Chk1 kinase upon DNA damage
    • Yarden, R.I., Pardo-Reoyo, S., Sgagias, M., Cowan, K.H. & Brody, L.C. BRCA1 regulates the G2/M checkpoint by activating Chk1 kinase upon DNA damage. Nat. Genet. 30, 285-289 (2002).
    • (2002) Nat. Genet. , vol.30 , pp. 285-289
    • Yarden, R.I.1    Pardo-Reoyo, S.2    Sgagias, M.3    Cowan, K.H.4    Brody, L.C.5
  • 13
    • 0035032649 scopus 로고    scopus 로고
    • Involvement of Brca1 in S-phase and G(2)-phase checkpoints after ionizing irradiation
    • Xu, B., Kim, S. & Kastan, M.B. Involvement of Brca1 in S-phase and G(2)-phase checkpoints after ionizing irradiation. Mol. Cell. Biol. 21, 3445-3450 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 3445-3450
    • Xu, B.1    Kim, S.2    Kastan, M.B.3
  • 14
    • 0019918242 scopus 로고
    • Cytogenetic toxicity of antitumor platinum compounds in Fanconi's anemia
    • Poll, E.H., Arwert, F., Joenje, H. & Eriksson, A.W. Cytogenetic toxicity of antitumor platinum compounds in Fanconi's anemia. Hum. Genet. 61, 228-230 (1982).
    • (1982) Hum. Genet. , vol.61 , pp. 228-230
    • Poll, E.H.1    Arwert, F.2    Joenje, H.3    Eriksson, A.W.4
  • 15
    • 0037388452 scopus 로고    scopus 로고
    • Rev1 is essential for DNA damage tolerance and non-templated immunoglobulin gene mutation in a vertebrate cell line
    • Simpson, L.J. & Sale, J.E. Rev1 is essential for DNA damage tolerance and non-templated immunoglobulin gene mutation in a vertebrate cell line. EMBO J. 22, 1654-1664 (2003).
    • (2003) EMBO J. , vol.22 , pp. 1654-1664
    • Simpson, L.J.1    Sale, J.E.2
  • 16
    • 0037107370 scopus 로고    scopus 로고
    • RAD18 and RAD54 cooperatively contribute to maintenance of genomic stability in vertebrate cells
    • Yamashita, Y.M. et al. RAD18 and RAD54 cooperatively contribute to maintenance of genomic stability in vertebrate cells. EMBO J. 21, 5558-5566 (2002).
    • (2002) EMBO J. , vol.21 , pp. 5558-5566
    • Yamashita, Y.M.1
  • 17
    • 0017118656 scopus 로고
    • Susceptibility of Fanconi's anaemia fibroblasts to chromosome damage by carcinogens
    • Auerbach, A.D. & Wolman, S.R. Susceptibility of Fanconi's anaemia fibroblasts to chromosome damage by carcinogens. Nature 261, 494-496 (1976).
    • (1976) Nature , vol.261 , pp. 494-496
    • Auerbach, A.D.1    Wolman, S.R.2
  • 18
    • 0020357892 scopus 로고
    • Susceptibility of Fanconi's anemia lymphoblasts to DNA-cross-linking and alkylating agents
    • Ishida, R. & Buchwald, M. Susceptibility of Fanconi's anemia lymphoblasts to DNA-cross-linking and alkylating agents. Cancer Res. 42, 4000-4006 (1982).
    • (1982) Cancer Res. , vol.42 , pp. 4000-4006
    • Ishida, R.1    Buchwald, M.2
  • 19
    • 0015891353 scopus 로고
    • A high susceptibility of Fanconi's anemia to chromosome breakage by DNA cross-linking agents
    • Sasaki, M.S. & Tonomura, A. A high susceptibility of Fanconi's anemia to chromosome breakage by DNA cross-linking agents. Cancer Res. 33, 1829-1836 (1973).
    • (1973) Cancer Res. , vol.33 , pp. 1829-1836
    • Sasaki, M.S.1    Tonomura, A.2
  • 20
    • 0035379611 scopus 로고    scopus 로고
    • The emerging genetic and molecular basis of Fanconi anaemia
    • Joenje, H. & Patel, K.J. The emerging genetic and molecular basis of Fanconi anaemia. Nat. Rev. Genet. 2, 446-457 (2001).
    • (2001) Nat. Rev. Genet. , vol.2 , pp. 446-457
    • Joenje, H.1    Patel, K.J.2
  • 21
    • 4344597147 scopus 로고    scopus 로고
    • The Fanconi anaemia gene FANCC promotes homologous recombination and error-prone DNA repair
    • Niedzwiedz, W. et al. The Fanconi anaemia gene FANCC promotes homologous recombination and error-prone DNA repair. Mol. Cell 15, 607-620 (2004).
    • (2004) Mol. Cell , vol.15 , pp. 607-620
    • Niedzwiedz, W.1
  • 22
    • 0019444973 scopus 로고
    • Oxygen-dependence of chromosomal aberrations in Fanconi's anaemia
    • Joenje, H., Arwert, F., Eriksson, A.W., de Koning, H. & Oostra, A.B. Oxygen-dependence of chromosomal aberrations in Fanconi's anaemia. Nature 290, 142-143 (1981).
    • (1981) Nature , vol.290 , pp. 142-143
    • Joenje, H.1    Arwert, F.2    Eriksson, A.W.3    De Koning, H.4    Oostra, A.B.5
  • 23
    • 0035105291 scopus 로고    scopus 로고
    • Interaction of the Fanconi anemia proteins and BRCA1 in a common pathway
    • Garcia-Higuera, I. et al. Interaction of the Fanconi anemia proteins and BRCA1 in a common pathway. Mol. Cell 7, 249-262 (2001).
    • (2001) Mol. Cell , vol.7 , pp. 249-262
    • Garcia-Higuera, I.1
  • 24
    • 12144288675 scopus 로고    scopus 로고
    • Heterogeneity in Fanconi anemia: Evidence for 2 new genetic subtypes
    • Levitus, M. et al. Heterogeneity in Fanconi anemia: evidence for 2 new genetic subtypes. Blood 103, 2498-2503 (2004).
    • (2004) Blood , vol.103 , pp. 2498-2503
    • Levitus, M.1
  • 25
    • 25144457604 scopus 로고    scopus 로고
    • The DNA helicase BRIP1 is defective in Fanconi anemia complementation group
    • advance online publication 21 August (doi:10.1038/ng1625.)
    • Levitus, M. et al. The DNA helicase BRIP1 is defective in Fanconi anemia complementation group J. Nat. Genet., advance online publication 21 August 2005 (doi:10.1038/ng1625).
    • (2005) J. Nat. Genet.
    • Levitus, M.1
  • 26
    • 0037137430 scopus 로고    scopus 로고
    • A comprehensive collection of chicken cDNAs
    • Boardman, P.E. et al. A comprehensive collection of chicken cDNAs. Curr. Biol. 12, 1965-1969 (2002).
    • (2002) Curr. Biol. , vol.12 , pp. 1965-1969
    • Boardman, P.E.1
  • 27
    • 3042559648 scopus 로고    scopus 로고
    • Mutant loxP vectors for selectable marker recycle and conditional knock-outs
    • Arakawa, H., Lodygin, D. & Buerstedde, J.M. Mutant loxP vectors for selectable marker recycle and conditional knock-outs. BMC Biotechnol. 1, 7 (2001).
    • (2001) BMC Biotechnol. , vol.1 , pp. 7
    • Arakawa, H.1    Lodygin, D.2    Buerstedde, J.M.3
  • 28
    • 0042671242 scopus 로고    scopus 로고
    • BRCA1-independent ubiquitination of FANCD2
    • Vandenberg, C.J. et al. BRCA1-independent ubiquitination of FANCD2. Mol. Cell 12, 247-254 (2003).
    • (2003) Mol. Cell , vol.12 , pp. 247-254
    • Vandenberg, C.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.