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Volumn 312, Issue 4, 2006, Pages 488-499

Involvement of the ubiquitin pathway in decreasing Ku70 levels in response to drug-induced apoptosis

Author keywords

Apoptosis; Bax; DNA PK; Ku70; Ku80; Ubiquitination

Indexed keywords

KU ANTIGEN; UBIQUITIN;

EID: 29144533365     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2005.11.016     Document Type: Article
Times cited : (26)

References (49)
  • 1
    • 0842281645 scopus 로고    scopus 로고
    • Cell death: Critical control points
    • N.N. Danial, and S.J. Korsmeyer Cell death: critical control points Cell 116 2004 205 219
    • (2004) Cell , vol.116 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 2
    • 0033302523 scopus 로고    scopus 로고
    • Programmed cell death and the regulation of homeostasis
    • S.J. Korsmeyer Programmed cell death and the regulation of homeostasis Harvey Lect. 95 1999 21 41
    • (1999) Harvey Lect. , vol.95 , pp. 21-41
    • Korsmeyer, S.J.1
  • 4
    • 14144251559 scopus 로고    scopus 로고
    • Apoptosis mechanisms: Implications for cancer drug discovery
    • J.C. Reed Apoptosis mechanisms: implications for cancer drug discovery Oncology (Huntingt.) 18 2004 11 20
    • (2004) Oncology (Huntingt.) , vol.18 , pp. 11-20
    • Reed, J.C.1
  • 5
    • 19244365798 scopus 로고    scopus 로고
    • The domains of apoptosis: A genomics perspective
    • J.C. Reed, K.S. Doctor, and A. Godzik The domains of apoptosis: a genomics perspective Sci. STKE 2004 2004 re9
    • (2004) Sci. STKE , vol.2004 , pp. 9
    • Reed, J.C.1    Doctor, K.S.2    Godzik, A.3
  • 6
    • 0030979773 scopus 로고    scopus 로고
    • Double identity for proteins of the Bcl-2 family
    • J.C. Reed Double identity for proteins of the Bcl-2 family Nature 387 1997 773 776
    • (1997) Nature , vol.387 , pp. 773-776
    • Reed, J.C.1
  • 7
    • 0033179760 scopus 로고    scopus 로고
    • BCL-2 family members and the mitochondria in apoptosis
    • A. Gross, J.M. McDonnell, and S.J. Korsmeyer BCL-2 family members and the mitochondria in apoptosis Genes Dev. 13 1999 1899 1911
    • (1999) Genes Dev. , vol.13 , pp. 1899-1911
    • Gross, A.1    McDonnell, J.M.2    Korsmeyer, S.J.3
  • 8
    • 0034786019 scopus 로고    scopus 로고
    • BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis
    • E.H. Cheng, M.C. Wei, S. Weiler, R.A. Flavell, T.W. Mak, T. Lindsten, and S.J. Korsmeyer BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis Mol. Cell 8 2001 705 711
    • (2001) Mol. Cell , vol.8 , pp. 705-711
    • Cheng, E.H.1    Wei, M.C.2    Weiler, S.3    Flavell, R.A.4    Mak, T.W.5    Lindsten, T.6    Korsmeyer, S.J.7
  • 10
    • 11444270251 scopus 로고    scopus 로고
    • Apoptosis: A mitochondrial perspective on cell death
    • N.C. Mishra, and S. Kumar Apoptosis: a mitochondrial perspective on cell death Indian J. Exp. Biol. 43 2005 25 34
    • (2005) Indian J. Exp. Biol. , vol.43 , pp. 25-34
    • Mishra, N.C.1    Kumar, S.2
  • 11
    • 0037427412 scopus 로고    scopus 로고
    • Mechanisms of cytochrome c release by proapoptotic BCL-2 family members
    • L. Scorrano, and S.J. Korsmeyer Mechanisms of cytochrome c release by proapoptotic BCL-2 family members Biochem. Biophys. Res. Commun. 304 2003 437 444
    • (2003) Biochem. Biophys. Res. Commun. , vol.304 , pp. 437-444
    • Scorrano, L.1    Korsmeyer, S.J.2
  • 12
    • 0035856495 scopus 로고    scopus 로고
    • DNA repair: How Ku makes ends meet
    • A.J. Doherty, and S.P. Jackson DNA repair: how Ku makes ends meet Curr. Biol. 11 2001 R920 R924
    • (2001) Curr. Biol. , vol.11
    • Doherty, A.J.1    Jackson, S.P.2
  • 13
    • 0027397867 scopus 로고
    • The DNA-dependent protein kinase: Requirement for DNA ends and association with Ku antigen
    • T.M. Gottlieb, and S.P. Jackson The DNA-dependent protein kinase: requirement for DNA ends and association with Ku antigen Cell 72 1993 131 142
    • (1993) Cell , vol.72 , pp. 131-142
    • Gottlieb, T.M.1    Jackson, S.P.2
  • 14
    • 0035313706 scopus 로고    scopus 로고
    • DNA-PK, ATM and ATR as sensors of DNA damage: Variations on a theme?
    • D. Durocher, and S.P. Jackson DNA-PK, ATM and ATR as sensors of DNA damage: variations on a theme? Curr. Opin. Cell Biol. 13 2001 225 231
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 225-231
    • Durocher, D.1    Jackson, S.P.2
  • 15
    • 0029884756 scopus 로고    scopus 로고
    • Intracellular redistribution of Ku immunoreactivity in response to cell-cell contact and growth modulating components in the medium
    • J.W. Fewell, and E.L. Kuff Intracellular redistribution of Ku immunoreactivity in response to cell-cell contact and growth modulating components in the medium J. Cell Sci. 109 Pt. 7 1996 1937 1946
    • (1996) J. Cell Sci. , vol.109 , Issue.PART 7 , pp. 1937-1946
    • Fewell, J.W.1    Kuff, E.L.2
  • 16
    • 0032573467 scopus 로고    scopus 로고
    • Subcellular localization and protein-protein interaction regions of Ku proteins
    • M. Koike, T. Miyasaka, T. Mimori, and T. Shiomi Subcellular localization and protein-protein interaction regions of Ku proteins Biochem. Biophys. Res. Commun. 252 1998 679 685
    • (1998) Biochem. Biophys. Res. Commun. , vol.252 , pp. 679-685
    • Koike, M.1    Miyasaka, T.2    Mimori, T.3    Shiomi, T.4
  • 17
    • 0035815607 scopus 로고    scopus 로고
    • Dimerization and nuclear localization of ku proteins
    • M. Koike, T. Shiomi, and A. Koike Dimerization and nuclear localization of ku proteins J. Biol. Chem. 276 2001 11167 11173
    • (2001) J. Biol. Chem. , vol.276 , pp. 11167-11173
    • Koike, M.1    Shiomi, T.2    Koike, A.3
  • 18
    • 6344261567 scopus 로고    scopus 로고
    • The membrane form of the DNA repair protein Ku interacts at the cell surface with metalloproteinase 9
    • S. Monferran, J. Paupert, S. Dauvillier, B. Salles, and C. Muller The membrane form of the DNA repair protein Ku interacts at the cell surface with metalloproteinase 9 EMBO J. 23 2004 3758 3768
    • (2004) EMBO J. , vol.23 , pp. 3758-3768
    • Monferran, S.1    Paupert, J.2    Dauvillier, S.3    Salles, B.4    Muller, C.5
  • 20
    • 0035833552 scopus 로고    scopus 로고
    • Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair
    • J.R. Walker, R.A. Corpina, and J. Goldberg Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair Nature 412 2001 607 614
    • (2001) Nature , vol.412 , pp. 607-614
    • Walker, J.R.1    Corpina, R.A.2    Goldberg, J.3
  • 21
    • 0037386258 scopus 로고    scopus 로고
    • Cytoprotective membrane-permeable peptides designed from the Bax-binding domain of Ku70
    • M. Sawada, P. Hayes, and S. Matsuyama Cytoprotective membrane-permeable peptides designed from the Bax-binding domain of Ku70 Nat. Cell Biol. 5 2003 352 357
    • (2003) Nat. Cell Biol. , vol.5 , pp. 352-357
    • Sawada, M.1    Hayes, P.2    Matsuyama, S.3
  • 24
    • 8644286794 scopus 로고    scopus 로고
    • The role of Bax-inhibiting peptide in retinal ganglion cell apoptosis after optic nerve transection
    • Q. Qin, K. Patil, and S.C. Sharma The role of Bax-inhibiting peptide in retinal ganglion cell apoptosis after optic nerve transection Neurosci. Lett. 372 2004 17 21
    • (2004) Neurosci. Lett. , vol.372 , pp. 17-21
    • Qin, Q.1    Patil, K.2    Sharma, S.C.3
  • 25
    • 0022379602 scopus 로고
    • The immunochemical detection and quantitation of intracellular ubiquitin-protein conjugates
    • A.L. Haas, and P.M. Bright The immunochemical detection and quantitation of intracellular ubiquitin-protein conjugates J. Biol. Chem. 260 1985 12464 12473
    • (1985) J. Biol. Chem. , vol.260 , pp. 12464-12473
    • Haas, A.L.1    Bright, P.M.2
  • 26
    • 0042744088 scopus 로고    scopus 로고
    • Transforming growth factor-beta inhibition of proteasomal activity: A potential mechanism of growth arrest
    • L. Tadlock, Y. Yamagiwa, J. Hawker, C. Marienfeld, and T. Patel Transforming growth factor-beta inhibition of proteasomal activity: a potential mechanism of growth arrest Am. J. Physiol.: Cell Physiol. 285 2003 C277 C285
    • (2003) Am. J. Physiol.: Cell Physiol. , vol.285
    • Tadlock, L.1    Yamagiwa, Y.2    Hawker, J.3    Marienfeld, C.4    Patel, T.5
  • 28
    • 0942277026 scopus 로고    scopus 로고
    • The use of housekeeping genes (HKG) as an internal control for the detection of gene expression by quantitative real-time RT-PCR
    • V. Ullmannova, and C. Haskovec The use of housekeeping genes (HKG) as an internal control for the detection of gene expression by quantitative real-time RT-PCR Folia Biol. (Praha) 49 2003 211 216
    • (2003) Folia Biol. (Praha) , vol.49 , pp. 211-216
    • Ullmannova, V.1    Haskovec, C.2
  • 29
    • 0042062320 scopus 로고    scopus 로고
    • Relationship between cyclin D1 and p21(Waf1/Cip1) during differentiation of human myeloid leukemia cell lines
    • V. Ullmannova, P. Stockbauer, M. Hradcova, J. Soucek, and C. Haskovec Relationship between cyclin D1 and p21(Waf1/Cip1) during differentiation of human myeloid leukemia cell lines Leuk. Res. 27 2003 1115 1123
    • (2003) Leuk. Res. , vol.27 , pp. 1115-1123
    • Ullmannova, V.1    Stockbauer, P.2    Hradcova, M.3    Soucek, J.4    Haskovec, C.5
  • 30
    • 1642569566 scopus 로고    scopus 로고
    • Quantitative analysis of nucleic acids-The last few years of progress
    • C. Ding, and C.R. Cantor Quantitative analysis of nucleic acids-The last few years of progress J. Biochem. Mol. Biol. 37 2004 1 10
    • (2004) J. Biochem. Mol. Biol. , vol.37 , pp. 1-10
    • Ding, C.1    Cantor, C.R.2
  • 31
    • 0035292759 scopus 로고    scopus 로고
    • Themes and variations on ubiquitylation
    • A.M. Weissman Themes and variations on ubiquitylation Nat. Rev., Mol. Cell Biol. 2 2001 169 178
    • (2001) Nat. Rev., Mol. Cell Biol. , vol.2 , pp. 169-178
    • Weissman, A.M.1
  • 32
    • 0030737501 scopus 로고    scopus 로고
    • Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation
    • C.S. Arendt, and M. Hochstrasser Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation Proc. Natl. Acad. Sci. U. S. A. 94 1997 7156 7161
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 7156-7161
    • Arendt, C.S.1    Hochstrasser, M.2
  • 33
    • 0033197542 scopus 로고    scopus 로고
    • Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown
    • A.F. Kisselev, T.N. Akopian, V. Castillo, and A.L. Goldberg Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown Mol. Cell 4 1999 395 402
    • (1999) Mol. Cell , vol.4 , pp. 395-402
    • Kisselev, A.F.1    Akopian, T.N.2    Castillo, V.3    Goldberg, A.L.4
  • 35
    • 0030858967 scopus 로고    scopus 로고
    • Ku70-deficient embryonic stem cells have increased ionizing radiosensitivity, defective DNA end-binding activity, and inability to support V(D)J recombination
    • Y. Gu, S. Jin, Y. Gao, D.T. Weaver, and F.W. Alt Ku70-deficient embryonic stem cells have increased ionizing radiosensitivity, defective DNA end-binding activity, and inability to support V(D)J recombination Proc. Natl. Acad. Sci. U. S. A. 94 1997 8076 8081
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 8076-8081
    • Gu, Y.1    Jin, S.2    Gao, Y.3    Weaver, D.T.4    Alt, F.W.5
  • 36
    • 0038046166 scopus 로고    scopus 로고
    • Elimination of Mcl-1 is required for the initiation of apoptosis following ultraviolet irradiation
    • D. Nijhawan, M. Fang, E. Traer, Q. Zhong, W. Gao, F. Du, and X. Wang Elimination of Mcl-1 is required for the initiation of apoptosis following ultraviolet irradiation Genes Dev. 17 2003 1475 1486
    • (2003) Genes Dev. , vol.17 , pp. 1475-1486
    • Nijhawan, D.1    Fang, M.2    Traer, E.3    Zhong, Q.4    Gao, W.5    Du, F.6    Wang, X.7
  • 39
    • 0037377060 scopus 로고    scopus 로고
    • Ubiquitination, phosphorylation and acetylation: The molecular basis for p53 regulation
    • C.L. Brooks, and W. Gu Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation Curr. Opin. Cell Biol. 15 2003 164 171
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 164-171
    • Brooks, C.L.1    Gu, W.2
  • 40
    • 23644436275 scopus 로고    scopus 로고
    • Histone modifications as key regulators of transcription
    • A.U. Khan, and S. Krishnamurthy Histone modifications as key regulators of transcription Front. Biosci. 10 2005 866 872
    • (2005) Front. Biosci. , vol.10 , pp. 866-872
    • Khan, A.U.1    Krishnamurthy, S.2
  • 41
    • 4344601100 scopus 로고    scopus 로고
    • YY1 inhibits the activation of the p53 tumor suppressor in response to genotoxic stress
    • E. Gronroos, A.A. Terentiev, T. Punga, and J. Ericsson YY1 inhibits the activation of the p53 tumor suppressor in response to genotoxic stress Proc. Natl. Acad. Sci. U. S. A. 101 2004 12165 12170
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 12165-12170
    • Gronroos, E.1    Terentiev, A.A.2    Punga, T.3    Ericsson, J.4
  • 43
    • 0028819412 scopus 로고
    • Role of free p70 (Ku) subunit in posttranslational stabilization of newly synthesized p80 during DNA-dependent protein kinase assembly
    • M. Satoh, J. Wang, and W.H. Reeves Role of free p70 (Ku) subunit in posttranslational stabilization of newly synthesized p80 during DNA-dependent protein kinase assembly Eur. J. Cell Biol. 66 1995 127 135
    • (1995) Eur. J. Cell Biol. , vol.66 , pp. 127-135
    • Satoh, M.1    Wang, J.2    Reeves, W.H.3
  • 44
    • 0030746109 scopus 로고    scopus 로고
    • Interaction of DNA-dependent protein kinase with DNA and with Ku: Biochemical and atomic-force microscopy studies
    • M. Yaneva, T. Kowalewski, and M.R. Lieber Interaction of DNA-dependent protein kinase with DNA and with Ku: biochemical and atomic-force microscopy studies EMBO J. 16 1997 5098 5112
    • (1997) EMBO J. , vol.16 , pp. 5098-5112
    • Yaneva, M.1    Kowalewski, T.2    Lieber, M.R.3
  • 45
    • 0032972734 scopus 로고    scopus 로고
    • DNA-dependent protein kinase phosphorylation sites in Ku 70/80 heterodimer
    • D.W. Chan, R. Ye, C.J. Veillette, and S.P. Lees-Miller DNA-dependent protein kinase phosphorylation sites in Ku 70/80 heterodimer Biochemistry 38 1999 1819 1828
    • (1999) Biochemistry , vol.38 , pp. 1819-1828
    • Chan, D.W.1    Ye, R.2    Veillette, C.J.3    Lees-Miller, S.P.4
  • 46
    • 0842303313 scopus 로고    scopus 로고
    • Back to the future with ubiquitin
    • C.M. Pickart Back to the future with ubiquitin Cell 116 2004 181 190
    • (2004) Cell , vol.116 , pp. 181-190
    • Pickart, C.M.1
  • 47
    • 0141442586 scopus 로고    scopus 로고
    • Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins
    • L. Hicke, and R. Dunn Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins Annu. Rev. Cell Dev. Biol. 19 2003 141 172
    • (2003) Annu. Rev. Cell Dev. Biol. , vol.19 , pp. 141-172
    • Hicke, L.1    Dunn, R.2
  • 48
    • 9744227183 scopus 로고    scopus 로고
    • Ubiquitin: Structures, functions, mechanisms
    • C.M. Pickart, and M.J. Eddins Ubiquitin: structures, functions, mechanisms Biochim. Biophys. Acta 1695 2004 55 72
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 55-72
    • Pickart, C.M.1    Eddins, M.J.2
  • 49
    • 8844237615 scopus 로고    scopus 로고
    • Polyubiquitin chains: Polymeric protein signals
    • C.M. Pickart, and D. Fushman Polyubiquitin chains: polymeric protein signals Curr. Opin. Chem. Biol. 8 2004 610 616
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 610-616
    • Pickart, C.M.1    Fushman, D.2


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