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Volumn 27, Issue 4, 2007, Pages 1394-1406

The Caenorhabditis elegans replication licensing factor CDT-1 is targeted for degradation by the CUL-4/DDB-1 complex

Author keywords

[No Author keywords available]

Indexed keywords

DNA; PROTEIN CUL4; PROTEIN DDB1; PROTEIN SCFSKP2; REPLICATION LICENSING FACTOR CDT1; S PHASE KINASE ASSOCIATED PROTEIN; S PHASE KINASE ASSOCIATED PROTEIN 2; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 33846916845     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.00736-06     Document Type: Article
Times cited : (48)

References (84)
  • 1
    • 33749535905 scopus 로고    scopus 로고
    • Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery
    • Angers, S., T. Li, X. Yi, M. J. Maccoss, R. T. Moon, and N. Zheng. 2006. Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery. Nature 443:590-593.
    • (2006) Nature , vol.443 , pp. 590-593
    • Angers, S.1    Li, T.2    Yi, X.3    Maccoss, M.J.4    Moon, R.T.5    Zheng, N.6
  • 2
    • 30344455639 scopus 로고    scopus 로고
    • PCNA functions as a molecular platform to trigger Cdt1 destruction and prevent re-replication
    • Arias, E. E., and J. C. Walter. 2006. PCNA functions as a molecular platform to trigger Cdt1 destruction and prevent re-replication. Nat. Cell Biol. 8: 84-90.
    • (2006) Nat. Cell Biol , vol.8 , pp. 84-90
    • Arias, E.E.1    Walter, J.C.2
  • 3
    • 11844273174 scopus 로고    scopus 로고
    • Replication-dependent destruction of Cdt1 limits DNA replication to a single round per cell cycle in Xenopus egg extracts
    • Arias, E. E., and J. C. Walter. 2005. Replication-dependent destruction of Cdt1 limits DNA replication to a single round per cell cycle in Xenopus egg extracts. Genes Dev. 19:114-126.
    • (2005) Genes Dev , vol.19 , pp. 114-126
    • Arias, E.E.1    Walter, J.C.2
  • 4
    • 0038708117 scopus 로고    scopus 로고
    • Bhattacharya, S., J. Garriga, J. Calbo, T. Yong, D. S. Haines, and X. Grana. 2003. SKP2 associates with p130 and accelerates p130 ubiquitylation and degradation in human cells. Oncogene 22:2443-2451.
    • Bhattacharya, S., J. Garriga, J. Calbo, T. Yong, D. S. Haines, and X. Grana. 2003. SKP2 associates with p130 and accelerates p130 ubiquitylation and degradation in human cells. Oncogene 22:2443-2451.
  • 5
    • 20344396122 scopus 로고    scopus 로고
    • Preventing re-replication of chromosomal DNA
    • Blow, J. J., and A. Dutta. 2005. Preventing re-replication of chromosomal DNA. Nat. Rev. Mol. Cell Biol. 6:476-486.
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 476-486
    • Blow, J.J.1    Dutta, A.2
  • 6
    • 33645216339 scopus 로고    scopus 로고
    • Cul4A and DDB1 associate with Skp2 to target p27Kip1 for proteolysis involving the COP9 signalosome
    • Bondar, T., A. Kalinina, L. Khair, D. Kopanja, A. Nag, S. Bagchi, and P. Raychaudhuri. 2006. Cul4A and DDB1 associate with Skp2 to target p27Kip1 for proteolysis involving the COP9 signalosome. Mol. Cell. Biol. 26:2531-2539.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 2531-2539
    • Bondar, T.1    Kalinina, A.2    Khair, L.3    Kopanja, D.4    Nag, A.5    Bagchi, S.6    Raychaudhuri, P.7
  • 7
    • 0037325684 scopus 로고    scopus 로고
    • Cyclin E expression during development in Caenorhabditis elegans
    • Brodigan, T. M., J. Liu, M. Park, E. T. Kipreos, and M. Krause. 2003. Cyclin E expression during development in Caenorhabditis elegans. Dev. Biol. 254: 102-115.
    • (2003) Dev. Biol , vol.254 , pp. 102-115
    • Brodigan, T.M.1    Liu, J.2    Park, M.3    Kipreos, E.T.4    Krause, M.5
  • 8
    • 0033176887 scopus 로고    scopus 로고
    • SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27
    • Carrano, A. C., E. Eytan, A. Hershko, and M. Pagano. 1999. SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27. Nat. Cell Biol. 1:193-199.
    • (1999) Nat. Cell Biol , vol.1 , pp. 193-199
    • Carrano, A.C.1    Eytan, E.2    Hershko, A.3    Pagano, M.4
  • 9
    • 0034660079 scopus 로고    scopus 로고
    • Degradation of B-Myb by ubiquitin-mediated proteolysis: Involvement of the Cdc34-SCF(p45Skp2) pathway
    • Charrasse, S., I. Carena, V. Brondani, K. H. Klempnaucr, and S. Ferrari. 2000. Degradation of B-Myb by ubiquitin-mediated proteolysis: involvement of the Cdc34-SCF(p45Skp2) pathway. Oncogene 19:2986-2995.
    • (2000) Oncogene , vol.19 , pp. 2986-2995
    • Charrasse, S.1    Carena, I.2    Brondani, V.3    Klempnaucr, K.H.4    Ferrari, S.5
  • 10
    • 0023803543 scopus 로고
    • Xeroderma pigmentosum group E cells lack a nuclear factor that binds to damaged DNA
    • Chu, G., and E. Chang. 1988. Xeroderma pigmentosum group E cells lack a nuclear factor that binds to damaged DNA. Science 242:564-567.
    • (1988) Science , vol.242 , pp. 564-567
    • Chu, G.1    Chang, E.2
  • 11
    • 0033755967 scopus 로고    scopus 로고
    • Protruding vulva mutants identify novel loci and Wnt signaling factors that function during Caenorhabditis elegans vulva development
    • Eisenmann, D. M., and S. K. Kim. 2000. Protruding vulva mutants identify novel loci and Wnt signaling factors that function during Caenorhabditis elegans vulva development. Genetics 156:1097-1116.
    • (2000) Genetics , vol.156 , pp. 1097-1116
    • Eisenmann, D.M.1    Kim, S.K.2
  • 12
    • 0029866457 scopus 로고    scopus 로고
    • Heterochronic genes control cell cycle progress and developmental competence of C. elegans vulva precursor cells
    • Euling, S., and V. Ambros. 1996. Heterochronic genes control cell cycle progress and developmental competence of C. elegans vulva precursor cells. Cell 84:667-676.
    • (1996) Cell , vol.84 , pp. 667-676
    • Euling, S.1    Ambros, V.2
  • 13
    • 0033789694 scopus 로고    scopus 로고
    • Mutations in cye-1, a Caenorhabditis elegans cyclin E homolog, reveal coordination between cell-cycle control and vulval development
    • Fay, D. S., and M. Han. 2000. Mutations in cye-1, a Caenorhabditis elegans cyclin E homolog, reveal coordination between cell-cycle control and vulval development. Development 127:4049-4060.
    • (2000) Development , vol.127 , pp. 4049-4060
    • Fay, D.S.1    Han, M.2
  • 14
    • 2342642220 scopus 로고    scopus 로고
    • Preventing DNA re-replication-divergent safeguards in yeast and metazoa
    • Feng, H., and E. T. Kipreos. 2003. Preventing DNA re-replication-divergent safeguards in yeast and metazoa. Cell Cycle 2:431-434.
    • (2003) Cell Cycle , vol.2 , pp. 431-434
    • Feng, H.1    Kipreos, E.T.2
  • 15
    • 0033257474 scopus 로고    scopus 로고
    • CUL-2 is required for the G1-to-S-phase transition and mitotic chromosome condensation in Caenorhabditis elegans
    • Feng, H., W. Zhong, G. Punkosdy, S. Gu, L. Zhou, E. K. Seabolt, and E. T. Kipreos. 1999. CUL-2 is required for the G1-to-S-phase transition and mitotic chromosome condensation in Caenorhabditis elegans. Nat. Cell Biol. 1:486-492.
    • (1999) Nat. Cell Biol , vol.1 , pp. 486-492
    • Feng, H.1    Zhong, W.2    Punkosdy, G.3    Gu, S.4    Zhou, L.5    Seabolt, E.K.6    Kipreos, E.T.7
  • 16
    • 0034625050 scopus 로고    scopus 로고
    • Somatic polyploidization and cellular proliferation drive body size evolution in nematodes
    • Flemming, A. J., Z. Z. Shen, A. Cunha, S. W. Emmons, and A. M. Leroi. 2000. Somatic polyploidization and cellular proliferation drive body size evolution in nematodes. Proc. Natl. Acad. Sci. USA 97:5285-5290.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5285-5290
    • Flemming, A.J.1    Shen, Z.Z.2    Cunha, A.3    Emmons, S.W.4    Leroi, A.M.5
  • 17
    • 0027212498 scopus 로고
    • Solubilization and purification of enzymatically active glutathione S-transferase (pGEX) fusion proteins
    • Frangioni, J. V., and B. G. Neel. 1993. Solubilization and purification of enzymatically active glutathione S-transferase (pGEX) fusion proteins. Anal. Biochem. 210:179-187.
    • (1993) Anal. Biochem , vol.210 , pp. 179-187
    • Frangioni, J.V.1    Neel, B.G.2
  • 18
    • 0035092687 scopus 로고    scopus 로고
    • The cell-cycle regulatory protein Cks1 is required for SCF-(Skp2)-mediated ubiquitinylation of p27
    • Ganoth, D., G. Bornstein, T. K. Ko, B. Larsen, M. Tyers, M. Pagano, and A. Hershko. 2001. The cell-cycle regulatory protein Cks1 is required for SCF-(Skp2)-mediated ubiquitinylation of p27. Nat. Cell Biol. 3:321-324.
    • (2001) Nat. Cell Biol , vol.3 , pp. 321-324
    • Ganoth, D.1    Bornstein, G.2    Ko, T.K.3    Larsen, B.4    Tyers, M.5    Pagano, M.6    Hershko, A.7
  • 19
    • 0042592926 scopus 로고    scopus 로고
    • Garriga, J., S. Bhattacharya, J. Calbo, R. M. Marshall, M. Truongcao, D. S. Haines, and X. Grana. 2003. CDK9 is constitutively expressed throughout the cell cycle, and its steady-state expression is independent of SKP2. Mol. Cell. Biol. 23:5165-5173.
    • Garriga, J., S. Bhattacharya, J. Calbo, R. M. Marshall, M. Truongcao, D. S. Haines, and X. Grana. 2003. CDK9 is constitutively expressed throughout the cell cycle, and its steady-state expression is independent of SKP2. Mol. Cell. Biol. 23:5165-5173.
  • 20
    • 33744795969 scopus 로고    scopus 로고
    • CSA-dependent degradation of CSB by the ubiquitin-proteasome pathway establishes a link between complementation factors of the Cockayne syndrome
    • Groisman, R., I. Kuraoka, O. Chevallier, N. Gaye, T. Magnaldo, K. Tanaka, A. F. Kisselev, A. Harel-Bellan, and Y. Nakatani. 2006. CSA-dependent degradation of CSB by the ubiquitin-proteasome pathway establishes a link between complementation factors of the Cockayne syndrome. Genes Dev. 20:1429-1434.
    • (2006) Genes Dev , vol.20 , pp. 1429-1434
    • Groisman, R.1    Kuraoka, I.2    Chevallier, O.3    Gaye, N.4    Magnaldo, T.5    Tanaka, K.6    Kisselev, A.F.7    Harel-Bellan, A.8    Nakatani, Y.9
  • 21
    • 0037509859 scopus 로고    scopus 로고
    • The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage
    • Groisman, R., J. Polanowska, I. Kuraoka, J. Sawada, M. Saijo, R. Drapkin, A. F. Kisselev, K. Tanaka, and Y. Nakatani. 2003. The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage. Cell 113:357-367.
    • (2003) Cell , vol.113 , pp. 357-367
    • Groisman, R.1    Polanowska, J.2    Kuraoka, I.3    Sawada, J.4    Saijo, M.5    Drapkin, R.6    Kisselev, A.F.7    Tanaka, K.8    Nakatani, Y.9
  • 22
    • 0021994541 scopus 로고
    • Polyploid tissues in the nematode Caenorhabditis elegans
    • Hedgecock, E. M., and J. G. White. 1985. Polyploid tissues in the nematode Caenorhabditis elegans. Dev. Biol. 107:128-133.
    • (1985) Dev. Biol , vol.107 , pp. 128-133
    • Hedgecock, E.M.1    White, J.G.2
  • 23
    • 33747831132 scopus 로고    scopus 로고
    • L2DTL/CDT2 interacts with the CUL4/DDB1 complex and PCNA and regulates CDT1 proteolysis in response to DNA damage
    • Higa, L. A., D. Banks, M. Wu, R. Kobayashi, H. Sun, and H. Zhang. 2006. L2DTL/CDT2 interacts with the CUL4/DDB1 complex and PCNA and regulates CDT1 proteolysis in response to DNA damage. Cell Cycle 5:1675-1680.
    • (2006) Cell Cycle , vol.5 , pp. 1675-1680
    • Higa, L.A.1    Banks, D.2    Wu, M.3    Kobayashi, R.4    Sun, H.5    Zhang, H.6
  • 24
    • 0242525214 scopus 로고    scopus 로고
    • Radiation-mediated proteolysis of CDT1 by CUL4-ROC1 and CSN complexes constitutes a new checkpoint
    • Higa, L. A., I. S. Mihaylov, D. P. Banks, J. Zheng, and H. Zhang. 2003. Radiation-mediated proteolysis of CDT1 by CUL4-ROC1 and CSN complexes constitutes a new checkpoint. Nat. Cell Biol. 5:1008-1015.
    • (2003) Nat. Cell Biol , vol.5 , pp. 1008-1015
    • Higa, L.A.1    Mihaylov, I.S.2    Banks, D.P.3    Zheng, J.4    Zhang, H.5
  • 25
    • 33645309411 scopus 로고    scopus 로고
    • Involvement of CUL4 ubiquitin E3 ligases in regulating CDK inhibitors Dacapo/p27Kip1 and cyclin E degradation
    • Higa, L. A., X. Yang, J. Zheng, D. Banks, M. Wu, P. Ghosh, H. Sun, and H. Zhang. 2006. Involvement of CUL4 ubiquitin E3 ligases in regulating CDK inhibitors Dacapo/p27Kip1 and cyclin E degradation. Cell Cycle 5:71-77.
    • (2006) Cell Cycle , vol.5 , pp. 71-77
    • Higa, L.A.1    Yang, X.2    Zheng, J.3    Banks, D.4    Wu, M.5    Ghosh, P.6    Sun, H.7    Zhang, H.8
  • 26
    • 5444274523 scopus 로고    scopus 로고
    • Targeted ubiquitination of CDT1 by the DDB1-CUL4A-ROC1 ligase in response to DNA damage
    • Hu, J., C. M. McCall, T. Ohta, and Y. Xiong. 2004. Targeted ubiquitination of CDT1 by the DDB1-CUL4A-ROC1 ligase in response to DNA damage. Nat. Cell Biol. 6:1003-1009.
    • (2004) Nat. Cell Biol , vol.6 , pp. 1003-1009
    • Hu, J.1    McCall, C.M.2    Ohta, T.3    Xiong, Y.4
  • 27
    • 33645212112 scopus 로고    scopus 로고
    • An evolutionarily conserved function of proliferating cell nuclear antigen for Cdt1 degradation by the Cul4-Ddb1 ubiquitin ligase in response to DNA damage
    • Hu, J., and Y. Xiong. 2006. An evolutionarily conserved function of proliferating cell nuclear antigen for Cdt1 degradation by the Cul4-Ddb1 ubiquitin ligase in response to DNA damage. J. Biol. Chem. 281:3753-3756.
    • (2006) J. Biol. Chem , vol.281 , pp. 3753-3756
    • Hu, J.1    Xiong, Y.2
  • 29
    • 0030455820 scopus 로고    scopus 로고
    • Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast
    • James, P., J. Halladay, and E. A. Craig. 1996. Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast. Genetics 144:1425-1436.
    • (1996) Genetics , vol.144 , pp. 1425-1436
    • James, P.1    Halladay, J.2    Craig, E.A.3
  • 30
    • 0004270170 scopus 로고
    • Janssen, K, ed, John Wiley & Sons, Boston, MA
    • Janssen, K. (ed.). 1995. Current protocols in molecular biology. John Wiley & Sons, Boston, MA.
    • (1995) Current protocols in molecular biology
  • 31
    • 20444403003 scopus 로고    scopus 로고
    • Ubiquitylation of RAG-2 by Skp2-SCF links destruction of the V(D)J recombinase to the cell cycle
    • Jiang, H., F. C. Chang, A. E. Ross, J. Lee, K. Nakayama, K. Nakayama, and S. Desiderio. 2005. Ubiquitylation of RAG-2 by Skp2-SCF links destruction of the V(D)J recombinase to the cell cycle. Mol. Cell 18:699-709.
    • (2005) Mol. Cell , vol.18 , pp. 699-709
    • Jiang, H.1    Chang, F.C.2    Ross, A.E.3    Lee, J.4    Nakayama, K.5    Nakayama, K.6    Desiderio, S.7
  • 32
    • 33747873322 scopus 로고    scopus 로고
    • A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is required for S phase destruction of the replication factor Cdtl
    • Jin, J., E. E. Arias, J. Chen, J. W. Harper, and J. C. Walter. 2006. A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is required for S phase destruction of the replication factor Cdtl. Mol. Cell 23:709-721.
    • (2006) Mol. Cell , vol.23 , pp. 709-721
    • Jin, J.1    Arias, E.E.2    Chen, J.3    Harper, J.W.4    Walter, J.C.5
  • 33
    • 0035229245 scopus 로고    scopus 로고
    • Effectiveness of specific RNA-mediated interference through ingested double-stranded RNA in Caenorhabditis elegans
    • RESEARCH0002
    • Kamath, R. S., M. Martinez-Campos, P. Zipperlen, A. G. Fraser, and J. Ahringer. 2001. Effectiveness of specific RNA-mediated interference through ingested double-stranded RNA in Caenorhabditis elegans. Genome Biol. 2:RESEARCH0002. http://genomebiology.com/2000/2/1/research/0002.
    • (2001) Genome Biol , vol.2
    • Kamath, R.S.1    Martinez-Campos, M.2    Zipperlen, P.3    Fraser, A.G.4    Ahringer, J.5
  • 34
    • 0027442869 scopus 로고
    • Characterization of a human DNA damage binding protein implicated in xeroderma pigmentosum E
    • Keeney, S., G. J. Chang, and S. Linn. 1993. Characterization of a human DNA damage binding protein implicated in xeroderma pigmentosum E. J. Biol. Chem. 268:21293-21300.
    • (1993) J. Biol. Chem , vol.268 , pp. 21293-21300
    • Keeney, S.1    Chang, G.J.2    Linn, S.3
  • 35
    • 0031926583 scopus 로고    scopus 로고
    • Chromatin silencing and the maintenance of a functional germ line in Caenorhabditis elegans
    • Kelly, W. G., and A. Fire. 1998. Chromatin silencing and the maintenance of a functional germ line in Caenorhabditis elegans. Development 125:2451-2456.
    • (1998) Development , vol.125 , pp. 2451-2456
    • Kelly, W.G.1    Fire, A.2
  • 39
    • 0035427387 scopus 로고    scopus 로고
    • Cell migration in invertebrates: Clues from border and distal tip cells
    • Lehmann, R. 2001. Cell migration in invertebrates: clues from border and distal tip cells. Curr. Opin. Genet. Dev. 11:457-463.
    • (2001) Curr. Opin. Genet. Dev , vol.11 , pp. 457-463
    • Lehmann, R.1
  • 40
    • 1942426448 scopus 로고    scopus 로고
    • Cul-4A targets p27 for degradation and regulates proliferation, cell cycle exit, and differentiation during erythropoiesis
    • Li, B., N. Jia, R. Kapur, and K. T. Chun. 2006. Cul-4A targets p27 for degradation and regulates proliferation, cell cycle exit, and differentiation during erythropoiesis. Blood 101:1769-1776.
    • (2006) Blood , vol.101 , pp. 1769-1776
    • Li, B.1    Jia, N.2    Kapur, R.3    Chun, K.T.4
  • 41
    • 30344460705 scopus 로고    scopus 로고
    • Structure of DDB1 in complex with a paramyxovirus V protein: Viral hijack of a propeller cluster in ubiquitin ligase
    • Li, T., X. Chen, K. C. Garbutt, P. Zhou, and N. Zheng. 2006. Structure of DDB1 in complex with a paramyxovirus V protein: viral hijack of a propeller cluster in ubiquitin ligase. Cell 124:105-117.
    • (2006) Cell , vol.124 , pp. 105-117
    • Li, T.1    Chen, X.2    Garbutt, K.C.3    Zhou, P.4    Zheng, N.5
  • 42
    • 0043234476 scopus 로고    scopus 로고
    • The SCF(Skp2) ubiquitin ligase complex interacts with the human replication licensing factor Cdt1 and regulates Cdt1 degradation
    • Li, X., Q. Zhao, R. Liao, P. Sun, and X. Wu. 2003. The SCF(Skp2) ubiquitin ligase complex interacts with the human replication licensing factor Cdt1 and regulates Cdt1 degradation. J. Biol. Chem. 278:30854-30858.
    • (2003) J. Biol. Chem , vol.278 , pp. 30854-30858
    • Li, X.1    Zhao, Q.2    Liao, R.3    Sun, P.4    Wu, X.5
  • 43
    • 33644863486 scopus 로고    scopus 로고
    • Cooperation of ERK and SCFSkp2 for MKP-1 destruction provides a positive feedback regulation of proliferating signaling
    • Lin, Y. W., and J. L. Yang. 2006. Cooperation of ERK and SCFSkp2 for MKP-1 destruction provides a positive feedback regulation of proliferating signaling. J. Biol. Chem. 281:915-926.
    • (2006) J. Biol. Chem , vol.281 , pp. 915-926
    • Lin, Y.W.1    Yang, J.L.2
  • 45
    • 0038185375 scopus 로고    scopus 로고
    • Cop9/signalosome subunits and Pcu4 regulate ribonucleotide reductase by both checkpoint-dependent and -independent mechanisms
    • Liu, C., K. A. Powell, K. Mundt, L. Wu, A. M. Carr, and T. Caspari. 2003. Cop9/signalosome subunits and Pcu4 regulate ribonucleotide reductase by both checkpoint-dependent and -independent mechanisms. Genes Dev. 17:1130-1140.
    • (2003) Genes Dev , vol.17 , pp. 1130-1140
    • Liu, C.1    Powell, K.A.2    Mundt, K.3    Wu, L.4    Carr, A.M.5    Caspari, T.6
  • 46
    • 2342442851 scopus 로고    scopus 로고
    • Cyclin-dependent kinases phosphorylate human Cdt1 and induce its degradation
    • Lia, E., X. Li, F. Yan, Q. Zhao, and X. Wu. 2004. Cyclin-dependent kinases phosphorylate human Cdt1 and induce its degradation. J. Biol. Chem. 279:17283-17288.
    • (2004) J. Biol. Chem , vol.279 , pp. 17283-17288
    • Lia, E.1    Li, X.2    Yan, F.3    Zhao, Q.4    Wu, X.5
  • 47
    • 26244431903 scopus 로고    scopus 로고
    • Right place, right time, and only once: Replication initiation in metazoans
    • Machida, Y. J., J. L. Hamlin, and A. Dutta. 2005. Right place, right time, and only once: replication initiation in metazoans. Cell 123:13-24.
    • (2005) Cell , vol.123 , pp. 13-24
    • Machida, Y.J.1    Hamlin, J.L.2    Dutta, A.3
  • 48
    • 0033130137 scopus 로고    scopus 로고
    • Interaction between ubiquitin-protein ligase SCFSKP2 and E2F-1 underlies the regulation of E2F-1 degradation
    • Marti, A., C. Wirbelauer, M. Scheffner, and W. Krek. 1999. Interaction between ubiquitin-protein ligase SCFSKP2 and E2F-1 underlies the regulation of E2F-1 degradation. Nat. Cell Biol. 1:14-19.
    • (1999) Nat. Cell Biol , vol.1 , pp. 14-19
    • Marti, A.1    Wirbelauer, C.2    Scheffner, M.3    Krek, W.4
  • 49
    • 0029443103 scopus 로고
    • DNA transformation
    • Mello, C., and A. Fire. 1995. DNA transformation. Methods Cell Biol. 48:451-482.
    • (1995) Methods Cell Biol , vol.48 , pp. 451-482
    • Mello, C.1    Fire, A.2
  • 50
    • 0036208817 scopus 로고    scopus 로고
    • Human origin recognition complex large subunit is degraded by ubiquitin-mediated proteolysis after initiation of DNA replication
    • Mendez, J., X. H. Zou-Yang, S. Y. Kim, M. Hidaka, W. P. Tansey, and B. Stillman. 2002. Human origin recognition complex large subunit is degraded by ubiquitin-mediated proteolysis after initiation of DNA replication. Mol. Cell 9:481-491.
    • (2002) Mol. Cell , vol.9 , pp. 481-491
    • Mendez, J.1    Zou-Yang, X.H.2    Kim, S.Y.3    Hidaka, M.4    Tansey, W.P.5    Stillman, B.6
  • 52
    • 0026573580 scopus 로고
    • A general and fast method to generate multiple site directed mutations
    • Mikaelian, I., and A. Sergeant. 1992. A general and fast method to generate multiple site directed mutations. Nucleic Acids Res. 20:376.
    • (1992) Nucleic Acids Res , vol.20 , pp. 376
    • Mikaelian, I.1    Sergeant, A.2
  • 53
    • 0029447440 scopus 로고
    • Immunofluorescence microscopy
    • Miller, D. M., and D. C. Shakes. 1995. Immunofluorescence microscopy. Methods Cell Biol. 48:365-394.
    • (1995) Methods Cell Biol , vol.48 , pp. 365-394
    • Miller, D.M.1    Shakes, D.C.2
  • 54
    • 0036172085 scopus 로고    scopus 로고
    • Recovery of liver mass without proliferation of hepatocytes after partial hepatectomy in Skp2-deficient mice
    • Minamishima, Y. A., K. Nakayama, and K. Nakayama. 2002. Recovery of liver mass without proliferation of hepatocytes after partial hepatectomy in Skp2-deficient mice. Cancer Res. 62:995-999.
    • (2002) Cancer Res , vol.62 , pp. 995-999
    • Minamishima, Y.A.1    Nakayama, K.2    Nakayama, K.3
  • 57
    • 0034611749 scopus 로고    scopus 로고
    • The Cdt1 protein is required to license DNA for replication in fission yeast
    • Nishitani, H., Z. Lygerou, T. Nishimoto, and P. Nurse. 2000. The Cdt1 protein is required to license DNA for replication in fission yeast. Nature 404:625-628.
    • (2000) Nature , vol.404 , pp. 625-628
    • Nishitani, H.1    Lygerou, Z.2    Nishimoto, T.3    Nurse, P.4
  • 59
    • 0035976980 scopus 로고    scopus 로고
    • The human licensing factor for DNA replication Cdt1 accumulates in G1 and is destabilized after initiation of S-phase
    • Nishitani, H., S. Taraviras, Z. Lygerou, and T. Nishimoto. 2001. The human licensing factor for DNA replication Cdt1 accumulates in G1 and is destabilized after initiation of S-phase. J. Biol. Chem. 276:44905-44911.
    • (2001) J. Biol. Chem , vol.276 , pp. 44905-44911
    • Nishitani, H.1    Taraviras, S.2    Lygerou, Z.3    Nishimoto, T.4
  • 60
    • 11244351579 scopus 로고    scopus 로고
    • Function and regulation of cullin-RING ubiquitin ligases
    • Petroski, M. D., and R. J. Deshaies. 2005. Function and regulation of cullin-RING ubiquitin ligases. Nat Rev. Mol. Cell Biol. 6:9-20.
    • (2005) Nat Rev. Mol. Cell Biol , vol.6 , pp. 9-20
    • Petroski, M.D.1    Deshaies, R.J.2
  • 61
    • 0035887012 scopus 로고    scopus 로고
    • The Drosophila Geminin homolog: Roles for Geminin in limiting DNA replication, in anaphase and in neurogenesis
    • Quinn, L. M., A. Herr, T. J. McGarry, and H. Richardson. 2001. The Drosophila Geminin homolog: roles for Geminin in limiting DNA replication, in anaphase and in neurogenesis. Genes Dev. 15:2741-2754.
    • (2001) Genes Dev , vol.15 , pp. 2741-2754
    • Quinn, L.M.1    Herr, A.2    McGarry, T.J.3    Richardson, H.4
  • 62
    • 33646504727 scopus 로고    scopus 로고
    • PCNA is a cofactor for Cdt1 degradation by CUL4/DDB1-mediated N-terminal ubiquitination
    • Senga, T., U. Sivaprasad, W. Zhu, J. H. Park, E. E. Arias, J. C. Walter, and A. Dutta. 2006. PCNA is a cofactor for Cdt1 degradation by CUL4/DDB1-mediated N-terminal ubiquitination. J. Biol. Chem. 281:6246-6252.
    • (2006) J. Biol. Chem , vol.281 , pp. 6246-6252
    • Senga, T.1    Sivaprasad, U.2    Zhu, W.3    Park, J.H.4    Arias, E.E.5    Walter, J.C.6    Dutta, A.7
  • 63
    • 0027213431 scopus 로고
    • Isolation and characterization of mutations causing abnormal eversion of the vulva in Caenorhabditis elegans
    • Seydoux, G., C. Savage, and I. Greenwald. 1993. Isolation and characterization of mutations causing abnormal eversion of the vulva in Caenorhabditis elegans. Dev. Biol. 157:423-436.
    • (1993) Dev. Biol , vol.157 , pp. 423-436
    • Seydoux, G.1    Savage, C.2    Greenwald, I.3
  • 64
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith, D. B., and K. S. Johnson. 1988. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 67:31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 65
    • 0035265829 scopus 로고    scopus 로고
    • A CDK-independent function of mammalian Cks1: Targeting of SCF(Skp2) to the CDK inhibitor p27Kip1
    • Spruck, C., H. Strohmaier, M. Watson, A. P. Smith, A. Ryan, T. W. Krek, and S. I. Reed. 2001. A CDK-independent function of mammalian Cks1: targeting of SCF(Skp2) to the CDK inhibitor p27Kip1. Mol. Cell 7:639-650.
    • (2001) Mol. Cell , vol.7 , pp. 639-650
    • Spruck, C.1    Strohmaier, H.2    Watson, M.3    Smith, A.P.4    Ryan, A.5    Krek, T.W.6    Reed, S.I.7
  • 67
    • 2442427423 scopus 로고    scopus 로고
    • Cdt1 phosphorylation by cyclin A-dependent kinases negatively regulates its function without affecting geminin binding
    • Sugimoto, N., Y. Tatsumi, T. Tsurumi, A. Matsukage, T. Kiyono, H. Nishitani, and M. Fujita. 2004. Cdt1 phosphorylation by cyclin A-dependent kinases negatively regulates its function without affecting geminin binding. J. Biol. Chem. 279:19691-19697.
    • (2004) J. Biol. Chem , vol.279 , pp. 19691-19697
    • Sugimoto, N.1    Tatsumi, Y.2    Tsurumi, T.3    Matsukage, A.4    Kiyono, T.5    Nishitani, H.6    Fujita, M.7
  • 68
    • 0017618537 scopus 로고
    • Post-embryonic cell lineages of the nematode, Caenorhabditis elegans
    • Sulston, J. E., and H. R. Horvitz. 1977. Post-embryonic cell lineages of the nematode, Caenorhabditis elegans. Dev. Biol. 56:110-156.
    • (1977) Dev. Biol , vol.56 , pp. 110-156
    • Sulston, J.E.1    Horvitz, H.R.2
  • 70
    • 0000807693 scopus 로고
    • The desoxyribose nucleic acid content of animal nuclei
    • Swift, H. H. 1950. The desoxyribose nucleic acid content of animal nuclei. Physiol. Zool. 23:169-198.
    • (1950) Physiol. Zool , vol.23 , pp. 169-198
    • Swift, H.H.1
  • 71
    • 0035147434 scopus 로고    scopus 로고
    • Repression of origin assembly in metaphase depends on inhibition of RLF-B/Cdt1 by geminin
    • Tada, S., A. Li, D. Maiorano, M. Mechali, and J. J. Blow. 2001. Repression of origin assembly in metaphase depends on inhibition of RLF-B/Cdt1 by geminin. Nat. Cell Biol. 3:107-113.
    • (2001) Nat. Cell Biol , vol.3 , pp. 107-113
    • Tada, S.1    Li, A.2    Maiorano, D.3    Mechali, M.4    Blow, J.J.5
  • 72
    • 20744458539 scopus 로고    scopus 로고
    • Degradation of Cdt1 during S phase is Skp2-independent and is required for efficient progression of mammalian cells through S phase
    • Takeda, D. Y., J. D. Parvin, and A. Dutta. 2005. Degradation of Cdt1 during S phase is Skp2-independent and is required for efficient progression of mammalian cells through S phase. J. Biol. Chem. 280:23416-23423.
    • (2005) J. Biol. Chem , vol.280 , pp. 23416-23423
    • Takeda, D.Y.1    Parvin, J.D.2    Dutta, A.3
  • 73
    • 7244239295 scopus 로고    scopus 로고
    • Drosophila double-parked is sufficient to induce re-replication during development and is regulated by cyclin E/CDK2
    • Thomer, M., N. R. May, B. D. Aggarwal, G. Kwok, and B. R. Calvi. 2004. Drosophila double-parked is sufficient to induce re-replication during development and is regulated by cyclin E/CDK2. Development 131:4807-4818.
    • (2004) Development , vol.131 , pp. 4807-4818
    • Thomer, M.1    May, N.R.2    Aggarwal, B.D.3    Kwok, G.4    Calvi, B.R.5
  • 74
    • 0033578073 scopus 로고    scopus 로고
    • p27(Kip1) ubiquitination and degradation is regulated by the SCF(Skp2) complex through phosphorylated Thr187 in p27
    • Tsvetkov, L. M., K. H. Yeh, S. J. Lee, H. Sun, and H. Zhang. 1999. p27(Kip1) ubiquitination and degradation is regulated by the SCF(Skp2) complex through phosphorylated Thr187 in p27. Curr. Biol. 9:661-664.
    • (1999) Curr. Biol , vol.9 , pp. 661-664
    • Tsvetkov, L.M.1    Yeh, K.H.2    Lee, S.J.3    Sun, H.4    Zhang, H.5
  • 75
    • 0036942290 scopus 로고    scopus 로고
    • Paramyxoviruses SV5 and HPIV2 assemble STAT protein ubiquitin ligase complexes from cellular components
    • Ulane, C. M., and C. M. Horvath. 2002. Paramyxoviruses SV5 and HPIV2 assemble STAT protein ubiquitin ligase complexes from cellular components. Virology 304:160-166.
    • (2002) Virology , vol.304 , pp. 160-166
    • Ulane, C.M.1    Horvath, C.M.2
  • 76
    • 23244438013 scopus 로고    scopus 로고
    • Composition and assembly of STAT-targeting ubiquitin ligase complexes: Paramyxovirus V protein carboxyl terminus is an oligomerization domain
    • Ulane, C. M., A. Kentsis, C. D. Cruz, J. P. Parisien, K. L. Schneider, and C. M. Horvath. 2005. Composition and assembly of STAT-targeting ubiquitin ligase complexes: paramyxovirus V protein carboxyl terminus is an oligomerization domain. J. Virol. 79:10180-10189.
    • (2005) J. Virol , vol.79 , pp. 10180-10189
    • Ulane, C.M.1    Kentsis, A.2    Cruz, C.D.3    Parisien, J.P.4    Schneider, K.L.5    Horvath, C.M.6
  • 79
    • 33744781568 scopus 로고    scopus 로고
    • Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage
    • Wang, H., L. Zhai, J. Xu, H. Y. Joo, S. Jackson, H. Erdjument-Bromage, P. Tempst, Y. Xiong, and Y. Zhang. 2006. Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage. Mol. Cell 22:383-394.
    • (2006) Mol. Cell , vol.22 , pp. 383-394
    • Wang, H.1    Zhai, L.2    Xu, J.3    Joo, H.Y.4    Jackson, S.5    Erdjument-Bromage, H.6    Tempst, P.7    Xiong, Y.8    Zhang, Y.9
  • 81
    • 0034704221 scopus 로고    scopus 로고
    • 81. Wohlschlegel, J. A., B. T. Dwyer, S. K. Dhar, C. Cvetic, J. C. Walter, and A. Dutta. 2000. Inhibition of eukaryotic DNA replication by geminin binding to Cdt1. Science 290:2309-2312.
    • 81. Wohlschlegel, J. A., B. T. Dwyer, S. K. Dhar, C. Cvetic, J. C. Walter, and A. Dutta. 2000. Inhibition of eukaryotic DNA replication by geminin binding to Cdt1. Science 290:2309-2312.
  • 82
    • 21244485431 scopus 로고    scopus 로고
    • Caenorhabditis elegans geminin homologue participates in cell cycle regulation and germ line development
    • Yanagi, K., T. Mizuno, T. Tsuyama, S. Tada, Y. Iida, A. Sugimoto, T. Eki, T. Enomoto, and F. Hanaoka. 2005. Caenorhabditis elegans geminin homologue participates in cell cycle regulation and germ line development. J. Biol. Chem. 280:19689-19694.
    • (2005) J. Biol. Chem , vol.280 , pp. 19689-19694
    • Yanagi, K.1    Mizuno, T.2    Tsuyama, T.3    Tada, S.4    Iida, Y.5    Sugimoto, A.6    Eki, T.7    Enomoto, T.8    Hanaoka, F.9
  • 83
    • 0032530151 scopus 로고    scopus 로고
    • Human CUL-1 associates with the SKP1/SKP2 complex and regulates p21(CIP1/WAF1) and cyclin D proteins
    • Yu, Z. K., J. L. Gervais, and H. Zhang. 1998. Human CUL-1 associates with the SKP1/SKP2 complex and regulates p21(CIP1/WAF1) and cyclin D proteins. Proc. Natl. Acad. Sci. USA. 95:11324-11329.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11324-11329
    • Yu, Z.K.1    Gervais, J.L.2    Zhang, H.3
  • 84
    • 0037967230 scopus 로고    scopus 로고
    • CUL-4 ubiquitin ligase maintains genome stability by restraining DNA-replication licensing
    • Zhong, W., H. Feng, F. E. Santiago, and E. T. Kipreos. 2003. CUL-4 ubiquitin ligase maintains genome stability by restraining DNA-replication licensing. Nature 423:885-889.
    • (2003) Nature , vol.423 , pp. 885-889
    • Zhong, W.1    Feng, H.2    Santiago, F.E.3    Kipreos, E.T.4


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