메뉴 건너뛰기




Volumn 425, Issue 6955, 2003, Pages 311-316

The BTB protein MEL-26 is a substrate-specific adaptor of the CUL-3 ubiquitin-ligase

Author keywords

[No Author keywords available]

Indexed keywords

BIODEGRADATION; CELL CULTURE; MOLECULAR BIOLOGY;

EID: 0141493448     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature01959     Document Type: Article
Times cited : (358)

References (27)
  • 1
    • 0034676443 scopus 로고    scopus 로고
    • Insights into SCF ubiquitin ligases from the structure of the Skp1-Skp2 complex
    • Schulman, B.A. et al. Insights into SCF ubiquitin ligases from the structure of the Skp1-Skp2 complex. Nature 408, 381-386 (2000).
    • (2000) Nature , vol.408 , pp. 381-386
    • Schulman, B.A.1
  • 2
    • 18344391432 scopus 로고    scopus 로고
    • Structure of the Cult-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex
    • Zheng, N. et al. Structure of the Cult-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex. Nature 416, 703-709 (2002).
    • (2002) Nature , vol.416 , pp. 703-709
    • Zheng, N.1
  • 3
    • 0033574737 scopus 로고    scopus 로고
    • Structure of the VHL-ElonginC-ElonginB complex: Implications for VHL tumor suppressor function
    • Stebbins, C. E., Kaelin, W. G. Jr & Pavletich, N. P. Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function. Science 284, 455-461 (1999).
    • (1999) Science , vol.284 , pp. 455-461
    • Stebbins, C.E.1    Kaelin W.G., Jr.2    Pavletich, N.P.3
  • 4
    • 0037513423 scopus 로고    scopus 로고
    • Neddylation and deneddylation of CUL-3 is required to target MEI-1/Katanin for degradation at the meiosis-to-mitosis transition in C. elegans
    • Pintard, L. et al. Neddylation and deneddylation of CUL-3 is required to target MEI-1/Katanin for degradation at the meiosis-to-mitosis transition in C. elegans. Curr. Biol. 13, 911-921 (2003).
    • (2003) Curr. Biol. , vol.13 , pp. 911-921
    • Pintard, L.1
  • 5
    • 0028110129 scopus 로고
    • The BTB domain, found primarily in zinc finger proteins, defines an evolutionarily conserved family that includes several developmentally regulated genes in Drosophila
    • Zollman, S., Godt, D., Prive, G. G., Couderc, J. L. & Laski, F. A. The BTB domain, found primarily in zinc finger proteins, defines an evolutionarily conserved family that includes several developmentally regulated genes in Drosophila. Proc. Natl Acad. Sci USA 91, 10717-10721 (1994).
    • (1994) Proc. Natl Acad. Sci USA , vol.91 , pp. 10717-10721
    • Zollman, S.1    Godt, D.2    Prive, G.G.3    Couderc, J.L.4    Laski, F.A.5
  • 6
    • 0037083528 scopus 로고    scopus 로고
    • Cytoskeletal regulation by the Nedd8 ubiquitin-like protein modification pathway
    • Kurz, T. et al. Cytoskeletal regulation by the Nedd8 ubiquitin-like protein modification pathway. Science 295, 1294-1298 (2002).
    • (2002) Science , vol.295 , pp. 1294-1298
    • Kurz, T.1
  • 7
    • 0028236624 scopus 로고
    • Localization of the mei-1 gene product of Caenorhabditis elegans, a meiotic-specific spindle component
    • Clark-Maguire, S. & Mains, P. E. Localization of the mei-1 gene product of Caenorhabditis elegans, a meiotic-specific spindle component. J. Cell Biol. 126, 199-209 (1994).
    • (1994) J. Cell Biol. , vol.126 , pp. 199-209
    • Clark-Maguire, S.1    Mains, P.E.2
  • 8
    • 0034192639 scopus 로고    scopus 로고
    • MEI-1/MEI-2 katanin-like microtubule severing activity is required for Caenorhabditis elegans meiosis
    • Srayko, M., Buster, D. W., Bazirgan, O. A., McNally, F. J. & Mains, P. E. MEI-1/MEI-2 katanin-like microtubule severing activity is required for Caenorhabditis elegans meiosis. Genes Dev. 14, 1072-1084 (2000).
    • (2000) Genes Dev. , vol.14 , pp. 1072-1084
    • Srayko, M.1    Buster, D.W.2    Bazirgan, O.A.3    McNally, F.J.4    Mains, P.E.5
  • 9
    • 0025119673 scopus 로고
    • Mutations affecting the meiotic and mitotic divisions of the early Caenorhabditis elegans embryo
    • Mains, P. E., Kemphues, K. J., Sprunger, S. A., Sulston, I. A. & Wood, W. B. Mutations affecting the meiotic and mitotic divisions of the early Caenorhabditis elegans embryo. Genetics 126, 593-605 (1990).
    • (1990) Genetics , vol.126 , pp. 593-605
    • Mains, P.E.1    Kemphues, K.J.2    Sprunger, S.A.3    Sulston, I.A.4    Wood, W.B.5
  • 10
    • 0031717483 scopus 로고    scopus 로고
    • Genetic and molecular characterization of the Caenorhabditis elegans gene, mel-26, a postmeiotic negative regulator of mei-1, a meiotic-specific spindle component
    • Dow, M. R. & Mains, P. E. Genetic and molecular characterization of the Caenorhabditis elegans gene, mel-26, a postmeiotic negative regulator of mei-1, a meiotic-specific spindle component. Genetics 150, 119-128 (1998).
    • (1998) Genetics , vol.150 , pp. 119-128
    • Dow, M.R.1    Mains, P.E.2
  • 11
    • 0028147310 scopus 로고
    • mei-1, a gene required for meiotic spindle formation in Caenorhabditis elegans, is a member of a family of ATPases
    • Clark-Maguire, S. & Mains, P. E. mei-1, a gene required for meiotic spindle formation in Caenorhabditis elegans, is a member of a family of ATPases. Genetics 136, 533-546 (1994).
    • (1994) Genetics , vol.136 , pp. 533-546
    • Clark-Maguire, S.1    Mains, P.E.2
  • 12
    • 0028171039 scopus 로고
    • G1 cyclin degradation: The PEST motif of yeast Cln2 is necessary, but not sufficient, for rapid protein turnover
    • Salama, S. R., Hendricks, K. B. & Thorner, J. G1 cyclin degradation: the PEST motif of yeast Cln2 is necessary, but not sufficient, for rapid protein turnover. Mol. Cell. Biol. 14, 7953-7966 (1994).
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7953-7966
    • Salama, S.R.1    Hendricks, K.B.2    Thorner, J.3
  • 13
    • 0033529757 scopus 로고    scopus 로고
    • Ubiquitin-dependent degradation of multiple F-box proteins by an autocatalytic mechanism
    • Galan, J. M. & Peter, M. Ubiquitin-dependent degradation of multiple F-box proteins by an autocatalytic mechanism. Proc. Natl Acad. Sci. USA 96, 9124-9129 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 9124-9129
    • Galan, J.M.1    Peter, M.2
  • 14
    • 0034675922 scopus 로고    scopus 로고
    • The F-box protein Skp2 is a ubiquitylation target of a Cul1-based core ubiquitin ligase complex: Evidence for a role of Cul1 in the suppression of Skp2 expression in quiescent fibroblasts
    • Wirbelauer, C. et al. The F-box protein Skp2 is a ubiquitylation target of a Cul1-based core ubiquitin ligase complex: evidence for a role of Cul1 in the suppression of Skp2 expression in quiescent fibroblasts. EMBO J. 19, 5362-5375 (2000).
    • (2000) EMBO J. , vol.19 , pp. 5362-5375
    • Wirbelauer, C.1
  • 15
    • 0032215237 scopus 로고    scopus 로고
    • Ubiquitination and degradation of the substrate recognition subunits of SCF ubiquitin-protein ligases
    • Zhou, P. & Howley, P. M. Ubiquitination and degradation of the substrate recognition subunits of SCF ubiquitin-protein ligases. Mol. Cell 2, 571-580 (1998).
    • (1998) Mol. Cell , vol.2 , pp. 571-580
    • Zhou, P.1    Howley, P.M.2
  • 16
    • 0033535574 scopus 로고    scopus 로고
    • F-box/WD-repeat proteins pop1p and Sud1p/Pop2p form complexes that bind and direct the proteolysis of cdc18p
    • Wolf, D. A., McKeon, F. & Jackson, P. K. F-box/WD-repeat proteins pop1p and Sud1p/Pop2p form complexes that bind and direct the proteolysis of cdc18p. Curr. Biol. 9, 373-376 (1999).
    • (1999) Curr. Biol. , vol.9 , pp. 373-376
    • Wolf, D.A.1    McKeon, F.2    Jackson, P.K.3
  • 17
    • 34248339595 scopus 로고    scopus 로고
    • Combinatorial diversity of fission yeast SCF ubiquitin ligases by homo- and heterooligomeric assemblies of the F-box proteins Pop 1p and Pop2p
    • Seibert, V. et al. Combinatorial diversity of fission yeast SCF ubiquitin ligases by homo- and heterooligomeric assemblies of the F-box proteins Pop1p and Pop2p. BMC Biochem. 3, 1-15 (2002).
    • (2002) BMC Biochem. , vol.3 , pp. 1-15
    • Seibert, V.1
  • 18
    • 0030757226 scopus 로고    scopus 로고
    • Drosophila kelch is an oligomeric ring canal actin organizer
    • Robinson, D. N. & Cooley, L. Drosophila kelch is an oligomeric ring canal actin organizer. J. Cell Biol. 138, 799-810 (1997).
    • (1997) J. Cell Biol. , vol.138 , pp. 799-810
    • Robinson, D.N.1    Cooley, L.2
  • 19
    • 0032816182 scopus 로고    scopus 로고
    • Characterization of Mayven, a novel actin-binding protein predominantly expressed in brain
    • Soltysik-Espanola, M. et al. Characterization of Mayven, a novel actin-binding protein predominantly expressed in brain. Mol. Biol. Cell 10, 2361-2375 (1999).
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2361-2375
    • Soltysik-Espanola, M.1
  • 20
    • 0033763056 scopus 로고    scopus 로고
    • The gene encoding gigaxonin, a new member of the cytoskeletal BTB/kelch repeat family, is mutated in giant axonal neuropathy
    • Bomont, P. et al. The gene encoding gigaxonin, a new member of the cytoskeletal BTB/kelch repeat family, is mutated in giant axonal neuropathy. Nature Genet. 26, 370-374 (2000).
    • (2000) Nature Genet. , vol.26 , pp. 370-374
    • Bomont, P.1
  • 21
    • 0016063911 scopus 로고
    • The genetics of Caenorhabditis elegans
    • Brenner, S. The genetics of Caenorhabditis elegans. Genetics 77, 71-94 (1974).
    • (1974) Genetics , vol.77 , pp. 71-94
    • Brenner, S.1
  • 22
    • 0004270170 scopus 로고
    • Greene Publishing Associates and Wiley-Interscience, New York
    • Ausubel, F. M. et al. Current Protocols in Molecular Biology (Greene Publishing Associates and Wiley-Interscience, New York, 1991).
    • (1991) Current Protocols in Molecular Biology
    • Ausubel, F.M.1
  • 23
    • 0027496935 scopus 로고
    • The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases
    • Harper, J. W., Adami, G. R., Wei, N., Keyomarsi, K. & Elledge, S. J. The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases. Cell 75, 805-816 (1993).
    • (1993) Cell , vol.75 , pp. 805-816
    • Harper, J.W.1    Adami, G.R.2    Wei, N.3    Keyomarsi, K.4    Elledge, S.J.5
  • 25
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • Altschul, S. F. et al. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25, 3389-3402 (1997).
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3389-3402
    • Altschul, S.F.1
  • 26
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G. & Gibson, T. J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680 (1994).
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 27
    • 0141493447 scopus 로고    scopus 로고
    • BTB proteins are substrate-specific adaptors in an SCF-like modular ubiquitin ligase containing CUL-3
    • advance online publication; 3 September (doi:10.10.38/nature01985
    • Xu, L. et al. BTB proteins are substrate-specific adaptors in an SCF-like modular ubiquitin ligase containing CUL-3. Nature advance online publication; 3 September 2003 (doi:10.10.38/nature01985).
    • (2003) Nature
    • Xu, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.