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Volumn 422, Issue 6929, 2003, Pages 330-334

Insights into the ubiquitin transfer cascade from the structure of the activating enzyme for NEDD8

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; CATALYST ACTIVITY; CELLS; MOLECULAR BIOLOGY; PROTEINS;

EID: 0037456828     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature01456     Document Type: Article
Times cited : (189)

References (30)
  • 1
    • 0034725918 scopus 로고    scopus 로고
    • Biochemistry. All in the ubiquitin family
    • Hochstrasser, M. Biochemistry. All in the ubiquitin family. Science 289, 563-564 (2000).
    • (2000) Science , vol.289 , pp. 563-564
    • Hochstrasser, M.1
  • 2
    • 0034256031 scopus 로고    scopus 로고
    • Ubiquitin and its kin: How close are the family ties?
    • Jentsch, S. & Pyrowolakis G. Ubiquitin and its kin: how close are the family ties? Trends Cell Biol. 10, 335-342 (2000).
    • (2000) Trends Cell Biol. , vol.10 , pp. 335-342
    • Jentsch, S.1    Pyrowolakis, G.2
  • 3
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart, C. M. Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70, 503-533 (2001).
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 4
    • 0032053829 scopus 로고    scopus 로고
    • Modification of yeast Cdc53p by the ubiquitin-related protein Rublp affects function of the SCFCdc4 complex
    • Lammer, D. et al. Modification of yeast Cdc53p by the ubiquitin-related protein Rublp affects function of the SCFCdc4 complex. Genes Dev. 12, 914-926 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 914-926
    • Lammer, D.1
  • 5
    • 0032511111 scopus 로고    scopus 로고
    • The ubiquitin-related protein RUBl and auxin response in Arabidopsis
    • Pozo, J. C., Timpte, C., Tan, S., Callis, J. & Estelle, M. The ubiquitin-related protein RUBl and auxin response in Arabidopsis. Science 280, 1760-1763 (1998).
    • (1998) Science , vol.280 , pp. 1760-1763
    • Pozo, J.C.1    Timpte, C.2    Tan, S.3    Callis, J.4    Estelle, M.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
    • 0020478717 scopus 로고
    • Ubiquitin-activating enzyme. Mechanism and role in protein-ubiquitin conjugation
    • Haas, A. L., Warms, J. V., Hershko, A. & Rose, I. A. Ubiquitin-activating enzyme. Mechanism and role in protein-ubiquitin conjugation. J. Biol. Chem. 257, 2543-2548 (1982).
    • (1982) J. Biol. Chem. , vol.257 , pp. 2543-2548
    • Haas, A.L.1    Warms, J.V.2    Hershko, A.3    Rose, I.A.4
  • 8
    • 0020479562 scopus 로고
    • The mechanism of ubiquitin activating enzyme. A kinetic and equilibrium analysis
    • Haas, A. L. & Rose, I. A. The mechanism of ubiquitin activating enzyme. A kinetic and equilibrium analysis. J. Biol. Chem. 257, 10329-10337 (1982).
    • (1982) J. Biol. Chem. , vol.257 , pp. 10329-10337
    • Haas, A.L.1    Rose, I.A.2
  • 9
    • 0021099710 scopus 로고
    • Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown
    • Hershko, A., Heller, H., Elias, S. & Ciechanover, A. Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown. J. Biol. Chem. 258, 8206-8214 (1983).
    • (1983) J. Biol. Chem. , vol.258 , pp. 8206-8214
    • Hershko, A.1    Heller, H.2    Elias, S.3    Ciechanover, A.4
  • 10
    • 0023789174 scopus 로고
    • Functional diversity among putative E2 isozymes in the mechanism of ubiquitin-histone ligation
    • Haas, A. L., Bright, P. M. & Jackson, V. E. Functional diversity among putative E2 isozymes in the mechanism of ubiquitin-histone ligation. J. Biol. Chem. 263, 13268-13275 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 13268-13275
    • Haas, A.L.1    Bright, P.M.2    Jackson, V.E.3
  • 11
    • 0032146145 scopus 로고    scopus 로고
    • A new NEDD8-ligating system for cullin-4A
    • Osaka, F. et al. A new NEDD8-ligating system for cullin-4A. Genes Dev. 12, 2263-2268 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 2263-2268
    • Osaka, F.1
  • 12
    • 0035891318 scopus 로고    scopus 로고
    • Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex
    • Lake, M. W., Wuebbens, M. M., Rajagopalan, K. V. & Schindelin, H. Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex. Nature 414, 325-329 (2001).
    • (2001) Nature , vol.414 , pp. 325-329
    • Lake, M.W.1    Wuebbens, M.M.2    Rajagopalan, K.V.3    Schindelin, H.4
  • 13
    • 0021139080 scopus 로고
    • Thermolability of ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85
    • Finley, D., Ciechanover, A. & Varshavsky, A. Thermolability of ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85. Cell 37, 43-55 (1984).
    • (1984) Cell , vol.37 , pp. 43-55
    • Finley, D.1    Ciechanover, A.2    Varshavsky, A.3
  • 14
    • 0024995885 scopus 로고
    • Cloning of ubiquitin activating enzyme from wheat and expression of a functional protein in Escherichia coli
    • Hatfield, P. M., Callis, J. & Vierstra, R. D. Cloning of ubiquitin activating enzyme from wheat and expression of a functional protein in Escherichia coli. J. Biol. Chem. 265, 15813-15817 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 15813-15817
    • Hatfield, P.M.1    Callis, J.2    Vierstra, R.D.3
  • 15
    • 0030794729 scopus 로고    scopus 로고
    • The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer
    • Johnson, E. S., Schwienhorst, I., Dohmen, R. J. & Blobel, G. The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer. EMBO J. 16, 5509-5519 (1997).
    • (1997) EMBO J. , vol.16 , pp. 5509-5519
    • Johnson, E.S.1    Schwienhorst, I.2    Dohmen, R.J.3    Blobel, G.4
  • 16
    • 0032522382 scopus 로고    scopus 로고
    • A novel protein modification pathway related to the ubiquitin system
    • Liakopoulos, D., Doenges, G., Matuschewski, K. & Jentsch, S. A novel protein modification pathway related to the ubiquitin system. EMBO J. 17, 2208-2214 (1998).
    • (1998) EMBO J. , vol.17 , pp. 2208-2214
    • Liakopoulos, D.1    Doenges, G.2    Matuschewski, K.3    Jentsch, S.4
  • 17
    • 0032567528 scopus 로고    scopus 로고
    • Crystal structure of the human ubiquitin-like protein NEDD 8 and interactions with ubiquitin pathway enzymes
    • Whitby, F. G., Xia, G., Pickart, C. M. & Hill, C. P. Crystal structure of the human ubiquitin-like protein NEDD8 and interactions with ubiquitin pathway enzymes. J. Biol. Chem. 273, 34983-34991 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 34983-34991
    • Whitby, F.G.1    Xia, G.2    Pickart, C.M.3    Hill, C.P.4
  • 19
    • 0030052841 scopus 로고    scopus 로고
    • Surface hydrophobic residues of multiubiquitin chains essential for proteolytic targeting
    • Beal, R., Deveraux, Q., Xia, G., Rechsteiner, M. & Pickart, C. Surface hydrophobic residues of multiubiquitin chains essential for proteolytic targeting. Proc. Natl. Acad. Sci. USA 93, 861-866 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 861-866
    • Beal, R.1    Deveraux, Q.2    Xia, G.3    Rechsteiner, M.4    Pickart, C.5
  • 20
    • 0028308828 scopus 로고
    • Site-directed mutagenesis of ubiquitin. Differential roles for arginine in the interaction with ubiquitin-activating enzyme
    • Burch, T. J. & Haas, A. L. Site-directed mutagenesis of ubiquitin. Differential roles for arginine in the interaction with ubiquitin-activating enzyme. Biochemistry 33, 7300-7308 (1994).
    • (1994) Biochemistry , vol.33 , pp. 7300-7308
    • Burch, T.J.1    Haas, A.L.2
  • 21
    • 0028235968 scopus 로고
    • Substrate properties of site-specific mutant ubiquitin protein (G76A) reveal unexpected mechanistic features of ubiquitin-activating enzyme (E1)
    • Pickart, C. M., Kasperek, E. M., Beal, R. & Kim, A. Substrate properties of site-specific mutant ubiquitin protein (G76A) reveal unexpected mechanistic features of ubiquitin-activating enzyme (E1). J. Biol. Chem. 269, 7115-7123 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 7115-7123
    • Pickart, C.M.1    Kasperek, E.M.2    Beal, R.3    Kim, A.4
  • 22
    • 0032499264 scopus 로고    scopus 로고
    • Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
    • Kitada, T. et al. Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature 392, 605-608 (1998).
    • (1998) Nature , vol.392 , pp. 605-608
    • Kitada, T.1
  • 23
    • 0033574737 scopus 로고    scopus 로고
    • Structure of the VHL-ElonginC-ElonginB complex: Implications for VHL tumour suppressor function
    • Stebbins, C. E., Kaelin, W. G. Jr. & Pavletich, N. P. Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumour 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
  • 24
    • 0037033071 scopus 로고    scopus 로고
    • Identification of a multifunctional binding site on Ubc9p required for Smt3p conjugation
    • Bencsath, K. P., Podgorski, M. S., Pagala, V. R., Slaughter, C. A. & Schulman, B. A. Identification of a multifunctional binding site on Ubc9p required for Smt3p conjugation. J. Biol. Chem. 277, 47938-47945 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 47938-47945
    • Bencsath, K.P.1    Podgorski, M.S.2    Pagala, V.R.3    Slaughter, C.A.4    Schulman, B.A.5
  • 25
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 176, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.176 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 27
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • de la Fortelle, E. & Bricogne, G. Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276, 472-494 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De la Fortelle, E.1    Bricogne, G.2
  • 28
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 29
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brünger, A. T. et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brünger, A.T.1
  • 30
    • 0027358723 scopus 로고
    • The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
    • Scheffner, M., Huibregtse, J. M., Vierstra, R. D. & Howley, P. M. The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. Cell 75, 495-505 (1993).
    • (1993) Cell , vol.75 , pp. 495-505
    • Scheffner, M.1    Huibregtse, J.M.2    Vierstra, R.D.3    Howley, P.M.4


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