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Volumn 22, Issue 19, 2003, Pages 5241-5250

Erratum: A conserved catalytic residue in the ubiquitin-conjugating enzyme family (EMBO Journal (2003) 22 (5241-5250) doi: 10.1093/emboj/cdg501);A conserved catalytic residue in the ubiquitin-conjugating enzyme family

Author keywords

Catalytic mechanism; E2; E3; Isopeptide; Ubiquitin

Indexed keywords

ASPARAGINE; LIGASE; UBIQUITIN CONJUGATING ENZYME;

EID: 0141753130     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.emboj.7600513     Document Type: Erratum
Times cited : (157)

References (52)
  • 1
    • 0036177128 scopus 로고    scopus 로고
    • Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1
    • Bernier-Villamor, V., Sampson, D.A., Matunis, M.J. and Lima, C.D. (2002) Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1. Cell, 108, 345-356.
    • (2002) Cell , vol.108 , pp. 345-356
    • Bernier-Villamor, V.1    Sampson, D.A.2    Matunis, M.J.3    Lima, C.D.4
  • 5
    • 0024280501 scopus 로고
    • Dissecting the catalytic triad of a serine protease
    • Carter, P. and Wells, J.A. (1988) Dissecting the catalytic triad of a serine protease. Nature, 332, 564-568.
    • (1988) Nature , vol.332 , pp. 564-568
    • Carter, P.1    Wells, J.A.2
  • 6
    • 0026076015 scopus 로고
    • Isolation of a cDNA encoding a mammalian multi-ubiquitinating enzyme (E2-25K) and overexpression of the functional enzyme in E. coli
    • Chen, Z., Niles, E.G. and Pickart, C.M. (1991) Isolation of a cDNA encoding a mammalian multi-ubiquitinating enzyme (E2-25K) and overexpression of the functional enzyme in E. coli. J. Biol. Chem., 266, 15698-15704.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15698-15704
    • Chen, Z.1    Niles, E.G.2    Pickart, C.M.3
  • 7
    • 0033279836 scopus 로고    scopus 로고
    • SCF and cullin/RING H2-based ubiquitin ligases
    • Deshaies, R.J. (1999) SCF and cullin/RING H2-based ubiquitin ligases. Annu. Rev. Cell Dev. Biol., 15, 435-467.
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 435-467
    • Deshaies, R.J.1
  • 8
    • 0034708458 scopus 로고    scopus 로고
    • Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53
    • Fang, S., Jensen, J.P., Ludwig, R.L., Vousden, K.H. and Weissman, A.M. (2000) Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53. J. Biol. Chem., 275, 8945-8951.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8945-8951
    • Fang, S.1    Jensen, J.P.2    Ludwig, R.L.3    Vousden, K.H.4    Weissman, A.M.5
  • 9
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-Pdb viewer: An environment for comparative protein modeling
    • Guex, N. and Peitsch, M.C. (1997) SWISS-MODEL and the Swiss-Pdb viewer: an environment for comparative protein modeling. Electrophoresis, 18, 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 10
    • 0030772445 scopus 로고    scopus 로고
    • Structure and function of ubiquitin conjugating enzyme E2-25K: The tail is a core-dependent activity element
    • Haldeman, M.T., Xia, G., Kasperek, E.M. and Pickart, C.M. (1997) Structure and function of ubiquitin conjugating enzyme E2-25K: the tail is a core-dependent activity element. Biochemistry, 36, 10526-10537.
    • (1997) Biochemistry , vol.36 , pp. 10526-10537
    • Haldeman, M.T.1    Xia, G.2    Kasperek, E.M.3    Pickart, C.M.4
  • 13
    • 0034253588 scopus 로고    scopus 로고
    • Evolution and function of ubiquitin-like protein-conjugation systems
    • Hochstrasser, M. (2000) Evolution and function of ubiquitin-like protein-conjugation systems. Nat. Cell Biol., 2, E153-E157.
    • (2000) Nat. Cell Biol. , vol.2
    • Hochstrasser, M.1
  • 14
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • Hoege, C., Pfander, B., Moldovan, G.-L., Pyrowolakis, G. and Jentsch, S. (2002) RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature, 419, 135-141.
    • (2002) Nature , vol.419 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.-L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 15
    • 0033525582 scopus 로고    scopus 로고
    • Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair
    • Hofmann, R.M. and Pickart, C.M. (1999) Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair. Cell, 96, 645-653.
    • (1999) Cell , vol.96 , pp. 645-653
    • Hofmann, R.M.1    Pickart, C.M.2
  • 16
    • 0035958926 scopus 로고    scopus 로고
    • In vitro assembly and recognition of Lys-63 polyubiquitin chains
    • Hofmann, R.M. and Pickart, C.M. (2001) In vitro assembly and recognition of Lys-63 polyubiquitin chains. J. Biol. Chem., 276, 27936-27943.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27936-27943
    • Hofmann, R.M.1    Pickart, C.M.2
  • 17
    • 0037184947 scopus 로고    scopus 로고
    • Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde
    • Hu, M., Li, P., Li, M., Li, W., Yao, T., Wu, J.-W., Gu, W., Cohen, R.E. and Shi, Y. (2002) Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde. Cell, 111, 1041-1054.
    • (2002) Cell , vol.111 , pp. 1041-1054
    • Hu, M.1    Li, P.2    Li, M.3    Li, W.4    Yao, T.5    Wu, J.-W.6    Gu, W.7    Cohen, R.E.8    Shi, Y.9
  • 18
    • 0032741446 scopus 로고    scopus 로고
    • Structure of an E6AP-UbcH7 complex: Insights into ubiquitination by the E2-E3 enzyme cascade
    • Huang, L., Kinnucan, E., Wang, G., Beaudenon, S., Howley, P.M., Huibregtse, J.M. and Pavletich, N.P. (1999) Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade. Science, 286, 1321-1326.
    • (1999) Science , vol.286 , pp. 1321-1326
    • Huang, L.1    Kinnucan, E.2    Wang, G.3    Beaudenon, S.4    Howley, P.M.5    Huibregtse, J.M.6    Pavletich, N.P.7
  • 19
    • 0028907874 scopus 로고
    • A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase
    • Huibregtse, J.M., Scheffner, M., Beaudenon, S. and Howley, P.M. (1995) A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. Proc. Natl Acad. Sci. USA, 92, 2563-2567.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2563-2567
    • Huibregtse, J.M.1    Scheffner, M.2    Beaudenon, S.3    Howley, P.M.4
  • 20
    • 0034256031 scopus 로고    scopus 로고
    • Ubiquitin and its kin: How close are the family ties?
    • Jentsch, S. and Pyrowolakis, G. (2000) Ubiquitin and its kin: how close are the family ties? Trends Cell Biol., 10, 335-342.
    • (2000) Trends Cell Biol. , vol.10 , pp. 335-342
    • Jentsch, S.1    Pyrowolakis, G.2
  • 21
    • 0034266806 scopus 로고    scopus 로고
    • RING finger proteins: Mediators of ubiquitin ligase activity
    • Joazeiro, C.A.P. and Weissman, A.M. (2000) RING finger proteins: mediators of ubiquitin ligase activity. Cell, 102, 549-552.
    • (2000) Cell , vol.102 , pp. 549-552
    • Joazeiro, C.A.P.1    Weissman, A.M.2
  • 22
    • 0035929279 scopus 로고    scopus 로고
    • An E3-like factor that promotes SUMO conjugation to the yeast septins
    • Johnson, E.S. and Gupta, A.A. (2001) An E3-like factor that promotes SUMO conjugation to the yeast septins. Cell, 106, 735-744.
    • (2001) Cell , vol.106 , pp. 735-744
    • Johnson, E.S.1    Gupta, A.A.2
  • 23
    • 0031011721 scopus 로고    scopus 로고
    • Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 Å resolution
    • Johnston, S.C., Larsen, C.N., Cook, W.J., Wilkinson, K.D. and Hill, C.P. (1997) Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 Å resolution. EMBO J., 16, 3787-3796.
    • (1997) EMBO J. , vol.16 , pp. 3787-3796
    • Johnston, S.C.1    Larsen, C.N.2    Cook, W.J.3    Wilkinson, K.D.4    Hill, C.P.5
  • 24
    • 0033565867 scopus 로고    scopus 로고
    • Structural basis for the specificity of ubiquitin C-terminal hydrolases
    • Johnston, S.C., Riddle, S.M., Cohen, R.E. and Hill, C.P. (1999) Structural basis for the specificity of ubiquitin C-terminal hydrolases. EMBO J., 18, 3877-3887.
    • (1999) EMBO J. , vol.18 , pp. 3877-3887
    • Johnston, S.C.1    Riddle, S.M.2    Cohen, R.E.3    Hill, C.P.4
  • 25
    • 0034789730 scopus 로고    scopus 로고
    • Involvement of PIAS1 in the sumoylation of tumor suppressor p53
    • Kahyo, T., Nishida, T. and Yasuda, H. (2001) Involvement of PIAS1 in the sumoylation of tumor suppressor p53. Mol. Cell, 8, 713-718.
    • (2001) Mol. Cell , vol.8 , pp. 713-718
    • Kahyo, T.1    Nishida, T.2    Yasuda, H.3
  • 26
    • 0037207126 scopus 로고    scopus 로고
    • The catalytic cycle of biosynthetic thiolase: A conformational journey of an acetyl group through four binding modes and two oxyanion holes
    • Kursula, P., Ojala, J., Lambeir, A.-M. and Wierenga, R.K. (2002) The catalytic cycle of biosynthetic thiolase: a conformational journey of an acetyl group through four binding modes and two oxyanion holes. Biochemistry, 41, 15543-15556.
    • (2002) Biochemistry , vol.41 , pp. 15543-15556
    • Kursula, P.1    Ojala, J.2    Lambeir, A.-M.3    Wierenga, R.K.4
  • 27
    • 0033553532 scopus 로고    scopus 로고
    • Substrate targeting in the ubiquitin system
    • Laney, J.D. and Hochstrasser, M. (1999) Substrate targeting in the ubiquitin system. Cell, 97, 427-430.
    • (1999) Cell , vol.97 , pp. 427-430
    • Laney, J.D.1    Hochstrasser, M.2
  • 28
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the sterochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S. and Thornton, J.M. (1993) PROCHECK: a program to check the sterochemical quality of protein structures. J. Appl. Crystallogr., 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 30
    • 0038579251 scopus 로고    scopus 로고
    • An NMR-based model of the ubiquitin-bound human ubiquitin conjugation complex Mms2-Ubc13. The structural basis for lysine 63 chain synthesis
    • McKenna, S., Moraes, T., Pastushok, L., Ptak, C., Xiao, W., Spyracopoulos, L. and Ellison, M.J. (2003) An NMR-based model of the ubiquitin-bound human ubiquitin conjugation complex Mms2-Ubc13. The structural basis for lysine 63 chain synthesis. J. Biol. Chem., 278, 13151-13158.
    • (2003) J. Biol. Chem. , vol.278 , pp. 13151-13158
    • McKenna, S.1    Moraes, T.2    Pastushok, L.3    Ptak, C.4    Xiao, W.5    Spyracopoulos, L.6    Ellison, M.J.7
  • 31
    • 0034523266 scopus 로고    scopus 로고
    • SUMO-nonclassical ubiquitin
    • Melchior, F. (2000) SUMO-nonclassical ubiquitin. Annu. Rev. Cell Dev. Biol., 16, 591-626.
    • (2000) Annu. Rev. Cell Dev. Biol. , vol.16 , pp. 591-626
    • Melchior, F.1
  • 33
    • 0033638223 scopus 로고    scopus 로고
    • Ulpl-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast
    • Mossessova, E. and Lima, C.D. (2000) Ulpl-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast. Mol. Cell, 5, 865-876.
    • (2000) Mol. Cell , vol.5 , pp. 865-876
    • Mossessova, E.1    Lima, C.D.2
  • 34
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart, C. (2001) Mechanisms underlying ubiquitination. Annu. Rev. Biochem., 70, 503-533.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.1
  • 35
    • 0021996450 scopus 로고
    • Functional heterogeneity of ubiquitin carrier proteins
    • Pickart, C.M. and Rose, I.A. (1985) Functional heterogeneity of ubiquitin carrier proteins. J. Biol. Chem., 260, 1573-1581.
    • (1985) J. Biol. Chem. , vol.260 , pp. 1573-1581
    • Pickart, C.M.1    Rose, I.A.2
  • 36
    • 0037646406 scopus 로고    scopus 로고
    • Rad23 ubiquitin-associated domains (UBA) inhibit 26S proteasome-catalyzed proteolysis by sequestering lysine 48-linked polyubiquitin chains
    • Raasi, S. and Pickart, C.M. (2003) Rad23 ubiquitin-associated domains (UBA) inhibit 26S proteasome-catalyzed proteolysis by sequestering lysine 48-linked polyubiquitin chains. J. Biol. Chem., 278, 8951-8959.
    • (2003) J. Biol. Chem. , vol.278 , pp. 8951-8959
    • Raasi, S.1    Pickart, C.M.2
  • 37
    • 0028673327 scopus 로고
    • Families of cysteine peptidases
    • Rawlings, N.D. and Barrett, A.J. (1994) Families of cysteine peptidases. Methods Enzymol., 244, 461-486.
    • (1994) Methods Enzymol. , vol.244 , pp. 461-486
    • Rawlings, N.D.1    Barrett, A.J.2
  • 38
    • 0041529514 scopus 로고    scopus 로고
    • SUMO modification of STAT1 and its role in PIAS-mediated inhibition of gene activation
    • Rogers, R.S., Horvath, C.M. and Matunis, M.J. (2003) SUMO modification of STAT1 and its role in PIAS-mediated inhibition of gene activation. J. Biol. Chem., 278, 30091-30097.
    • (2003) J. Biol. Chem. , vol.278 , pp. 30091-30097
    • Rogers, R.S.1    Horvath, C.M.2    Matunis, M.J.3
  • 39
    • 0034689773 scopus 로고    scopus 로고
    • Role of NF-κB in p53-mediated programmed cell death
    • Ryan, K.M., Ernst, J.K., Rice, N.R. and Vousden, K.H. (2000) Role of NF-κB in p53-mediated programmed cell death. Nature, 404, 892-897.
    • (2000) Nature , vol.404 , pp. 892-897
    • Ryan, K.M.1    Ernst, J.K.2    Rice, N.R.3    Vousden, K.H.4
  • 40
    • 0028607435 scopus 로고
    • Identification of a human ubiquitin-conjugating enzyme that mediates the E6-AP-dependent ubiquitination of p53
    • Scheffner, M., Huibregtse, J.M. and Howley, P.M. (1994) Identification of a human ubiquitin-conjugating enzyme that mediates the E6-AP-dependent ubiquitination of p53. Proc. Natl Acad. Sci. USA, 91, 8797-8801.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8797-8801
    • Scheffner, M.1    Huibregtse, J.M.2    Howley, P.M.3
  • 41
    • 0028898424 scopus 로고
    • Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade
    • Scheffner, M., Nuber, U. and Huibregtse, J.M. (1995) Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade. Nature, 373, 81-83.
    • (1995) Nature , vol.373 , pp. 81-83
    • Scheffner, M.1    Nuber, U.2    Huibregtse, J.M.3
  • 42
    • 0030772385 scopus 로고    scopus 로고
    • Crystal structure of murine/human Ubc9 provides insight into the variability of the ubiquitin-conjugating system
    • Tong, H., Hateboer, G., Perrakis, A., Bernards, R. and Sixma, T.K. (1997) Crystal structure of murine/human Ubc9 provides insight into the variability of the ubiquitin-conjugating system. J. Biol. Chem., 272, 21381-21387.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21381-21387
    • Tong, H.1    Hateboer, G.2    Perrakis, A.3    Bernards, R.4    Sixma, T.K.5
  • 43
    • 0036463909 scopus 로고    scopus 로고
    • Degradation or maintenance: Actions of the ubiquitin system on eukaryotic chromatin
    • Ulrich, H.D. (2002) Degradation or maintenance: actions of the ubiquitin system on eukaryotic chromatin. Eukaryot. Cell, 1, 1-10.
    • (2002) Eukaryot. Cell , vol.1 , pp. 1-10
    • Ulrich, H.D.1
  • 44
    • 0034600851 scopus 로고    scopus 로고
    • Two RING finger proteins mediate cooperation between ubiquitin-conjugating enzymes in DNA repair
    • Ulrich, H.D. and Jentsch, S. (2000) Two RING finger proteins mediate cooperation between ubiquitin-conjugating enzymes in DNA repair. EMBO J., 19, 3388-3397.
    • (2000) EMBO J. , vol.19 , pp. 3388-3397
    • Ulrich, H.D.1    Jentsch, S.2
  • 46
    • 0035875079 scopus 로고    scopus 로고
    • Molecular insights into polyubiquitin chain assembly: Crystal structure of the Mms2/Ubc13 heterodimer
    • Van Demark, A.P., Hofmann, R.M., Tsui, C., Pickart, C.M. and Wolberger, C. (2001) Molecular insights into polyubiquitin chain assembly: crystal structure of the Mms2/Ubc13 heterodimer. Cell, 105, 711-720.
    • (2001) Cell , vol.105 , pp. 711-720
    • Van Demark, A.P.1    Hofmann, R.M.2    Tsui, C.3    Pickart, C.M.4    Wolberger, C.5
  • 47
    • 0037249354 scopus 로고    scopus 로고
    • Conformational flexibility underlies ubiquitin ligation mediated by the WWP1 HECT domain E3 ligase
    • Verdecia, M.A., Joazeiro, C.A.P., Wells, N.J., Ferrer, J.-L., Bowman, M.E., Hunter, T. and Noel, J.P. (2003) Conformational flexibility underlies ubiquitin ligation mediated by the WWP1 HECT domain E3 ligase. Mol. Cell, 11, 249-259.
    • (2003) Mol. Cell , vol.11 , pp. 249-259
    • Verdecia, M.A.1    Joazeiro, C.A.P.2    Wells, N.J.3    Ferrer, J.-L.4    Bowman, M.E.5    Hunter, T.6    Noel, J.P.7
  • 48
    • 0032513037 scopus 로고    scopus 로고
    • Crystal structure of the Saccharomyces cerevisiae ubiquitin-conjugating enzyme Rad6 at 2.6 Å resolution
    • Worthylake, D.K., Prakash, S., Prakash, L. and Hill, C.P. (1998) Crystal structure of the Saccharomyces cerevisiae ubiquitin-conjugating enzyme Rad6 at 2.6 Å resolution. J. Biol. Chem., 273, 6271-6276.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6271-6276
    • Worthylake, D.K.1    Prakash, S.2    Prakash, L.3    Hill, C.P.4
  • 49
    • 0035827707 scopus 로고    scopus 로고
    • A hect domain E3 enzyme assembles novel polyubiquitin chains
    • You, J. and Pickart, C.M. (2001) A hect domain E3 enzyme assembles novel polyubiquitin chains. J. Biol. Chem., 276, 19871-19878.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19871-19878
    • You, J.1    Pickart, C.M.2
  • 50
    • 0036724599 scopus 로고    scopus 로고
    • Enzymes of the SUMO modification pathway localize to filaments of the nuclear pore complex
    • Zhang, H., Saitoh, H. and Matunis, M.J. (2002) Enzymes of the SUMO modification pathway localize to filaments of the nuclear pore complex. Mol. Cell. Biol., 22, 6498-6508.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6498-6508
    • Zhang, H.1    Saitoh, H.2    Matunis, M.J.3
  • 51
    • 0034682718 scopus 로고    scopus 로고
    • Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases
    • Zheng, N., Wang, P., Jeffrey, P.D. and Pavletich, N.P. (2000) Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases. Cell, 102, 533-539.
    • (2000) Cell , vol.102 , pp. 533-539
    • Zheng, N.1    Wang, P.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 52
    • 18344391432 scopus 로고    scopus 로고
    • Skp2 SCF ubiquitin ligase complex
    • Skp2 SCF ubiquitin ligase complex. Nature, 416, 703-709.
    • (2002) Nature , vol.416 , pp. 703-709
    • Zheng, N.1


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