메뉴 건너뛰기




Volumn 11, Issue 1, 2003, Pages 249-259

Conformational flexibility underlies ubiquitin ligation mediated by the WWP1 HECT domain E3 ligase

Author keywords

[No Author keywords available]

Indexed keywords

LIGASE; UBIQUITIN;

EID: 0037249354     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(02)00774-8     Document Type: Article
Times cited : (241)

References (53)
  • 1
    • 0030038464 scopus 로고    scopus 로고
    • Methods used in the structure determination of bovine mitochondrial F1 ATPase
    • Abrahams J.P., Leslie A.G.W. Methods used in the structure determination of bovine mitochondrial F1 ATPase. Acta Crystallogr. D. 52:1996;30-42.
    • (1996) Acta Crystallogr. D , vol.52 , pp. 30-42
    • Abrahams, J.P.1    Leslie, A.G.W.2
  • 3
    • 0032827035 scopus 로고    scopus 로고
    • Rsp5 ubiquitin-protein ligase mediates DNA damage-induced degradation of the large subunit of RNA polymerase II in Saccharomyces cerevisiae
    • Beaudenon S.L., Huacani M.R., Wang G., McDonell D.P., Huibregtse J.M. Rsp5 ubiquitin-protein ligase mediates DNA damage-induced degradation of the large subunit of RNA polymerase II in Saccharomyces cerevisiae. Mol. Cell. Biol. 19:1999;6972-6979.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6972-6979
    • Beaudenon, S.L.1    Huacani, M.R.2    Wang, G.3    McDonell, D.P.4    Huibregtse, J.M.5
  • 4
    • 0034748469 scopus 로고    scopus 로고
    • MHC class I ubiquitylation by a viral PHD/LAP finger protein
    • Boname J.M., Stevenson P.G. MHC class I ubiquitylation by a viral PHD/LAP finger protein. Immunity. 15:2001;627-636.
    • (2001) Immunity , vol.15 , pp. 627-636
    • Boname, J.M.1    Stevenson, P.G.2
  • 6
    • 0035800795 scopus 로고    scopus 로고
    • Lung Krüppel-like factor contains an autoinhibitory domain that regulates its transcriptional activation by binding WWP1, an E3 ubiquitin ligase
    • Conkright M.D., Wani M.A., Lingrel J.B. Lung Krüppel-like factor contains an autoinhibitory domain that regulates its transcriptional activation by binding WWP1, an E3 ubiquitin ligase. J. Biol. Chem. 276:2001;29299-29306.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29299-29306
    • Conkright, M.D.1    Wani, M.A.2    Lingrel, J.B.3
  • 7
    • 0035945349 scopus 로고    scopus 로고
    • A novel class of herpesvirus-encoded membrane-bound E3 ubiquitin ligases regulates endocytosis of proteins involved in immune recognition
    • Coscoy L., Sanchez D.J., Ganem D. A novel class of herpesvirus-encoded membrane-bound E3 ubiquitin ligases regulates endocytosis of proteins involved in immune recognition. J. Cell Biol. 155:2001;1265-1273.
    • (2001) J. Cell Biol. , vol.155 , pp. 1265-1273
    • Coscoy, L.1    Sanchez, D.J.2    Ganem, D.3
  • 8
    • 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. 276:1997;472-494.
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 9
    • 0033279836 scopus 로고    scopus 로고
    • SCF and Cullins/Ring H2-based ubiquitin ligases
    • Deshaies R.J. SCF and Cullins/Ring H2-based ubiquitin ligases. Annu. Rev. Cell Dev. Biol. 15:1999;435-467.
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 435-467
    • Deshaies, R.J.1
  • 10
    • 0031045585 scopus 로고    scopus 로고
    • Preparation of selenomethionyl proteins for phase determination
    • Doublié S. Preparation of selenomethionyl proteins for phase determination. Methods Enzymol. 276:1997;523-530.
    • (1997) Methods Enzymol. , vol.276 , pp. 523-530
    • Doublié, S.1
  • 14
    • 0034255264 scopus 로고    scopus 로고
    • The RING-H2 finger protein APC11 and the E2 enzyme UBC4 are sufficient to ubiquitinate substrates of the anaphase-promoting complex
    • Gmachl M., Gieffers C., Podtelejnikov A.V., Mann M., Peters J.M. The RING-H2 finger protein APC11 and the E2 enzyme UBC4 are sufficient to ubiquitinate substrates of the anaphase-promoting complex. Proc. Natl. Acad. Sci. USA. 97:2000;8973-8978.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8973-8978
    • Gmachl, M.1    Gieffers, C.2    Podtelejnikov, A.V.3    Mann, M.4    Peters, J.M.5
  • 17
    • 0026095584 scopus 로고
    • Determination of macromolecular structures from anomalous diffraction of synchrotron radiation
    • Hendrickson W.A. Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science. 254:1991;51-58.
    • (1991) Science , vol.254 , pp. 51-58
    • Hendrickson, W.A.1
  • 20
    • 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., Howley P.M. A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. Proc. Natl. Acad. Sci. USA. 92:1995;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
  • 22
    • 0035900793 scopus 로고    scopus 로고
    • CHIP is a U-box-dependent E3 ubiquitin ligase: Identification of Hsc70 as a target for ubiquitylation
    • Jiang J., Ballinger C.A., Wu Y., Dai Q., Cyr D.M., Hohfeld J., Patterson C. CHIP is a U-box-dependent E3 ubiquitin ligase. identification of Hsc70 as a target for ubiquitylation J. Biol. Chem. 276:2001;42938-42944.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42938-42944
    • Jiang, J.1    Ballinger, C.A.2    Wu, Y.3    Dai, Q.4    Cyr, D.M.5    Hohfeld, J.6    Patterson, C.7
  • 23
    • 0034266806 scopus 로고    scopus 로고
    • RING finger proteins: Mediators of ubiquitin ligase activity
    • Joazeiro C.A.P., Weissman A.M. RING finger proteins. mediators of ubiquitin ligase activity Cell. 102:2000;549-552.
    • (2000) Cell , vol.102 , pp. 549-552
    • Joazeiro, C.A.P.1    Weissman, A.M.2
  • 24
    • 0033536637 scopus 로고    scopus 로고
    • The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase
    • Joazeiro C.A.P., Wing S.S., Huang H.-K., Leverson J.D., Hunter T., Liu Y.-C. The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase. Science. 286:1999;223-225.
    • (1999) Science , vol.286 , pp. 223-225
    • Joazeiro, C.A.P.1    Wing, S.S.2    Huang, H.-K.3    Leverson, J.D.4    Hunter, T.5    Liu, Y.-C.6
  • 25
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones A.T., Zou J.-Y., Cowan S., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 47:1991;110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, A.T.1    Zou, J.-Y.2    Cowan, S.3    Kjeldgaard, M.4
  • 26
    • 0034517389 scopus 로고    scopus 로고
    • Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGFβ receptor for degradation
    • Kavsak P., Rasmussen R.K., Causing C.G., Bonni S., Zhu H., Thomsen G.H., Wrana J.L. Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGFβ receptor for degradation. Mol. Cell. 6:2000;1365-1375.
    • (2000) Mol. Cell , vol.6 , pp. 1365-1375
    • Kavsak, P.1    Rasmussen, R.K.2    Causing, C.G.3    Bonni, S.4    Zhu, H.5    Thomsen, G.H.6    Wrana, J.L.7
  • 27
    • 0033525589 scopus 로고    scopus 로고
    • A novel ubiquitylation factor, E4, is involved in multiubiquitin chain assembly
    • Koegl M., Hoppe T., Schlenker S., Ulrich H.D., Mayer T.U., Jentsch S. A novel ubiquitylation factor, E4, is involved in multiubiquitin chain assembly. Cell. 96:1999;635-644.
    • (1999) Cell , vol.96 , pp. 635-644
    • Koegl, M.1    Hoppe, T.2    Schlenker, S.3    Ulrich, H.D.4    Mayer, T.U.5    Jentsch, S.6
  • 28
    • 0026244229 scopus 로고
    • MOLSCRIPT. A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT. A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:1991;946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 29
    • 0030908874 scopus 로고    scopus 로고
    • Physical interaction between E2 and Hect E3 enzymes determines functional cooperativity
    • Kumar S., Kao W.H., Howley P.M. Physical interaction between E2 and Hect E3 enzymes determines functional cooperativity. J. Biol. Chem. 272:1997;13548-13554.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13548-13554
    • Kumar, S.1    Kao, W.H.2    Howley, P.M.3
  • 32
    • 0036279167 scopus 로고    scopus 로고
    • The PHD domain of Mekk1 acts as an E3 ubiquitin ligase and mediates ubiquitylation and degradation of ERK1/2
    • Lu Z., Xu S., Joazeiro C., Cobb M.H., Hunter T. The PHD domain of Mekk1 acts as an E3 ubiquitin ligase and mediates ubiquitylation and degradation of ERK1/2. Mol. Cell. 9:2002;945-956.
    • (2002) Mol. Cell , vol.9 , pp. 945-956
    • Lu, Z.1    Xu, S.2    Joazeiro, C.3    Cobb, M.H.4    Hunter, T.5
  • 33
    • 0002705842 scopus 로고
    • A visual protein crystallographic software system for X11/Xview
    • McRee D.E. A visual protein crystallographic software system for X11/Xview. J. Mol. Graph. 10:1992;44-46.
    • (1992) J. Mol. Graph. , vol.10 , pp. 44-46
    • McRee, D.E.1
  • 34
    • 0032991645 scopus 로고    scopus 로고
    • Ubiquitylation of RNA polymerase II large subunit signaled by phosphorylation of carboxy-terminal domain
    • Mitsui A., Sharp P.A. Ubiquitylation of RNA polymerase II large subunit signaled by phosphorylation of carboxy-terminal domain. Proc. Natl. Acad. Sci. USA. 96:1999;6054-6059.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6054-6059
    • Mitsui, A.1    Sharp, P.A.2
  • 36
    • 0032578476 scopus 로고    scopus 로고
    • Physical and functional interactions between the transactivation domain of the hematopoietic transcription factor NF-E2 and WW domains
    • Mosser E.A., Kasanov J.D., Forsberg E.C., Kay B.K., Ney P.A., Bresnick E.H. Physical and functional interactions between the transactivation domain of the hematopoietic transcription factor NF-E2 and WW domains. Biochemistry. 37:1998;13686-13695.
    • (1998) Biochemistry , vol.37 , pp. 13686-13695
    • Mosser, E.A.1    Kasanov, J.D.2    Forsberg, E.C.3    Kay, B.K.4    Ney, P.A.5    Bresnick, E.H.6
  • 37
    • 0030006130 scopus 로고    scopus 로고
    • Pub1 acts as an E6-AP-like protein ubiquitin ligase in the degradation of cdc25
    • Nefsky B., Beach D. Pub1 acts as an E6-AP-like protein ubiquitin ligase in the degradation of cdc25. EMBO J. 15:1996;1301-1312.
    • (1996) EMBO J. , vol.15 , pp. 1301-1312
    • Nefsky, B.1    Beach, D.2
  • 39
    • 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. 276:1997;307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 41
    • 0030863993 scopus 로고    scopus 로고
    • Inhibition of the 26 S proteosome by polyubiquitin chains synthesized to have defined lengths
    • Piotrowski J., Beal R., Hoffman L., Wilkinson K.D., Cohen R.E., Pickart C.M. Inhibition of the 26 S proteosome by polyubiquitin chains synthesized to have defined lengths. J. Biol. Chem. 272:1997;23712-23721.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23712-23721
    • Piotrowski, J.1    Beal, R.2    Hoffman, L.3    Wilkinson, K.D.4    Cohen, R.E.5    Pickart, C.M.6
  • 44
    • 0030781598 scopus 로고    scopus 로고
    • WW (WWP) domains: From structure to function
    • Rotin D. WW (WWP) domains. from structure to function Curr. Top. Microbiol. Immunol. 228:1998;115-133.
    • (1998) Curr. Top. Microbiol. Immunol. , vol.228 , pp. 115-133
    • Rotin, D.1
  • 45
    • 0032524621 scopus 로고    scopus 로고
    • Characterization of human hect domain family members and their interaction with UbcH5 and UbcH7
    • Schwarz S.E., Rosa J.L., Scheffner M. Characterization of human hect domain family members and their interaction with UbcH5 and UbcH7. J. Biol. Chem. 273:1998;12148-12154.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12148-12154
    • Schwarz, S.E.1    Rosa, J.L.2    Scheffner, M.3
  • 47
    • 0034704216 scopus 로고    scopus 로고
    • NeW wrinkles for an old domain
    • Sudol M., Hunter T. NeW wrinkles for an old domain. Cell. 103:2000;1001-1004.
    • (2000) Cell , vol.103 , pp. 1001-1004
    • Sudol, M.1    Hunter, T.2
  • 50
    • 0035875079 scopus 로고    scopus 로고
    • Molecular insights into polyubiquitin chain assembly: Crystal structure of the Mms2/Ubc13 heterodimer
    • VanDemark A.P., Hofmann R.M., Tsui C., Pickart C.M., Wolberger C. Molecular insights into polyubiquitin chain assembly. crystal structure of the Mms2/Ubc13 heterodimer Cell. 105:2001;711-720.
    • (2001) Cell , vol.105 , pp. 711-720
    • VanDemark, A.P.1    Hofmann, R.M.2    Tsui, C.3    Pickart, C.M.4    Wolberger, C.5
  • 51
    • 0035292759 scopus 로고    scopus 로고
    • Themes and variations on ubiquitylation
    • Weissman A.M. 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
  • 52
    • 0033485869 scopus 로고    scopus 로고
    • The E2-E3 interaction in the N-end rule pathway: The RING-H2 finger of E3 is required for the synthesis of multiubiquitin chain
    • Xie Y., Varshavsky A. The E2-E3 interaction in the N-end rule pathway. the RING-H2 finger of E3 is required for the synthesis of multiubiquitin chain EMBO J. 23:1999;6832-6844.
    • (1999) EMBO J. , vol.23 , pp. 6832-6844
    • Xie, Y.1    Varshavsky, A.2
  • 53
    • 0035827707 scopus 로고    scopus 로고
    • A HECT domain E3 enzyme assembles novel polyubiquitin chains
    • You J., Pickart C.M. A HECT domain E3 enzyme assembles novel polyubiquitin chains. J. Biol. Chem. 276:2001;19871-19878.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19871-19878
    • You, J.1    Pickart, C.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.