메뉴 건너뛰기




Volumn 290, Issue 7, 2015, Pages 4178-4191

Biophysical studies on interactions and assembly of full-size E3 ubiquitin ligase: Suppressor of cytokine signaling 2 (SOCS2)-elongin Bc-cullin 5-ring box protein 2 (RBX2)

Author keywords

[No Author keywords available]

Indexed keywords

MASS SPECTROMETRY;

EID: 84922772904     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.616664     Document Type: Article
Times cited : (28)

References (55)
  • 3
    • 0030695025 scopus 로고    scopus 로고
    • A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p
    • Feldman, R. M., Correll, C. C., Kaplan, K. B., and Deshaies, R. J. (1997) A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p. Cell 91, 221-230
    • (1997) Cell , vol.91 , pp. 221-230
    • Feldman, R.M.1    Correll, C.C.2    Kaplan, K.B.3    Deshaies, R.J.4
  • 4
    • 40749153516 scopus 로고    scopus 로고
    • Cullin-RING ubiquitin ligases: Global regulation and activation cycles
    • Bosu, D. R., and Kipreos, E. T. (2008) Cullin-RING ubiquitin ligases: global regulation and activation cycles. Cell Div. 3, 7
    • (2008) Cell Div. , vol.3 , pp. 7
    • Bosu, D.R.1    Kipreos, E.T.2
  • 5
    • 84889084791 scopus 로고    scopus 로고
    • Building and remodelling Cullin-RING E3 ubiquitin ligases
    • Lydeard, J. R., Schulman, B. A., and Harper, J. W. (2013) Building and remodelling Cullin-RING E3 ubiquitin ligases.EMBORep. 14, 1050-1061
    • (2013) EMBORep. , vol.14 , pp. 1050-1061
    • Lydeard, J.R.1    Schulman, B.A.2    Harper, J.W.3
  • 6
    • 78649653568 scopus 로고    scopus 로고
    • Structural assembly of cullin-RING ubiquitin ligase complexes
    • Zimmerman, E. S., Schulman, B. A., and Zheng, N. (2010) Structural assembly of cullin-RING ubiquitin ligase complexes. Curr. Opin. Struct. Biol. 20, 714-721
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 714-721
    • Zimmerman, E.S.1    Schulman, B.A.2    Zheng, N.3
  • 7
    • 10644276385 scopus 로고    scopus 로고
    • VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases
    • Kamura, T., Maenaka, K., Kotoshiba, S., Matsumoto, M., Kohda, D., Conaway, R. C., Conaway, J. W., and Nakayama, K. I. (2004) VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases. Genes Dev. 18, 3055-3065
    • (2004) Genes Dev. , vol.18 , pp. 3055-3065
    • Kamura, T.1    Maenaka, K.2    Kotoshiba, S.3    Matsumoto, M.4    Kohda, D.5    Conaway, R.C.6    Conaway, J.W.7    Nakayama, K.I.8
  • 11
    • 33646733227 scopus 로고    scopus 로고
    • Crystal structure of the SOCS2-elongin C-elongin B complex defines a prototypical SOCS box ubiquitin ligase
    • Bullock, A. N., Debreczeni, J. E., Edwards, A. M., Sundström, M., and Knapp, S. (2006) Crystal structure of the SOCS2-elongin C-elongin B complex defines a prototypical SOCS box ubiquitin ligase. Proc. Natl. Acad. Sci. U.S.A. 103, 7637-7642
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 7637-7642
    • Bullock, A.N.1    Debreczeni, J.E.2    Edwards, A.M.3    Sundström, M.4    Knapp, S.5
  • 12
    • 84881293765 scopus 로고    scopus 로고
    • Structural basis of intersubunit recognition in elongin BC-cullin 5-SOCS box ubiquitin-protein ligase complexes
    • Kim, Y. K., Kwak, M.-J., Ku, B., Suh, H.-Y., Joo, K., Lee, J., Jung, J. U., and Oh, B.-H. (2013) Structural basis of intersubunit recognition in elongin BC-cullin 5-SOCS box ubiquitin-protein ligase complexes. Acta Crystallogr. D 69, 1587-1597
    • (2013) Acta Crystallogr. D , vol.69 , pp. 1587-1597
    • Kim, Y.K.1    Kwak, M.-J.2    Ku, B.3    Suh, H.-Y.4    Joo, K.5    Lee, J.6    Jung, J.U.7    Oh, B.-H.8
  • 13
    • 79251473377 scopus 로고    scopus 로고
    • Will the ubiquitin system furnish as many drug targets as protein kinases?
    • Cohen, P., and Tcherpakov, M. (2010) Will the ubiquitin system furnish as many drug targets as protein kinases? Cell 143, 686-693
    • (2010) Cell , vol.143 , pp. 686-693
    • Cohen, P.1    Tcherpakov, M.2
  • 14
    • 54249104026 scopus 로고    scopus 로고
    • The ubiquitin system, disease, and drug discovery
    • Petroski, M. D. (2008) The ubiquitin system, disease, and drug discovery. BMC Biochem. 10.1186/1471-2091-9-S1-S7
    • (2008) BMC Biochem.
    • Petroski, M.D.1
  • 16
    • 84874995996 scopus 로고    scopus 로고
    • Cullin-RING Ligases as attractive anti-cancer targets
    • Zhao, Y., and Sun, Y. (2013) Cullin-RING Ligases as attractive anti-cancer targets. Curr. Pharm. Des. 19, 3215-3225
    • (2013) Curr. Pharm. Des. , vol.19 , pp. 3215-3225
    • Zhao, Y.1    Sun, Y.2
  • 18
    • 84881234582 scopus 로고    scopus 로고
    • Multimeric complexes among ankyrin-repeat and SOCS-box protein 9 (ASB9), ElonginBC, and Cullin 5: Insights into the structure and assembly of ECS-type Cullin-RING E3 ubiquitin ligases
    • Thomas, J. C., Matak-Vinkovic, D., Van Molle, I., and Ciulli, A. (2013) Multimeric complexes among ankyrin-repeat and SOCS-box protein 9 (ASB9), ElonginBC, and Cullin 5: insights into the structure and assembly of ECS-type Cullin-RING E3 ubiquitin ligases. Biochemistry 52, 5236-5246
    • (2013) Biochemistry , vol.52 , pp. 5236-5246
    • Thomas, J.C.1    Matak-Vinkovic, D.2    Van Molle, I.3    Ciulli, A.4
  • 22
    • 84878106641 scopus 로고    scopus 로고
    • Native ion mobilitymass spectrometry and related methods in structural biology
    • Konijnenberg, A., Butterer, A., and Sobott, F. (2013) Native ion mobilitymass spectrometry and related methods in structural biology. Biochim. Biophys. Acta 1834, 1239-1256
    • (2013) Biochim. Biophys. Acta , vol.1834 , pp. 1239-1256
    • Konijnenberg, A.1    Butterer, A.2    Sobott, F.3
  • 23
    • 78449267576 scopus 로고    scopus 로고
    • Collision cross sections of proteins and their complexes: A calibration framework and database for gas-phase structural biology
    • Bush, M. F., Hall, Z., Giles, K., Hoyes, J., Robinson, C. V., and Ruotolo, B. T. (2010) Collision cross sections of proteins and their complexes: a calibration framework and database for gas-phase structural biology. Anal. Chem. 82, 9557-9565
    • (2010) Anal. Chem. , vol.82 , pp. 9557-9565
    • Bush, M.F.1    Hall, Z.2    Giles, K.3    Hoyes, J.4    Robinson, C.V.5    Ruotolo, B.T.6
  • 24
    • 33748887803 scopus 로고    scopus 로고
    • Structural information from ion mobility measurements: Effects of the long-range potential
    • Mesleh, M. F., Hunter, J. M., Shvartsburg, A. A., Schatz, G. C., and Jarrold, M. F. (1996) Structural information from ion mobility measurements: effects of the long-range potential. J. Phys. Chem. 100, 16082-16086
    • (1996) J. Phys. Chem. , vol.100 , pp. 16082-16086
    • Mesleh, M.F.1    Hunter, J.M.2    Shvartsburg, A.A.3    Schatz, G.C.4    Jarrold, M.F.5
  • 25
    • 0030580028 scopus 로고    scopus 로고
    • An exact hard-spheres scattering model for the mobilities of polyatomic ions
    • Shvartsburg, A. A., and Jarrold, M. F. (1996) An exact hard-spheres scattering model for the mobilities of polyatomic ions. Chem. Phys. Lett. 261, 86-91
    • (1996) Chem. Phys. Lett. , vol.261 , pp. 86-91
    • Shvartsburg, A.A.1    Jarrold, M.F.2
  • 27
    • 50449108516 scopus 로고    scopus 로고
    • Structural insights into NEDD8 activation of cullin- RING ligases: Conformational control of conjugation
    • Duda, D. M., Borg, L. A., Scott, D. C., Hunt, H. W., Hammel, M., and Schulman, B. A. (2008) Structural insights into NEDD8 activation of cullin- RING ligases: conformational control of conjugation. Cell 134, 995-1006
    • (2008) Cell , vol.134 , pp. 995-1006
    • Duda, D.M.1    Borg, L.A.2    Scott, D.C.3    Hunt, H.W.4    Hammel, M.5    Schulman, B.A.6
  • 29
    • 1842591241 scopus 로고    scopus 로고
    • Nedd8 on cullin: Building an expressway to protein destruction
    • Pan, Z.-Q., Kentsis, A., Dias, D. C., Yamoah, K., and Wu, K. (2004) Nedd8 on cullin: building an expressway to protein destruction. Oncogene 23, 1985-1997
    • (2004) Oncogene , vol.23 , pp. 1985-1997
    • Pan, Z.-Q.1    Kentsis, A.2    Dias, D.C.3    Yamoah, K.4    Wu, K.5
  • 30
    • 84868601127 scopus 로고    scopus 로고
    • Core-binding factor β increases the affinity between human Cullin 5 and HIV-1 Vif within an E3 ligase complex
    • Salter, J. D., Lippa, G. M., Belashov, I. A., and Wedekind, J. E. (2012) Core-binding factor β increases the affinity between human Cullin 5 and HIV-1 Vif within an E3 ligase complex. Biochemistry 51, 8702-8704
    • (2012) Biochemistry , vol.51 , pp. 8702-8704
    • Salter, J.D.1    Lippa, G.M.2    Belashov, I.A.3    Wedekind, J.E.4
  • 31
    • 61349119266 scopus 로고    scopus 로고
    • The SOCS box encodes a hierarchy of affinities for Cullin5: Implications for ubiquitin ligase formation and cytokine signalling suppression
    • Babon, J. J., Sabo, J. K., Zhang, J.-G., Nicola, N. A., and Norton, R. S. (2009) The SOCS box encodes a hierarchy of affinities for Cullin5: implications for ubiquitin ligase formation and cytokine signalling suppression. J. Mol. Biol. 387, 162-174
    • (2009) J. Mol. Biol. , vol.387 , pp. 162-174
    • Babon, J.J.1    Sabo, J.K.2    Zhang, J.-G.3    Nicola, N.A.4    Norton, R.S.5
  • 32
    • 0001528720 scopus 로고    scopus 로고
    • Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules
    • Fraczkiewicz, R., and Braun, W. (1998) Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules. J. Comput. Chem. 19, 319-333
    • (1998) J. Comput. Chem. , vol.19 , pp. 319-333
    • Fraczkiewicz, R.1    Braun, W.2
  • 35
    • 0026684671 scopus 로고
    • Use of liquid hydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding from the removal of nonpolar and polar surface from water
    • Spolar, R. S., Livingstone, J. R., and Record, M. T. (1992) Use of liquid hydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding from the removal of nonpolar and polar surface from water. Biochemistry 31, 3947-3955
    • (1992) Biochemistry , vol.31 , pp. 3947-3955
    • Spolar, R.S.1    Livingstone, J.R.2    Record, M.T.3
  • 36
    • 0028820703 scopus 로고
    • Denaturantmvalues and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • Myers, J. K., Pace, C. N., and Scholtz, J. M. (1995) Denaturantmvalues and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4, 2138-2148
    • (1995) Protein Sci. , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 38
    • 0000159569 scopus 로고    scopus 로고
    • Protein structure and the energetics of protein stability
    • Robertson, A. D., and Murphy, K. P. (1997) Protein structure and the energetics of protein stability. Chem. Rev. 97, 1251-1268
    • (1997) Chem. Rev. , vol.97 , pp. 1251-1268
    • Robertson, A.D.1    Murphy, K.P.2
  • 39
    • 0026756702 scopus 로고
    • Thermodynamics of structural stability and cooperative folding behavior in proteins
    • Murphy, K. P., and Freire, E. (1992) Thermodynamics of structural stability and cooperative folding behavior in proteins. Adv. Protein Chem. 43, 313-361
    • (1992) Adv. Protein Chem. , vol.43 , pp. 313-361
    • Murphy, K.P.1    Freire, E.2
  • 41
    • 33749535905 scopus 로고    scopus 로고
    • Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery
    • Angers, S., Li, T., Yi, X., MacCoss, M. J., Moon, R. T., and Zheng, N. (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
  • 43
    • 33947261954 scopus 로고    scopus 로고
    • Characterization of cullin-based E3 ubiquitin ligases in intact mammalian cells: Evidence for cullin dimerization
    • Chew, E.-H., Poobalasingam, T., Hawkey, C. J., and Hagen, T. (2007) Characterization of cullin-based E3 ubiquitin ligases in intact mammalian cells: evidence for cullin dimerization. Cell. Signal. 19, 1071-1080
    • (2007) Cell. Signal. , vol.19 , pp. 1071-1080
    • Chew, E.-H.1    Poobalasingam, T.2    Hawkey, C.J.3    Hagen, T.4
  • 44
    • 33947107495 scopus 로고    scopus 로고
    • The Cullin3 ubiquitin ligase functions as a Nedd8-bound heterodimer
    • Wimuttisuk, W., and Singer, J. D. (2007) The Cullin3 ubiquitin ligase functions as a Nedd8-bound heterodimer. Mol. Biol. Cell 18, 899-909
    • (2007) Mol. Biol. Cell , vol.18 , pp. 899-909
    • Wimuttisuk, W.1    Singer, J.D.2
  • 46
    • 84875741479 scopus 로고    scopus 로고
    • Crystal structure of KLHL3 in complex with Cullin3
    • Ji, A. X., and Privé, G. G. (2013) Crystal structure of KLHL3 in complex with Cullin3. PLoS One 8, e60445
    • (2013) PLoS One , vol.8 , pp. e60445
    • Ji, A.X.1    Privé, G.G.2
  • 51
    • 34248339595 scopus 로고    scopus 로고
    • Combinatorial diversity of fission yeast SCF ubiquitin ligases by homo- and heterooligomeric assemblies of the F-box proteins Pop1p and Pop2p
    • Seibert, V., Prohl, C., Schoultz, I., Rhee, E., Lopez, R., Abderazzaq, K., Zhou, C., and Wolf, D. A. (2002) Combinatorial diversity of fission yeast SCF ubiquitin ligases by homo- and heterooligomeric assemblies of the F-box proteins Pop1p and Pop2p. BMC Biochem. 3, 22
    • (2002) BMC Biochem. , vol.3 , pp. 22
    • Seibert, V.1    Prohl, C.2    Schoultz, I.3    Rhee, E.4    Lopez, R.5    Abderazzaq, K.6    Zhou, C.7    Wolf, D.A.8
  • 52
    • 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., and Jackson, P. K. (1999) 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) Curr. Biol. , vol.9 , pp. 373-376
    • Wolf, D.A.1    McKeon, F.2    Jackson, P.K.3
  • 53
    • 77951552915 scopus 로고    scopus 로고
    • Structural basis of dimerization-dependent ubiquitination by the SCF(Fbx4) ubiquitin ligase
    • Li, Y., and Hao, B. (2010) Structural basis of dimerization-dependent ubiquitination by the SCF(Fbx4) ubiquitin ligase. J. Biol. Chem. 285, 13896-13906
    • (2010) J. Biol. Chem. , vol.285 , pp. 13896-13906
    • Li, Y.1    Hao, B.2
  • 55
    • 84893331326 scopus 로고    scopus 로고
    • Reconstruction of an active SOCS3-based E3 ubiquitin ligase complex in vitro: Identification of the active components and JAK2 and gp130 as substrates
    • Kershaw, N. J., Laktyushin, A., Nicola, N. A., and Babon, J. J. (2014) Reconstruction of an active SOCS3-based E3 ubiquitin ligase complex in vitro: identification of the active components and JAK2 and gp130 as substrates. Growth Factors 32, 1-10
    • (2014) Growth Factors , vol.32 , pp. 1-10
    • Kershaw, N.J.1    Laktyushin, A.2    Nicola, N.A.3    Babon, J.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.