메뉴 건너뛰기




Volumn 23, Issue 3, 2015, Pages 441-449

Insights into Cullin-RING E3 ubiquitin ligase recruitment: Structure of the VHL-EloBC-Cul2 complex

Author keywords

[No Author keywords available]

Indexed keywords

CULLIN; CULLIN 2; CULLIN 5; ELONGIN B; ELONGIN C; GLUTATHIONE TRANSFERASE; MALTOSE BINDING PROTEIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; VON HIPPEL LINDAU PROTEIN; ELONGIN; PROTEIN BINDING; TRANSCRIPTION FACTOR; VHL PROTEIN, HUMAN;

EID: 84923925542     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2014.12.014     Document Type: Article
Times cited : (57)

References (61)
  • 2
    • 84859482628 scopus 로고    scopus 로고
    • HIV/simian immunodeficiency virus (SIV) accessory virulence factor Vpx loads the host cell restriction factor SAMHD1 onto the E3 ubiquitin ligase complex CRL4DCAF1
    • J. Ahn, C. Hao, J. Yan, M. DeLucia, J. Mehrens, C. Wang, A.M. Gronenborn, and J. Skowronski HIV/simian immunodeficiency virus (SIV) accessory virulence factor Vpx loads the host cell restriction factor SAMHD1 onto the E3 ubiquitin ligase complex CRL4DCAF1 J. Biol. Chem. 287 2012 12550 12558
    • (2012) J. Biol. Chem. , vol.287 , pp. 12550-12558
    • Ahn, J.1    Hao, C.2    Yan, J.3    Delucia, M.4    Mehrens, J.5    Wang, C.6    Gronenborn, A.M.7    Skowronski, J.8
  • 3
    • 33749535905 scopus 로고    scopus 로고
    • Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery
    • S. Angers, T. Li, X.H. Yi, M.J. MacCoss, R.T. Moon, and N. Zheng Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery Nature 443 2006 590 593
    • (2006) Nature , vol.443 , pp. 590-593
    • Angers, S.1    Li, T.2    Yi, X.H.3    Maccoss, M.J.4    Moon, R.T.5    Zheng, N.6
  • 5
    • 61349119266 scopus 로고    scopus 로고
    • The SOCS box encodes a hierarchy of affinities for Cullin5: Implications for ubiquitin ligase formation and cytokine signalling suppression
    • J.J. Babon, J.K. Sabo, J.G. Zhang, N.A. Nicola, and R.S. Norton The SOCS box encodes a hierarchy of affinities for Cullin5: implications for ubiquitin ligase formation and cytokine signalling suppression J. Mol. Biol. 387 2009 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
  • 7
    • 33646733227 scopus 로고    scopus 로고
    • Crystal structure of the SOCS2-elongin C-elongin B complex defines a prototypical SOCS box ubiquitin ligase
    • A.N. Bullock, J.E. Debreczeni, A.M. Edwards, M. Sundstrom, and S. Knapp Crystal structure of the SOCS2-elongin C-elongin B complex defines a prototypical SOCS box ubiquitin ligase Proc. Natl. Acad. Sci. USA 103 2006 7637 7642
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 7637-7642
    • Bullock, A.N.1    Debreczeni, J.E.2    Edwards, A.M.3    Sundstrom, M.4    Knapp, S.5
  • 8
    • 35748984946 scopus 로고    scopus 로고
    • Structure of the SOCS4-ElonginB/C complex reveals a distinct SOCS box interface and the molecular basis for SOCS-dependent EGFR degradation
    • A.N. Bullock, M.C. Rodriguez, J.E. Debreczeni, Z. Songyang, and S. Knapp Structure of the SOCS4-ElonginB/C complex reveals a distinct SOCS box interface and the molecular basis for SOCS-dependent EGFR degradation Structure 15 2007 1493 1504
    • (2007) Structure , vol.15 , pp. 1493-1504
    • Bullock, A.N.1    Rodriguez, M.C.2    Debreczeni, J.E.3    Songyang, Z.4    Knapp, S.5
  • 10
    • 0000192748 scopus 로고
    • An automated-system for microbatch protein crystallization and screening
    • N.E. Chayen, P.D.S. Stewart, D.L. Maeder, and D.M. Blow An automated-system for microbatch protein crystallization and screening J. Appl. Crystallogr. 23 1990 297 302
    • (1990) J. Appl. Crystallogr. , vol.23 , pp. 297-302
    • Chayen, N.E.1    Stewart, P.D.S.2    Maeder, D.L.3    Blow, D.M.4
  • 11
    • 77955405903 scopus 로고    scopus 로고
    • Cytosolic pH is a second messenger for glucose and regulates the PKA pathway through V-ATPase
    • R. Dechant, M. Binda, S.S. Lee, S. Pelet, J. Winderickx, and M. Peter Cytosolic pH is a second messenger for glucose and regulates the PKA pathway through V-ATPase EMBO J. 29 2010 2515 2526
    • (2010) EMBO J. , vol.29 , pp. 2515-2526
    • Dechant, R.1    Binda, M.2    Lee, S.S.3    Pelet, S.4    Winderickx, J.5    Peter, M.6
  • 12
    • 84906101389 scopus 로고    scopus 로고
    • Cytosolic pH regulates cell growth through distinct GTPases, Arf1 and Gtr1, to promote Ras/PKA and TORC1 activity
    • R. Dechant, S. Saad, A.J. Ibanez, and M. Peter Cytosolic pH regulates cell growth through distinct GTPases, Arf1 and Gtr1, to promote Ras/PKA and TORC1 activity Mol. Cell 55 2014 409 421
    • (2014) Mol. Cell , vol.55 , pp. 409-421
    • Dechant, R.1    Saad, S.2    Ibanez, A.J.3    Peter, M.4
  • 16
    • 84908373179 scopus 로고    scopus 로고
    • Structure-guided design and optimization of small molecules targeting the protein-protein interaction between the von Hippel-Lindau (VHL) E3 ubiquitin ligase and the hypoxia inducible factor (HIF) alpha subunit with in vitro nanomolar affinities
    • C. Galdeano, M.S. Gadd, P. Soares, S. Scaffidi, I. Van Molle, I. Birced, S. Hewitt, D.M. Dias, and A. Ciulli Structure-guided design and optimization of small molecules targeting the protein-protein interaction between the von Hippel-Lindau (VHL) E3 ubiquitin ligase and the hypoxia inducible factor (HIF) alpha subunit with in vitro nanomolar affinities J. Med. Chem. 57 2014 8657 8663
    • (2014) J. Med. Chem. , vol.57 , pp. 8657-8663
    • Galdeano, C.1    Gadd, M.S.2    Soares, P.3    Scaffidi, S.4    Van Molle, I.5    Birced, I.6    Hewitt, S.7    Dias, D.M.8    Ciulli, A.9
  • 18
    • 75149124682 scopus 로고    scopus 로고
    • Prolyl hydroxylase domain inhibitors: A route to HIF activation and neuroprotection
    • S.K. Harten, M. Ashcroft, and P.H. Maxwell Prolyl hydroxylase domain inhibitors: a route to HIF activation and neuroprotection Antioxid. Redox Sign. 12 2010 459 480
    • (2010) Antioxid. Redox Sign. , vol.12 , pp. 459-480
    • Harten, S.K.1    Ashcroft, M.2    Maxwell, P.H.3
  • 22
    • 70849099495 scopus 로고    scopus 로고
    • The extracellular matrix: Not just pretty fibrils
    • R.O. Hynes The extracellular matrix: not just pretty fibrils Science 326 2009 1216 1219
    • (2009) Science , vol.326 , pp. 1216-1219
    • Hynes, R.O.1
  • 24
    • 0036718539 scopus 로고    scopus 로고
    • Molecular basis of the VHL hereditary cancer syndrome
    • W.G. Kaelin Jr. Molecular basis of the VHL hereditary cancer syndrome Nat. Rev. Cancer 2 2002 673 682
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 673-682
    • Kaelin, Jr.W.G.1
  • 25
    • 54549113030 scopus 로고    scopus 로고
    • The von Hippel-Lindau tumour suppressor protein: O-2 sensing and cancer
    • W.G. Kaelin The von Hippel-Lindau tumour suppressor protein: O-2 sensing and cancer Nat. Rev. Cancer 8 2008 865 873
    • (2008) Nat. Rev. Cancer , vol.8 , pp. 865-873
    • Kaelin, W.G.1
  • 27
  • 29
    • 32944464205 scopus 로고    scopus 로고
    • Characterization of a von Hippel Lindau pathway involved in extracellular matrix remodeling, cell invasion, and angiogenesis
    • G. Kurban, V. Hudon, E. Duplan, N. Ohh, and A. Pause Characterization of a von Hippel Lindau pathway involved in extracellular matrix remodeling, cell invasion, and angiogenesis Cancer Res. 66 2006 1313 1319
    • (2006) Cancer Res. , vol.66 , pp. 1313-1319
    • Kurban, G.1    Hudon, V.2    Duplan, E.3    Ohh, N.4    Pause, A.5
  • 30
    • 84893662498 scopus 로고    scopus 로고
    • Electron density sharpening as a general technique in crystallographic studies
    • C. Liu, and Y. Xiong Electron density sharpening as a general technique in crystallographic studies J. Mol. Biol. 426 2014 980 993
    • (2014) J. Mol. Biol. , vol.426 , pp. 980-993
    • Liu, C.1    Xiong, Y.2
  • 31
    • 0031907152 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible mRNAs by the von Hippel-Lindau tumor suppressor protein requires binding to complexes containing elongins B/C and Cul2
    • K.M. Lonergan, O. Iliopoulos, M. Ohh, T. Kamura, R.C. Conaway, J.W. Conaway, and W.G. Kaelin Jr. Regulation of hypoxia-inducible mRNAs by the von Hippel-Lindau tumor suppressor protein requires binding to complexes containing elongins B/C and Cul2 Mol. Cell Biol. 18 1998 732 741
    • (1998) Mol. Cell Biol. , vol.18 , pp. 732-741
    • Lonergan, K.M.1    Iliopoulos, O.2    Ohh, M.3    Kamura, T.4    Conaway, R.C.5    Conaway, J.W.6    Kaelin, Jr.W.G.7
  • 34
    • 33745225450 scopus 로고    scopus 로고
    • A zinc-binding region in Vif binds Cul5 and determines cullin selection
    • A. Mehle, E.R. Thomas, K.S. Rajendran, and D. Gabuzda A zinc-binding region in Vif binds Cul5 and determines cullin selection J. Biol. Chem. 281 2006 17259 17265
    • (2006) J. Biol. Chem. , vol.281 , pp. 17259-17265
    • Mehle, A.1    Thomas, E.R.2    Rajendran, K.S.3    Gabuzda, D.4
  • 35
    • 0037035851 scopus 로고    scopus 로고
    • Structure of an HIF-1 alpha-pVHL complex: Hydroxyproline recognition in signaling
    • J.H. Min, H.F. Yang, M. Ivan, F. Gertler, W.G. Kaelin, and N.P. Pavletich Structure of an HIF-1 alpha-pVHL complex: hydroxyproline recognition in signaling Science 296 2002 1886 1889
    • (2002) Science , vol.296 , pp. 1886-1889
    • Min, J.H.1    Yang, H.F.2    Ivan, M.3    Gertler, F.4    Kaelin, W.G.5    Pavletich, N.P.6
  • 36
    • 79953649414 scopus 로고    scopus 로고
    • HIF prolyl hydroxylase inhibitors for anemia
    • E. Muchnik, and J. Kaplan HIF prolyl hydroxylase inhibitors for anemia Expert Opin. Inv. Drug 20 2011 645 656
    • (2011) Expert Opin. Inv. Drug , vol.20 , pp. 645-656
    • Muchnik, E.1    Kaplan, J.2
  • 40
  • 41
    • 84865610131 scopus 로고    scopus 로고
    • Hypoxia-inducible factor as a therapeutic target for cardioprotection
    • S.G. Ong, and D.J. Hausenloy Hypoxia-inducible factor as a therapeutic target for cardioprotection Pharmacol. Ther. 136 2012 69 81
    • (2012) Pharmacol. Ther. , vol.136 , pp. 69-81
    • Ong, S.G.1    Hausenloy, D.J.2
  • 42
    • 84866648366 scopus 로고    scopus 로고
    • Genome-wide analysis of intracellular pH reveals quantitative control of cell division rate by pH(c) in Saccharomyces cerevisiae
    • R. Orij, M.L. Urbanus, F.J. Vizeacoumar, G. Giaever, C. Boone, C. Nislow, S. Brul, and G.J. Smits Genome-wide analysis of intracellular pH reveals quantitative control of cell division rate by pH(c) in Saccharomyces cerevisiae Genome Biol. 13 2012 R80
    • (2012) Genome Biol. , vol.13 , pp. R80
    • Orij, R.1    Urbanus, M.L.2    Vizeacoumar, F.J.3    Giaever, G.4    Boone, C.5    Nislow, C.6    Brul, S.7    Smits, G.J.8
  • 43
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor 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
  • 44
    • 0030953635 scopus 로고    scopus 로고
    • The von Hippel-Lindau tumor-suppressor gene product forms a stable complex with human CUL-2, a member of the Cdc53 family of proteins
    • A. Pause, S. Lee, R.A. Worrell, D.Y. Chen, W.H. Burgess, W.M. Linehan, and R.D. Klausner The von Hippel-Lindau tumor-suppressor gene product forms a stable complex with human CUL-2, a member of the Cdc53 family of proteins Proc. Natl. Acad. Sci. USA 94 1997 2156 2161
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2156-2161
    • Pause, A.1    Lee, S.2    Worrell, R.A.3    Chen, D.Y.4    Burgess, W.H.5    Linehan, W.M.6    Klausner, R.D.7
  • 45
    • 0033578405 scopus 로고    scopus 로고
    • Studying interactions of four proteins in the yeast two-hybrid system: Structural resemblance of the pVHL/elongin BC/hCUL-2 complex with the ubiquitin ligase complex SKP1/cullin/F-box protein
    • A. Pause, B. Peterson, G. Schaffar, R. Stearman, and R.D. Klausner Studying interactions of four proteins in the yeast two-hybrid system: structural resemblance of the pVHL/elongin BC/hCUL-2 complex with the ubiquitin ligase complex SKP1/cullin/F-box protein Proc. Natl. Acad. Sci. USA 96 1999 9533 9538
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 9533-9538
    • Pause, A.1    Peterson, B.2    Schaffar, G.3    Stearman, R.4    Klausner, R.D.5
  • 46
    • 0029983371 scopus 로고    scopus 로고
    • T7 vectors with a modified T7lac promoter for expression of proteins in Escherichia coli
    • J. Peranen, M. Rikkonen, M. Hyvonen, and L. Kaariainen T7 vectors with a modified T7lac promoter for expression of proteins in Escherichia coli Anal. Biochem. 236 1996 371 373
    • (1996) Anal. Biochem. , vol.236 , pp. 371-373
    • Peranen, J.1    Rikkonen, M.2    Hyvonen, M.3    Kaariainen, L.4
  • 47
    • 11244351579 scopus 로고    scopus 로고
    • Function and regulation of Cullin-RING ubiquitin ligases
    • M.D. Petroski, and R.J. Deshaies Function and regulation of Cullin-RING ubiquitin ligases Nat. Rev. Mol. Cell Biol. 6 2005 9 20
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 9-20
    • Petroski, M.D.1    Deshaies, R.J.2
  • 48
    • 84890449252 scopus 로고    scopus 로고
    • Inhibition of hypoxia-inducible factor prolyl hydroxylase domain oxygen sensors: Tricking the body into mounting orchestrated survival and repair responses
    • M.H. Rabinowitz Inhibition of hypoxia-inducible factor prolyl hydroxylase domain oxygen sensors: tricking the body into mounting orchestrated survival and repair responses J. Med. Chem. 56 2013 9369 9402
    • (2013) J. Med. Chem. , vol.56 , pp. 9369-9402
    • Rabinowitz, M.H.1
  • 49
    • 43049141895 scopus 로고    scopus 로고
    • NEDD8 acts as a 'molecular switch' defining the functional selectivity of VHL
    • R.C. Russell, and M. Ohh NEDD8 acts as a 'molecular switch' defining the functional selectivity of VHL EMBO Rep. 9 2008 486 491
    • (2008) EMBO Rep. , vol.9 , pp. 486-491
    • Russell, R.C.1    Ohh, M.2
  • 51
    • 50149097544 scopus 로고    scopus 로고
    • Structural insight into the human immunodeficiency virus Vif SOCS box and its role in human E3 ubiquitin ligase assembly
    • B.J. Stanley, E.S. Ehrlich, L. Short, Y. Yu, Z. Xiao, X.F. Yu, and Y. Xiong Structural insight into the human immunodeficiency virus Vif SOCS box and its role in human E3 ubiquitin ligase assembly J. Virol. 82 2008 8656 8663
    • (2008) J. Virol. , vol.82 , pp. 8656-8663
    • Stanley, B.J.1    Ehrlich, E.S.2    Short, L.3    Yu, Y.4    Xiao, Z.5    Yu, X.F.6    Xiong, Y.7
  • 52
    • 0033574737 scopus 로고    scopus 로고
    • Structure of the VHL-Elonginc-ElonginB complex: Implications for VHL tumor suppressor function
    • C.E. Stebbins, W.G. Kaelin, and N.P. Pavletich Structure of the VHL-Elonginc-ElonginB complex: implications for VHL tumor suppressor function Science 284 1999 455 461
    • (1999) Science , vol.284 , pp. 455-461
    • Stebbins, C.E.1    Kaelin, W.G.2    Pavletich, N.P.3
  • 53
    • 1842557655 scopus 로고    scopus 로고
    • PVHL modification by NEDD8 is required for fibronectin matrix assembly and suppression of tumor development
    • N.H. Stickle, J. Chung, J.M. Klco, R.P. Hill, W.G. Kaelin, and M. Ohh PVHL modification by NEDD8 is required for fibronectin matrix assembly and suppression of tumor development Mol. Cell Biol. 24 2004 3251 3261
    • (2004) Mol. Cell Biol. , vol.24 , pp. 3251-3261
    • Stickle, N.H.1    Chung, J.2    Klco, J.M.3    Hill, R.P.4    Kaelin, W.G.5    Ohh, M.6
  • 54
    • 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
    • J.C. Thomas, D. Matak-Vinkovic, I. Van Molle, and A. Ciulli 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 2013 5236 5246
    • (2013) Biochemistry , vol.52 , pp. 5236-5246
    • Thomas, J.C.1    Matak-Vinkovic, D.2    Van Molle, I.3    Ciulli, A.4
  • 56
    • 84868026890 scopus 로고    scopus 로고
    • Dissecting fragment-based lead discovery at the von Hippel-Lindau protein:hypoxia inducible factor 1alpha protein-protein interface
    • I. Van Molle, A. Thomann, D.L. Buckley, E.C. So, S. Lang, C.M. Crews, and A. Ciulli Dissecting fragment-based lead discovery at the von Hippel-Lindau protein:hypoxia inducible factor 1alpha protein-protein interface Chem. Biol. 19 2012 1300 1312
    • (2012) Chem. Biol. , vol.19 , pp. 1300-1312
    • Van Molle, I.1    Thomann, A.2    Buckley, D.L.3    So, E.C.4    Lang, S.5    Crews, C.M.6    Ciulli, A.7
  • 57
    • 33645288545 scopus 로고    scopus 로고
    • Structural and functional insights into the B30.2/SPRY domain
    • J.S. Woo, J.H. Imm, C.K. Min, K.J. Kim, S.S. Cha, and B.H. Oh Structural and functional insights into the B30.2/SPRY domain EMBO J. 25 2006 1353 1363
    • (2006) EMBO J. , vol.25 , pp. 1353-1363
    • Woo, J.S.1    Imm, J.H.2    Min, C.K.3    Kim, K.J.4    Cha, S.S.5    Oh, B.H.6
  • 58
    • 33646866382 scopus 로고    scopus 로고
    • Assembly of HIV-1 Vif-Cul5 E3 ubiquitin ligase through a novel zinc-binding domain-stabilized hydrophobic interface in Vif
    • Z. Xiao, E. Ehrlich, Y. Yu, K. Luo, T. Wang, C. Tian, and X.F. Yu Assembly of HIV-1 Vif-Cul5 E3 ubiquitin ligase through a novel zinc-binding domain-stabilized hydrophobic interface in Vif Virology 349 2006 290 299
    • (2006) Virology , vol.349 , pp. 290-299
    • Xiao, Z.1    Ehrlich, E.2    Yu, Y.3    Luo, K.4    Wang, T.5    Tian, C.6    Yu, X.F.7
  • 59
    • 0242578406 scopus 로고    scopus 로고
    • Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex
    • X. Yu, Y. Yu, B. Liu, K. Luo, W. Kong, P. Mao, and X.F. Yu Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex Science 302 2003 1056 1060
    • (2003) Science , vol.302 , pp. 1056-1060
    • Yu, X.1    Yu, Y.2    Liu, B.3    Luo, K.4    Kong, W.5    Mao, P.6    Yu, X.F.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.