메뉴 건너뛰기




Volumn 4, Issue , 2013, Pages

CSN-and CAND1-dependent remodelling of the budding yeast SCF complex

Author keywords

[No Author keywords available]

Indexed keywords

CARBON; COP9 SIGNALOSOME; CULLIN ASSOCIATED NEDD8 DISSOCIATED 1 PROTEIN; CULLIN RING LIGASE; FUNGAL PROTEIN; MULTIPROTEIN COMPLEX; SKP1 CDC53 F BOX PROTEIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 84875768399     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms2628     Document Type: Article
Times cited : (92)

References (49)
  • 1
    • 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
  • 2
    • 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
  • 3
    • 0023802469 scopus 로고
    • The resolution and characterization of putative ubiquitin carrier protein isozymes from rabbit reticulocytes
    • Haas, A. L. & Bright, P. M. The resolution and characterization of putative ubiquitin carrier protein isozymes from rabbit reticulocytes. J. Biol. Chem. 263, 13258-13267 (1988).
    • (1988) J. Biol. Chem , vol.263 , pp. 13258-13267
    • Haas, A.L.1    Bright, P.M.2
  • 4
    • 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
  • 6
    • 9644273891 scopus 로고    scopus 로고
    • A hitchhiker's guide to the cullin ubiquitin ligases: SCF and its kin
    • DOI 10.1016/j.bbamcr.2004.09.027, PII S0167488904002459, The Ubiquitin-Proteasome System
    • Willems, A. R., Schwab, M. & Tyers, M. A hitchhiker's guide to the cullin ubiquitin ligases: SCF and its kin. Biochim. Biophys. Acta 1695, 133-170 (2004). (Pubitemid 39574971)
    • (2004) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1695 , Issue.1-3 , pp. 133-170
    • Willems, A.R.1    Schwab, M.2    Tyers, M.3
  • 7
    • 11244351579 scopus 로고    scopus 로고
    • Function and regulation of cullin-RING ubiquitin ligases
    • DOI 10.1038/nrm1547
    • Petroski, M. D. & Deshaies, R. J. Function and regulation of cullin-RING ubiquitin ligases. Nat. Rev. Mol. Cell Biol. 6, 9-20 (2005). (Pubitemid 40064895)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.1 , pp. 9-20
    • Petroski, M.D.1    Deshaies, R.J.2
  • 9
    • 0032522382 scopus 로고    scopus 로고
    • A novel protein modification pathway related to the ubiquitin system
    • DOI 10.1093/emboj/17.8.2208
    • Liakopoulos, D., Doenges, G. & Matuschewski, K. A novel protein modification pathway related to the ubiquitin system. EMBO J. 17, 2208-2214 (1998). (Pubitemid 28171906)
    • (1998) EMBO Journal , vol.17 , Issue.8 , pp. 2208-2214
    • Liakopoulos, D.1    Doenges, G.2    Matuschewski, K.3    Jentsch, S.4
  • 11
    • 0033581899 scopus 로고    scopus 로고
    • Covalent modification of all members of human cullin family proteins by NEDD8
    • Hori, T. et al. Covalent modification of all members of human cullin family proteins by NEDD8. Oncogene 18, 6829-6834 (1999).
    • (1999) Oncogene , vol.18 , pp. 6829-6834
    • Hori, T.1
  • 12
    • 0942301187 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae ubiquitin-like protein Rub1 conjugates to cullin proteins Rtt101 and Cul3 in vivo
    • DOI 10.1042/BJ20030755
    • Laplaza, J. M., Bostick, M., Scholes, D. T., Curcio, M. J. & Callis, J. Saccharomyces cerevisiae ubiquitin-like protein Rub1 conjugates to cullin proteins Rtt101 and Cul3 in vivo. Biochem. J. 377, 459-467 (2004). (Pubitemid 38142201)
    • (2004) Biochemical Journal , vol.377 , Issue.2 , pp. 459-467
    • Laplaza, J.M.1    Bostick, M.2    Scholes, D.T.3    Curcio, M.J.4    Callis, J.5
  • 13
    • 50449108516 scopus 로고    scopus 로고
    • Structural insights into NEDD8 activation of cullin-RING ligases: Conformational control of conjugation
    • Duda, D. M. et al. Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation. Cell 134, 995-1006 (2008).
    • (2008) Cell , vol.134 , pp. 995-1006
    • Duda, D.M.1
  • 16
    • 1542713819 scopus 로고    scopus 로고
    • The COP9 signalosome: An alternative lid for the 26S proteasome?
    • DOI 10.1016/j.tcb.2003.08.002, PII S0962892403001934
    • Li, L. & Deng, X. W. The COP9 signalosome: an alternative lid for the 26S proteasome? Trends Cell Biol. 13, 507-509 (2003). (Pubitemid 38352692)
    • (2003) Trends in Cell Biology , vol.13 , Issue.10 , pp. 507-509
    • Li, L.1    Deng, X.W.2
  • 19
    • 0037509859 scopus 로고    scopus 로고
    • The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage
    • DOI 10.1016/S0092-8674(03)00316-7
    • Groisman, R. et al. The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage. Cell 113, 357-367 (2003). (Pubitemid 36556117)
    • (2003) Cell , vol.113 , Issue.3 , pp. 357-367
    • Groisman, R.1    Polanowska, J.2    Kuraoka, I.3    Sawada, J.-I.4    Saijo, M.5    Drapkin, R.6    Kisselev, A.F.7    Tanaka, K.8    Nakatani, Y.9
  • 20
    • 0037509945 scopus 로고    scopus 로고
    • Fission yeast COP9/signalosome suppresses cullin activity through recruitment of the deubiquitylating enzyme Ubp12p
    • DOI 10.1016/S1097-2765(03)00136-9
    • Zhou, C. et al. Fission yeast COP9/signalosome suppresses cullin activity through recruitment of the deubiquitylating enzyme Ubp12p. Mol. Cell 11, 927-938 (2003). (Pubitemid 36566315)
    • (2003) Molecular Cell , vol.11 , Issue.4 , pp. 927-938
    • Zhou, C.1    Wee, S.2    Rhee, E.3    Naumann, M.4    Dubiel, W.5    Wolf, D.A.6
  • 22
    • 0035478483 scopus 로고    scopus 로고
    • COP9 signalosome revisited: A novel mediator of protein degradation
    • DOI 10.1016/S0962-8924(01)02091-8, PII S0962892401020918
    • Schwechheimer, C. & Deng, X. W. COP9 signalosome revisited: a novel mediator of protein degradation. Trends Cell Biol. 11, 420-426 (2001). (Pubitemid 32900604)
    • (2001) Trends in Cell Biology , vol.11 , Issue.10 , pp. 420-426
    • Schwechheimer, C.1    Deng, X.-W.2
  • 23
    • 17344364820 scopus 로고    scopus 로고
    • CSN facilitates Cullin-RING ubiquitin ligase function by counteracting autocatalytic adapter instability
    • DOI 10.1038/ncb1241
    • Wee, S., Geyer, R. K., Toda, T. & Wolf, D. A. CSN facilitates Cullin-RING ubiquitin ligase function by counteracting autocatalytic adapter instability. Nat. Cell Biol. 7, 387-391 (2005). (Pubitemid 40533128)
    • (2005) Nature Cell Biology , vol.7 , Issue.4 , pp. 387-391
    • Wee, S.1    Geyer, R.K.2    Toda, T.3    Wolf, D.A.4
  • 24
    • 8344251662 scopus 로고    scopus 로고
    • Structure of the Cand1-Cul1-Roc1 complex reveals regulatory mechanisms for the assembly of the multisubunit cullin-dependent ubiquitin ligases
    • DOI 10.1016/j.cell.2004.10.019, PII S0092867404009535
    • Goldenberg, S. J. et al. Structure of the Cand1-Cul1-Roc1 complex reveals regulatory mechanisms for the assembly of the multisubunit Cullin-dependent ubiquitin ligases. Cell 119, 517-528 (2004). (Pubitemid 39482351)
    • (2004) Cell , vol.119 , Issue.4 , pp. 517-528
    • Goldenberg, S.J.1    Cascio, T.C.2    Shumway, S.D.3    Garbutt, K.C.4    Liu, J.5    Xiong, Y.6    Zheng, N.7
  • 25
    • 0036929129 scopus 로고    scopus 로고
    • CAND1, an inhibitor of CUL1-SKP1 binding and SCF ligases
    • DOI 10.1016/S1097-2765(02)00783-9
    • Liu, J., Furukawa, M., Matsumoto, T. & Xiong, Y. NEDD8 modification of CUL1 dissociates p120CAND1, an inhibitor of CUL1-SKP1 binding and SCF ligases. Mol. Cell 10, 1511-1518 (2002). (Pubitemid 36050891)
    • (2002) Molecular Cell , vol.10 , Issue.6 , pp. 1511-1518
    • Liu, J.1    Furukawa, M.2    Matsumoto, T.3    Xiong, Y.4
  • 27
    • 0037464452 scopus 로고    scopus 로고
    • TIP120A associates with unneddylated cullin 1 and regulates its neddylation
    • DOI 10.1016/S0014-5793(03)00321-1
    • Hwang, J.-W., Min, K.-W., Tamura, T.-A. & Yoon, J.-B. TIP120A associates with unneddylated cullin 1 and regulates its neddylation. FEBS Lett. 541, 102-108 (2003). (Pubitemid 36428926)
    • (2003) FEBS Letters , vol.541 , Issue.1-3 , pp. 102-108
    • Hwang, J.-W.1    Min, K.-W.2    Tamura, T.-A.3    Yoon, J.-B.4
  • 28
    • 77956406531 scopus 로고    scopus 로고
    • C. elegans CAND-1 regulates cullin neddylation, cell proliferation and morphogenesis in specific tissues
    • Bosu, D. R. et al. C. elegans CAND-1 regulates cullin neddylation, cell proliferation and morphogenesis in specific tissues. Dev. Biol. 346, 113-126 (2010).
    • (2010) Dev. Biol , vol.346 , pp. 113-126
    • Bosu, D.R.1
  • 29
    • 3042539802 scopus 로고    scopus 로고
    • AtCAND1, a Heat-repeat protein that participates in auxin signaling in Arabidopsis
    • DOI 10.1104/pp.104.044495
    • Cheng, Y., Dai, X. & Zhao, Y. AtCAND1, a HEAT-repeat protein that participates in auxin signaling in Arabidopsis. Plant Physiol. 135, 1020-1026 (2004). (Pubitemid 38819045)
    • (2004) Plant Physiology , vol.135 , Issue.2 , pp. 1020-1026
    • Cheng, Y.1    Dai, X.2    Zhao, Y.3
  • 30
    • 3142702185 scopus 로고    scopus 로고
    • TIR1 ubiquitin ligase
    • DOI 10.1105/tpc.021923
    • Chuang, H.-W., Zhang, W. & Gray, W. M. Arabidopsis ETA2, an apparent ortholog of the human cullin-interacting protein CAND1, is required for auxin responses mediated by the SCF(TIR1) ubiquitin ligase. Plant Cell 16, 1883-1897 (2004). (Pubitemid 38908782)
    • (2004) Plant Cell , vol.16 , Issue.7 , pp. 1883-1897
    • Chuang, H.-W.1    Zhang, W.2    Gray, W.M.3
  • 31
    • 3142732890 scopus 로고    scopus 로고
    • Arabidopsis CAND1, an unmodified CUL1-interacting protein, is involved in multiple developmental pathways controlled by ubiquitin/proteasome-mediated protein
    • DOI 10.1105/tpc.021949
    • Feng, S. et al. Arabidopsis CAND1, an unmodified CUL1-interacting protein, is involved in multiple developmental pathways controlled by ubiquitin/proteasome-mediated protein degradation. Plant Cell 16, 1870-1882 (2004). (Pubitemid 38908781)
    • (2004) Plant Cell , vol.16 , Issue.7 , pp. 1870-1882
    • Feng, S.1    Shen, Y.2    Sullivan, J.A.3    Rubio, V.4    Xiong, Y.5    Sun, T.-P.6    Deng, X.W.7
  • 32
    • 0141426637 scopus 로고    scopus 로고
    • COP9 signalosome: A multifunctional regulator of SCF and other cullin-based ubiquitin ligases
    • DOI 10.1016/S0092-8674(03)00722-0
    • Cope, G. A. & Deshaies, R. J. COP9 signalosome: a multifunctional regulator of SCF and other cullin-based ubiquitin ligases. Cell 114, 663-671 (2003). (Pubitemid 37186763)
    • (2003) Cell , vol.114 , Issue.6 , pp. 663-671
    • Cope, G.A.1    Deshaies, R.J.2
  • 33
    • 40749153516 scopus 로고    scopus 로고
    • Cullin-RING ubiquitin ligases: Global regulation and activation cycles
    • Bosu, D. R. & Kipreos, E. T. Cullin-RING ubiquitin ligases: global regulation and activation cycles. Cell Div. 3, 7 (2008).
    • (2008) Cell Div , vol.3 , pp. 7
    • Bosu, D.R.1    Kipreos, E.T.2
  • 34
    • 69749123290 scopus 로고    scopus 로고
    • F-box-directed CRL complex assembly and regulation by the CSN and CAND1
    • Schmidt, M. W., McQuary, P. R., Wee, S., Hofmann, K. & Wolf, D. A. F-box-directed CRL complex assembly and regulation by the CSN and CAND1. Mol. Cell 35, 586-597 (2009).
    • (2009) Mol. Cell , vol.35 , pp. 586-597
    • Schmidt, M.W.1    McQuary, P.R.2    Wee, S.3    Hofmann, K.4    Wolf, D.A.5
  • 36
    • 0019187844 scopus 로고
    • Reserve carbohydrate metabolism in Saccharomyces cerevisiae: responses to nutrient limitation
    • Lillie, S. H. & Pringle, J. R. Reserve carbohydrate metabolism in Saccharomyces cerevisiae: responses to nutrient limitation. J. Bacteriol. 143, 1384-1394 (1980). (Pubitemid 11255509)
    • (1980) Journal of Bacteriology , vol.143 , Issue.3 , pp. 1384-1394
    • Lillie, S.H.1    Pringle, J.R.2
  • 38
    • 34447135496 scopus 로고    scopus 로고
    • Substrate-mediated regulation of cullin neddylation
    • DOI 10.1074/jbc.M701153200
    • Chew, E.-H. & Hagen, T. Substrate-mediated regulation of cullin neddylation. J. Biol. Chem. 282, 17032-17040 (2007). (Pubitemid 47093199)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.23 , pp. 17032-17040
    • Chew, E.-H.1    Hagen, T.2
  • 39
    • 81855227619 scopus 로고    scopus 로고
    • The molecular basis of CRL4(DDB2/CSA) ubiquitin ligase architecture, targeting, and activation
    • Fischer, E. S. et al. The molecular basis of CRL4(DDB2/CSA) ubiquitin ligase architecture, targeting, and activation. Cell 147, 1024-1039 (2011).
    • (2011) Cell , vol.147 , pp. 1024-1039
    • Fischer, E.S.1
  • 40
    • 72449198439 scopus 로고    scopus 로고
    • Cullin neddylation and substrate-adaptors counteract SCF inhibition by the CAND1-like protein Lag2 in Saccharomyces cerevisiae
    • Siergiejuk, E. et al. Cullin neddylation and substrate-adaptors counteract SCF inhibition by the CAND1-like protein Lag2 in Saccharomyces cerevisiae. EMBO J. 28, 3845-3856 (2009).
    • (2009) EMBO J , vol.28 , pp. 3845-3856
    • Siergiejuk, E.1
  • 41
    • 70350769108 scopus 로고    scopus 로고
    • A longevity protein, Lag2, interacts with SCF complex and regulates SCF function
    • Liu, Y., Mimura, S., Kishi, T. & Kamura, T. A longevity protein, Lag2, interacts with SCF complex and regulates SCF function. EMBO J. 28, 3366-3377 (2009).
    • (2009) EMBO J , vol.28 , pp. 3366-3377
    • Liu, Y.1    Mimura, S.2    Kishi, T.3    Kamura, T.4
  • 42
    • 78649974984 scopus 로고    scopus 로고
    • Dynamics of Cullin-RING ubiquitin ligase network revealed by systematic quantitative proteomics
    • Bennett, E. J., Rush, J., Gygi, S. P. & Harper, J. W. Dynamics of Cullin-RING ubiquitin ligase network revealed by systematic quantitative proteomics. Cell 143, 951-965 (2010).
    • (2010) Cell , vol.143 , pp. 951-965
    • Bennett, E.J.1    Rush, J.2    Gygi, S.P.3    Harper, J.W.4
  • 43
    • 0035052506 scopus 로고    scopus 로고
    • Skp1p and the F-box protein Rcy1p form a non-SCF complex involved in recycling of the SNARE Snc1p in yeast
    • Galan, J. M. et al. Skp1p and the F-box protein Rcy1p form a non-SCF complex involved in recycling of the SNARE Snc1p in yeast. Mol. Cell Biol. 21, 3105-3117 (2001).
    • (2001) Mol. Cell Biol , vol.21 , pp. 3105-3117
    • Galan, J.M.1
  • 44
    • 0030695025 scopus 로고    scopus 로고
    • A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p
    • DOI 10.1016/S0092-8674(00)80404-3
    • Feldman, R. M., Correll, C. C., Kaplan, K. B. & Deshaies, R. J. A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p. Cell 91, 221-230 (1997). (Pubitemid 27456389)
    • (1997) Cell , vol.91 , Issue.2 , pp. 221-230
    • Feldman, R.M.R.1    Correll, C.C.2    Kaplan, K.B.3    Deshaies, R.J.4
  • 45
    • 4744373127 scopus 로고    scopus 로고
    • Grr1 targets in the glucose and amino acid signaling pathways
    • DOI 10.1128/MCB.24.20.8994-9005.2004
    • Spielewoy, N., Flick, K., Kalashnikova, T. I., Walker, J. R. & Wittenberg, C. Regulation and recognition of SCFGrr1 targets in the glucose and amino acid signaling pathways. Mol. Cell Biol. 24, 8994-9005 (2004). (Pubitemid 39313904)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.20 , pp. 8994-9005
    • Spielewoy, N.1    Flick, K.2    Kalashnikova, T.I.3    Walker, J.R.4    Wittenberg, C.5
  • 47
    • 0038414526 scopus 로고    scopus 로고
    • UFO and participates in Arabidopsis flower development
    • DOI 10.1105/tpc.009936
    • Wang, X. et al. The COP9 signalosome interacts with SCF UFO and participates in Arabidopsis flower development. Plant Cell 15, 1071-1082 (2003). (Pubitemid 36579968)
    • (2003) Plant Cell , vol.15 , Issue.5 , pp. 1071-1082
    • Wang, X.1    Feng, S.2    Nakayama, N.3    Crosby, W.L.4    Irish, V.5    Deng, X.W.6    Wei, N.7
  • 48
    • 69749124799 scopus 로고    scopus 로고
    • Resolving the CSN and CAND1 paradoxes
    • Dubiel, W. Resolving the CSN and CAND1 paradoxes. Mol. Cell 35, 547-549 (2009).
    • (2009) Mol. Cell , vol.35 , pp. 547-549
    • Dubiel, W.1
  • 49
    • 84864037626 scopus 로고    scopus 로고
    • The Dac-tag an affinity tag based on penicillin binding protein
    • Lee, D. W. et al. The Dac-tag, an affinity tag based on penicillin binding protein. Anal. Biochem. 428, 64-72 (2012).
    • (2012) Anal. Biochem. , vol.428 , pp. 64-72
    • Lee, D.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.