메뉴 건너뛰기




Volumn 7, Issue 4, 2005, Pages 387-391

CSN facilitates Cullin-RING ubiquitin ligase function by counteracting autocatalytic adapter instability

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; BINDING PROTEIN; CULLIN; UBIQUITIN PROTEIN LIGASE;

EID: 17344364820     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb1241     Document Type: Article
Times cited : (155)

References (27)
  • 1
    • 0141426637 scopus 로고    scopus 로고
    • COP9 signalosome: A multifunctional regulator of SCF and other cullin-based ubiquitin ligases
    • Cope, G. A. & Deshaies, R. J. COP9 signalosome: a multifunctional regulator of SCF and other cullin-based ubiquitin ligases. Cell 114, 663-671 (2003).
    • (2003) Cell , vol.114 , pp. 663-671
    • Cope, G.A.1    Deshaies, R.J.2
  • 2
    • 0345099331 scopus 로고    scopus 로고
    • The COP9 signalosome: An assembly and maintenance platform for cullin ubiquitin ligases?
    • Wolf, D. A., Zhou, C. & Wee, S. The COP9 signalosome: an assembly and maintenance platform for cullin ubiquitin ligases? Nature Cell Biol. 5, 1029-1033 (2003).
    • (2003) Nature Cell Biol. , vol.5 , pp. 1029-1033
    • Wolf, D.A.1    Zhou, C.2    Wee, S.3
  • 4
    • 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
    • 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).
    • (2003) Cell , vol.113 , pp. 357-367
    • Groisman, R.1
  • 5
    • 0037509945 scopus 로고    scopus 로고
    • Fission yeast COP9/signalosome suppresses cullin activity through recruitment of the deubiquitylating enzyme Ubp12p
    • Zhou, C. et al. Fission yeast COP9/signalosome suppresses cullin activity through recruitment of the deubiquitylating enzyme Ubp12p. Mol. Cell 11, 927-938 (2003).
    • (2003) Mol. Cell , vol.11 , pp. 927-938
    • Zhou, C.1
  • 6
    • 0033279836 scopus 로고    scopus 로고
    • SCF and Cullin/Ring H2-based ubiquitin ligases
    • Deshaies, R. J. SCF and Cullin/Ring H2-based ubiquitin ligases. Annu. Rev. Cell Dev. Biol. 15, 435-467 (1999).
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 435-467
    • Deshaies, R.J.1
  • 7
    • 0141493448 scopus 로고    scopus 로고
    • The BTB protein MEL-26 is a substrate-specific adaptor ofthe CUL-3 ubiquitin-ligase
    • Pintard, L. et al. The BTB protein MEL-26 is a substrate-specific adaptor ofthe CUL-3 ubiquitin-ligase. Nature 425, 311-316 (2003).
    • (2003) Nature , vol.425 , pp. 311-316
    • Pintard, L.1
  • 8
    • 0141493447 scopus 로고    scopus 로고
    • BTB proteins are substrate-specific adaptors in an SCF-like modular ubiquitin ligase containing CUL-3
    • Xu, L. et al. BTB proteins are substrate-specific adaptors in an SCF-like modular ubiquitin ligase containing CUL-3. Nature 425, 316-321.
    • Nature , vol.425 , pp. 316-321
    • Xu, L.1
  • 9
    • 0141750416 scopus 로고    scopus 로고
    • BTB/POZ domain proteins are putative substrate adaptors for cullin 3 ubiquitin ligases
    • Geyer, R., Wee, S., Anderson, S., Yates, J. R. I. & Wolf, D. A. BTB/POZ domain proteins are putative substrate adaptors for cullin 3 ubiquitin ligases. Mol. Cell 12, 783-790 (2003).
    • (2003) Mol. Cell , vol.12 , pp. 783-790
    • Geyer, R.1    Wee, S.2    Anderson, S.3    Yates, J.R.I.4    Wolf, D.A.5
  • 10
    • 0033529757 scopus 로고    scopus 로고
    • Ubiquitin-dependent degradation of multiple F-box proteins by an autocatalytic mechanism
    • Galan, J. M. & Peter, M. Ubiquitin-dependent degradation of multiple F-box proteins by an autocatalytic mechanism. Proc. Natl Acad. Sci. USA 96, 9124-9129 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 9124-9129
    • Galan, J.M.1    Peter, M.2
  • 11
    • 0034675922 scopus 로고    scopus 로고
    • The F-box protein Skp2 is a ubiquitylation target of a Cul1-based core ubiquitin ligase complex: Evidence for a role of Cul1 in the suppression of Skp2 expression in quiescent fibroblasts
    • Wirbelauer, C. et al. The F-box protein Skp2 is a ubiquitylation target of a Cul1-based core ubiquitin ligase complex: evidence for a role of Cul1 in the suppression of Skp2 expression in quiescent fibroblasts. EMBO J. 19, 5362-5375 (2000).
    • (2000) EMBO J. , vol.19 , pp. 5362-5375
    • Wirbelauer, C.1
  • 12
    • 0032215237 scopus 로고    scopus 로고
    • Ubiquitination and degradation of the substrate recognition subunits of SCF ubiquitin-protein ligases
    • Zhou, P. & Howley, P. M. Ubiquitination and degradation of the substrate recognition subunits of SCF ubiquitin-protein ligases. Mol. Cell 2, 571-580 (1998).
    • (1998) Mol. Cell , vol.2 , pp. 571-580
    • Zhou, P.1    Howley, P.M.2
  • 13
    • 0034677224 scopus 로고    scopus 로고
    • Feedback-regulated degradation of the transcriptional activator Met4 is triggered by the SCF(Met30) complex
    • Rouillon, A., Barbey, R., Patton, E. E., Tyers, M. & Thomas, D. Feedback-regulated degradation of the transcriptional activator Met4 is triggered by the SCF(Met30) complex. EMBO J. 19, 282-294 (2000).
    • (2000) EMBO J. , vol.19 , pp. 282-294
    • Rouillon, A.1    Barbey, R.2    Patton, E.E.3    Tyers, M.4    Thomas, D.5
  • 14
    • 1842591241 scopus 로고    scopus 로고
    • Nedd8 on cullin: Building an expressway to protein destruction
    • Pan, Z. Q., Kentsis, A., Dias, D. C., Yamoah, K. & Wu, K. Nedd8 on cullin: building an expressway to protein destruction. Oncogene 23, 1985-1997 (2004).
    • (2004) Oncogene , vol.23 , pp. 1985-1997
    • Pan, Z.Q.1    Kentsis, A.2    Dias, D.C.3    Yamoah, K.4    Wu, K.5
  • 15
    • 0035906430 scopus 로고    scopus 로고
    • Promotion of NEDD8-CUL1 conjugate cleavage by COP9 signalosome
    • Lyapina, S. et al. Promotion of NEDD8-CUL1 conjugate cleavage by COP9 signalosome. Science 292, 1382-1385 (2001).
    • (2001) Science , vol.292 , pp. 1382-1385
    • Lyapina, S.1
  • 16
    • 0035907047 scopus 로고    scopus 로고
    • Interactions of the COP9 signalosome with the E3 ubiquitin ligase SCFTIRI in mediating auxin response
    • Schwechheimer, C. et al. Interactions of the COP9 signalosome with the E3 ubiquitin ligase SCFTIRI in mediating auxin response. Science 292, 1379-1382 (2001).
    • (2001) Science , vol.292 , pp. 1379-1382
    • Schwechheimer, C.1
  • 17
    • 3042727952 scopus 로고    scopus 로고
    • The fission yeast COP9/signalosome is involved in cullin modification by ubiquitin-related Ned8p
    • Zhou, C. et al. The fission yeast COP9/signalosome is involved in cullin modification by ubiquitin-related Ned8p. BMC Biochemistry 2, 7 (2001).
    • (2001) BMC Biochemistry , vol.2 , pp. 7
    • Zhou, C.1
  • 18
    • 0037131242 scopus 로고    scopus 로고
    • Role of predicted metalloprotease motif of Jab1/Csn5 in cleavage of NEDD8 from CUL1
    • Cope, G. et al. Role of predicted metalloprotease motif of Jab1/Csn5 in cleavage of NEDD8 from CUL1. Science 298, 608-611 (2002).
    • (2002) Science , vol.298 , pp. 608-611
    • Cope, G.1
  • 19
    • 0036176144 scopus 로고    scopus 로고
    • Deletion mutants in COP9/signalosome subunits in fission yeast Schizosaccharomyces pombe display distinct phenotypes
    • Mundt, K. E., Liu, C. & Carr, A. M. Deletion mutants in COP9/signalosome subunits in fission yeast Schizosaccharomyces pombe display distinct phenotypes. Mol. Biol. Cell 13, 493-502 (2002).
    • (2002) Mol. Biol. Cell , vol.13 , pp. 493-502
    • Mundt, K.E.1    Liu, C.2    Carr, A.M.3
  • 20
    • 0037513423 scopus 로고    scopus 로고
    • Neddylation and deneddylation of CUL-3 is required to target MEI-1/katanin for degradation at the meiosis-to-mitosis transition in C. elegans
    • Pintard, L. et al. Neddylation and deneddylation of CUL-3 is required to target MEI-1/katanin for degradation at the meiosis-to-mitosis transition in C. elegans. Curr. Biol. 13, 911-921 (2003).
    • (2003) Curr. Biol. , vol.13 , pp. 911-921
    • Pintard, L.1
  • 21
    • 0033518297 scopus 로고    scopus 로고
    • The COP9/signalosome complex is conserved in fission yeast and has a role in S phase
    • Mundt, K. E. et al. The COP9/signalosome complex is conserved in fission yeast and has a role in S phase. Curr. Biol. 9, 1427-1430 (1999).
    • (1999) Curr. Biol. , vol.9 , pp. 1427-1430
    • Mundt, K.E.1
  • 22
    • 0032440674 scopus 로고    scopus 로고
    • Two F-box/WD-repeat proteins Pop1 and Pop2 form hetero- and homo- complexes together with cullin-1 in the fission yeast SCF (Skp1-Cullin-1-F-box) ubiquitin ligase
    • Kominami, K., Ochotorena, I. & Toda, T. Two F-box/WD-repeat proteins Pop1 and Pop2 form hetero- and homo- complexes together with cullin-1 in the fission yeast SCF (Skp1-Cullin-1-F-box) ubiquitin ligase. Genes Cells 3, 721-735 (1998).
    • (1998) Genes Cells , vol.3 , pp. 721-735
    • Kominami, K.1    Ochotorena, I.2    Toda, T.3
  • 23
    • 2942659469 scopus 로고    scopus 로고
    • Molecular interactions of fission yeast Skp1 and its role in the DNA damage checkpoint
    • Lehmann, A. et al. Molecular interactions of fission yeast Skp1 and its role in the DNA damage checkpoint. Genes Cells 9, 367-382 (2004).
    • (2004) Genes Cells , vol.9 , pp. 367-382
    • Lehmann, A.1
  • 24
    • 2342500360 scopus 로고    scopus 로고
    • The F-box protein SKP2 mediates androgen control of p27 stability in LNCaP human prostate cancer cells
    • Lu, L., Schulz, H. & Wolf, D. A. The F-box protein SKP2 mediates androgen control of p27 stability in LNCaP human prostate cancer cells. BMC Cell Biol. 3, 22 (2002).
    • (2002) BMC Cell Biol. , vol.3 , pp. 22
    • Lu, L.1    Schulz, H.2    Wolf, D.A.3
  • 25
    • 2942650133 scopus 로고    scopus 로고
    • The Fbw7 tumor suppressor regulates glycogen synthase kinase 3 phosphorylation-dependent c-Myc protein degradation
    • Welcker, M. et al. The Fbw7 tumor suppressor regulates glycogen synthase kinase 3 phosphorylation-dependent c-Myc protein degradation. Proc. Natl Acad. Sci. USA 101, 9085-9090 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 9085-9090
    • Welcker, M.1
  • 26
    • 0141522457 scopus 로고    scopus 로고
    • Release of ubiquitin charged Csc34-A-Ub from the RING domain is essential for ubiquitination of the SCFCdc4-bound substrate Sic1
    • Deffenbaugh, A. E. et al. Release of ubiquitin charged Csc34-A-Ub from the RING domain is essential for ubiquitination of the SCFCdc4-bound substrate Sic1. Cell 114, 611-622 (2003).
    • (2003) Cell , vol.114 , pp. 611-622
    • Deffenbaugh, A.E.1
  • 27
    • 0031818471 scopus 로고    scopus 로고
    • Heterologous modules for efficient and versatile PCR-based gene targeting in Schizosaccharomyces pombe
    • Bahler, J. et al. Heterologous modules for efficient and versatile PCR-based gene targeting in Schizosaccharomyces pombe. Yeast 14, 943-951 (1998).
    • (1998) Yeast , vol.14 , pp. 943-951
    • Bahler, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.