The DOI matches its Crossref record; 58 of the 58 references it cites were found in a registry or an index.
COP9 Signalosome
Open accessAbstract
COP9 Signalosome (CSN) is a fascinating protein complex whose biochemical and physiological functions are only beginning to be understood. It is conserved throughout eukaryotes and is critical to the proper development of all multicellular organisms in which its function has been explored. Recent work suggests that CSN plays a key role in sustaining the activity of SCF and other cullin-based ubiquitin ligases, which may account for its essential roles in development. Here, we summarize what is known about CSN, and discuss hypotheses for how CSN promotes the activity of SCF ubiquitin ligases.
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“Cullin-based ubiquitin ligase activity is stimulated by neddylation (i.e., NEDD8 conjugation) to cullin and downregulated by deneddylation mediated by the COP9 signalosome6,7.”
From Genome-wide screening reveals a role for subcellular localization of CRBN in the anti-myeloma activity of pomalidomide (2020) · cites this paper as [7]
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Cites
Auxin regulates SCFTIR1-dependent degradation of AUX/IAA proteins
Gray, W. M., Kepinski, S., Rouse, D. T., Leyser, O., & Estelle, M. A. (2001) · Nature · doi:10.1038/35104500 · Cited by 1,415
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SCF and Cullin/RING H2-Based Ubiquitin Ligases
Deshaies, R. J. (1999) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.15.1.435 · Cited by 1,238
Self-citationGroisman, R., Polanowska, J., Kuraoka, I., Sawada, J.-I., Saijo, M., Drapkin, R., Kisselev, A. F., Tanaka, K., & Nakatani, Y. (2003) · Cell · doi:10.1016/s0092-8674(03)00316-7 · Cited by 756
Promotion of NEDD8-CUL1 Conjugate Cleavage by COP9 Signalosome
Lyapina, S., Cope, G. A., Shevchenko, A., Serino, G., Tsuge, T., Zhou, C., Wolf, D. A., Wei, N., Shevchenko, A., & Deshaies, R. J. (2001) · Science · doi:10.1126/science.1059780 · Cited by 699
Self-citationRole of Predicted Metalloprotease Motif of Jab1/Csn5 in Cleavage of Nedd8 from Cul1
Cope, G. A., Suh, G. S. B., Aravind, L., Schwarz, S. E., Zipursky, S. L., Koonin, E. V., & Deshaies, R. J. (2002) · Science · doi:10.1126/science.1075901 · Cited by 682
Self-citationDegradation of the cyclin-dependent-kinase inhibitor p27Kip1 is instigated by Jab1
Tomoda, K., Kubota, Y., & Kato, J. (1999) · Nature · doi:10.1038/18230 · Cited by 632
Structure of a β-TrCP1-Skp1-β-Catenin Complex
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The RAR1 Interactor SGT1, an Essential Component of R Gene-Triggered Disease Resistance
Azevedo, C., Sadanandom, A., Kitagawa, K., Freialdenhoven, A., Shirasu, K., & Schulze‐Lefert, P. (2002) · Science · doi:10.1126/science.1067554 · Cited by 611
Intracellular action of the cytokine MIF to modulate AP-1 activity and the cell cycle through Jab1
Kleemann, R., Haußer, A., Geiger, G., Mischke, R., Burger‐Kentischer, A., Flieger, O., Johannes, F., Roger, T., Calandra, T., Kapurniotu, A., et al. (2000) · Nature · doi:10.1038/35041591 · Cited by 567
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Items 401–415 of 415
ANALYSIS OF ELECTROPHILE-INDUCED NRF2 GENE ACTIVATION
Hong, F. (2005) · UA Campus Repository (The University of Arizona)
Zhang, X., Ma, C., Wang, X., Wu, M., Shao, J., Huang, L., Yuan, L., Fu, Z., Li, W., Zhang, X., et al. (2021) · Figshare · doi:10.6084/m9.figshare.14129436
Zhang, X., Ma, C., Wang, X., Wu, M., Shao, J., Huang, L., Yuan, L., Fu, Z., Li, W., Zhang, X., et al. (2021) · Figshare · doi:10.6084/m9.figshare.14129448
Zhang, X., Ma, C., Wang, X., Wu, M., Shao, J., Huang, L., Yuan, L., Fu, Z., Li, W., Zhang, X., et al. (2021) · Figshare · doi:10.6084/m9.figshare.14129445
Zhang, X., Ma, C., Wang, X., Wu, M., Shao, J., Huang, L., Yuan, L., Fu, Z., Li, W., Zhang, X., et al. (2021) · Figshare · doi:10.6084/m9.figshare.14129442
Zhang, X., Ma, C., Wang, X., Wu, M., Shao, J., Huang, L., Yuan, L., Fu, Z., Li, W., Zhang, X., et al. (2021) · Figshare · doi:10.6084/m9.figshare.14129439
The Degradation Pathway of COP9 Signalosome–Cullin-RING Ubiquitin Ligase Complexes via Autophagy
Dubiel, D., Hartig, R., & Dubiel, W. (2026) · Biomolecules · doi:10.3390/biom16020218
Gerlach, I., Koch, M., Gatto, G., Lackmann, J., Lehmann, H. C., Schroeter, M., & Kohle, F. (2026) · Acta Neuropathologica Communications · doi:10.1186/s40478-026-02277-z
Study of the role of neddylation in the regulation of meiotic recombination
Tagliaro-Jahns, M. (2014) · theses.fr (ABES) · doi:10.70675/3d413e8bz3772z4ba9z8582z8698e585ff46
Regulation of proteotoxicity through atypical NEDDylation
Maghames, C. M. (2016) · theses.fr (ABES) · doi:10.70675/f67a0612z3cccz46b5zb058zebfbc60f1ac4
Yamanaka, S., Nagaoka, K., Shoya, Y., Nishino, K., Mikura, Y., Tanaka, K., Konishi, K., Hasegawa, Y., Hijikata, A., Kosako, H., et al. (2026) · Molecular Cell · doi:10.1016/j.molcel.2026.03.004 · Cited by 1
TCTP and CSN4 interact to control cell cycle progression and development in Arabidopsis thaliana
Betsch, L. (2017) · theses.fr (ABES) · doi:10.70675/42cb6fcfze078z4cf3zacc3zc1312590fc21
The COP9 signalosome subunit CSN1 regulates glioblastoma stem cell growth
Assaf, S., Heemskerk, K., Hao, X., Luchman, H. A., & Weiss, S. (2026) · PLoS ONE · doi:10.1371/journal.pone.0358568
Weiss, G. E., Wang, X., March, N. L., Spencer, C., Hickey, B., & Voronina, E. (2026) · Genetics · doi:10.1093/genetics/iyag241
Metadata
- Authors
- Cope, G. A., & Deshaies, R. J.
- Affiliations
- California Institute of Technology (US)
- Corresponding author
- Deshaies, Raymond J
- ORCID
- Deshaies, Raymond J
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2003-09
- Volume
- 114
- Issue
- 6
- Pages
- 663-671
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W1541556706
- Cited by
- 409
- References
- 58
- Citations by year
- 2026: 10 · 2025: 6 · 2024: 8 · 2023: 11 · 2022: 9 · 2021: 16 · 2020: 24 · 2019: 14 · 2018: 13 · 2017: 13 · 2016: 12 · 2015: 12 · 2014: 19 · 2013: 21 · 2012: 23
- FWCI
- 2.29
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- COP9 signalosome, SCF ubiquitin ligase, protein complexes, ubiquitination, multicellular development, eukaryotic evolution
- MeSH terms
- COP9 Signalosome Complex, Animals, Cell Differentiation, Cysteine Endopeptidases, Eukaryotic Cells, Humans, Multienzyme Complexes, Peptide Hydrolases, Peptide Synthases, Proteins, Ubiquitin, SKP Cullin F-Box Protein Ligases, Multiprotein Complexes, Proteasome Endopeptidase Complex
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