Control of cullin-ring ubiquitin ligase activity by nedd8.
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Summary
How the Nedd8 cycle controls CRL activity and how perturbations of this cycle can lead to disease are reviewed.
- Type
- review
- Published
- 2010-01-01
- Cited by
- 92
- References
- 107
- OpenAlex
- https://openalex.org/W166838764
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:10131334
Keywords
NEDD8, Cullin, Ubiquitin ligase, Ubiquitin, Cell biology
References
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- Structural basis for phosphodependent substrate selection and orientation by the SCFCdc4 ubiquitin ligase.
- Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin ligase.
- The Fbw7 tumor suppressor regulates glycogen synthase kinase 3 phosphorylation-dependent c-Myc protein degradation
- COP9 signalosome: a multifunctional regulator of SCF and other cullin-based ubiquitin ligases.
- Targeted silencing of Jab1/Csn5 in human cells downregulates SCF activity through reduction of F-box protein levels
- Nedd8 Modification of Cul-1 Activates SCFβTrCP-Dependent Ubiquitination of IκBα
- Mechanisms underlying ubiquitination.
- Function and regulation of protein neddylation
- A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p.
- Binding and recognition in the assembly of an active BRCA1/BARD1 ubiquitin-ligase complex
- Certain Pairs of Ubiquitin-conjugating Enzymes (E2s) and Ubiquitin-Protein Ligases (E3s) Synthesize Nondegradable Forked Ubiquitin Chains Containing All Possible Isopeptide Linkages*
- Direct interactions between NEDD8 and ubiquitin E2 conjugating enzymes upregulate cullin-based E3 ligase activity
- CSN facilitates Cullin–RING ubiquitin ligase function by counteracting autocatalytic adapter instability
- Structure of the Jab1/MPN domain and its implications for proteasome function.
- A general approach for investigating enzymatic pathways and substrates for ubiquitin-like modifiers.
- E2-RING expansion of the NEDD8 cascade confers specificity to cullin modification
- The COP9 signalosome regulates the Neurospora circadian clock by controlling the stability of the SCFFWD-1 complex.
- Function and regulation of cullin–RING ubiquitin ligases
- Structure of a Fbw7-Skp1-cyclin E complex: multisite-phosphorylated substrate recognition by SCF ubiquitin ligases.
Cited by
- Radiosensitization of Cancer Cells by Inactivation of Cullin-RING E3 Ubiquitin Ligases.
- TRIAD1 and HHARI bind to and are activated by distinct neddylated Cullin-RING ligase complexes
- Oxygen Sensing by Protozoans: How They Catch Their Breath
- A portrayal of E3 ubiquitin ligases and deubiquitylases in cancer
- Deneddylation and fungal development - Regulation of Nedd8 protein modification by DenA and the COP9 signalosome
- Deneddylase 1 regulates deneddylase activity of the Cop9 signalosome in Drosophila melanogaster
- CSN-associated USP48 confers stability to nuclear NF-κB/RelA by trimming K48-linked Ub-chains.
- Cullin-RING Ligases as Attractive Anti-cancer Targets
- Selective Recruitment of an E2∼Ubiquitin Complex by an E3 Ubiquitin Ligase
- Substrates of IAP ubiquitin ligases identified with a designed orthogonal E3 ligase, the NEDDylator
- Aquaporin-2 Levels in vitro and in vivo are Regulated by VACM-1, a Cul 5 Gene
- Targeting Cullin-RING ligases by MLN4924 induces autophagy via modulating the HIF1-REDD1-TSC1-mTORC1-DEPTOR axis
- Inhibition of a NEDD8 Cascade Restores Restriction of HIV by APOBEC3G
- The Cyclomodulin Cycle Inhibiting Factor (CIF) Alters Cullin Neddylation Dynamics*
- Modification by Ubiquitin-Like Proteins: Significance in Apoptosis and Autophagy Pathways
- Toward understanding ubiquitin-modifying enzymes: from pharmacological targeting to proteomics.
- Global Identification of Modular Cullin-Ring Ligase Substrates
- Assembly of the Elongin A Ubiquitin Ligase Is Regulated by Genotoxic and Other Stresses*
- CRL Ubiquitin Ligases and DNA Damage Response
- Ubiquitin-like protein modifiers and their potential for antiviral and anti-HCV therapy
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- Contents (Volume 16)
- Mechanism of Cullin3 E3 Ubiquitin Ligase Dimerization
- Arabidopsis Has Two Redundant Cullin3 Proteins That Are Essential for Embryo Development and That Interact with RBX1 and BTB Proteins to Form Multisubunit E3 Ubiquitin Ligase Complexes in Vivow⃞