Nedd8 on cullin: building an expressway to protein destruction

No abstract is available for this paper.

• Publication year

  2004

• Venue

  Oncogene

• Publication date

  2004-03-15

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1038/sj.onc.1207414PMID 15021886
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• COP9 signalosome: a multifunctional regulator of SCF and other cullin-based ubiquitin ligases.

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• Identification and Characterization of DEN1, a Deneddylase of the ULP Family*

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• BTB/POZ domain proteins are putative substrate adaptors for cullin 3 ubiquitin ligases.

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• Nedd8-modification of Cul1 is promoted by Roc1 as a Nedd8-E3 ligase and regulates its stability.

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• Parc: a cytoplasmic anchor for p53.

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  2003influential reference
• NEDP1, a Highly Conserved Cysteine Protease That deNEDDylates Cullins*

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• The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage.

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• Disruption of the COP9 Signalosome Csn2 Subunit in Mice Causes Deficient Cell Proliferation, Accumulation of p53 and Cyclin E, and Early Embryonic Death

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• Exclusion of germ plasm proteins from somatic lineages by cullin-dependent degradation

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• TIP120A Associates with Cullins and Modulates Ubiquitin Ligase Activity*

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• Targeting of protein ubiquitination by BTB–Cullin 3–Roc1 ubiquitin ligases

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• Insights into the ubiquitin transfer cascade from the structure of the activating enzyme for NEDD8

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• BTB proteins are substrate-specific adaptors in an SCF-like modular ubiquitin ligase containing CUL-3

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• Conservation in the Mechanism of Nedd8 Activation by the Human AppBp1-Uba3 Heterodimer*

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• The BTB protein MEL-26 is a substrate-specific adaptor of the CUL-3 ubiquitin-ligase

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• Doc1 mediates the activity of the anaphase‐promoting complex by contributing to substrate recognition

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• The COP9 signalosome promotes degradation of Cyclin E during early Drosophila oogenesis.

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• Cop9/signalosome subunits and Pcu4 regulate ribonucleotide reductase by both checkpoint-dependent and -independent mechanisms.

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• A Role for Saccharomyces cerevisiae Cul8 Ubiquitin Ligase in Proper Anaphase Progression*

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• Fission yeast COP9/signalosome suppresses cullin activity through recruitment of the deubiquitylating enzyme Ubp12p.

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• COP9 Signalosome Subunit 3 Is Essential for Maintenance of Cell Proliferation in the Mouse Embryonic Epiblast

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• DEN1 Is a Dual Function Protease Capable of Processing the C Terminus of Nedd8 and Deconjugating Hyper-neddylated CUL1*

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• Role of Predicted Metalloprotease Motif of Jab1/Csn5 in Cleavage of Nedd8 from Cul1

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• The COP9 signalosome.

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• Activation of UBC5 Ubiquitin-conjugating Enzyme by the RING Finger of ROC1 and Assembly of Active Ubiquitin Ligases by All Cullins*

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• AXR1-ECR1–Dependent Conjugation of RUB1 to the Arabidopsis Cullin AtCUL1 Is Required for Auxin Response Article, publication date, and citation information can be found at www.plantcell.org/cgi/doi/10.1105/tpc.010282.

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• The COP9 signalosome inhibits p27(kip1) degradation and impedes G1-S phase progression via deneddylation of SCF Cul1.

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• CSN1 N-terminal-dependent activity is required for Arabidopsis development but not for Rub1/Nedd8 deconjugation of cullins: a structure-function study of CSN1 subunit of COP9 signalosome.

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• An intact NEDD8 pathway is required for Cullin‐dependent ubiquitylation in mammalian cells

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• The Nedd8-conjugated ROC1-CUL1 Core Ubiquitin Ligase Utilizes Nedd8 Charged Surface Residues for Efficient Polyubiquitin Chain Assembly Catalyzed by Cdc34*

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• The Caenorhabditis elegans Skp1-related gene family: diverse functions in cell proliferation, morphogenesis, and meiosis.

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• Emerging Roles of Ubiquitin in Transcription Regulation

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• CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex.

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• CUL7: A DOC domain-containing cullin selectively binds Skp1⋅Fbx29 to form an SCF-like complex

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• Cytoskeletal Regulation by the Nedd8 Ubiquitin-Like Protein Modification Pathway

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• NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding and SCF ligases.

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• Promotion of NEDD8-CUL1 Conjugate Cleavage by COP9 Signalosome

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• Mechanisms underlying ubiquitination.

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• NUB1, a NEDD8-interacting Protein, Is Induced by Interferon and Down-regulates the NEDD8 Expression*

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• Targeting of HIF-α to the von Hippel-Lindau Ubiquitylation Complex by O2-Regulated Prolyl Hydroxylation

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• The Conserved RING-H2 Finger of ROC1 Is Required for Ubiquitin Ligation*

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• Ubiquitin-like proteins: new wines in new bottles.

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• Modification of cullin-1 by ubiquitin-like protein Nedd8 enhances the activity of SCF(skp2) toward p27(kip1).

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• Conjugation of Nedd8 to CUL1 Enhances the Ability of the ROC1-CUL1 Complex to Promote Ubiquitin Polymerization*

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• Identification of a Novel Isopeptidase with Dual Specificity for Ubiquitin- and NEDD8-conjugated Proteins*

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• Covalent modifier NEDD8 is essential for SCF ubiquitin‐ligase in fission yeast

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• The ubiquitin system

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• Reconstitution of G1 cyclin ubiquitination with complexes containing SCFGrr1 and Rbx1.

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• Cdc53/cullin and the essential Hrt1 RING-H2 subunit of SCF define a ubiquitin ligase module that activates the E2 enzyme Cdc34.

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• CUL-2 is required for the G1-to-S-phase transition and mitotic chromosome condensation in Caenorhabditis elegans

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• Identification of the Activating and Conjugating Enzymes of the NEDD8 Conjugation Pathway*

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• Covalent modification of all members of human cullin family proteins by NEDD8

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• ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity.

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