A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly
| Autor: | Stephan Schlenker, Thorsten Hoppe, Helle D. Ulrich, Thomas U. Mayer, Manfred Koegl, Stefan Jentsch |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Proteasome Endopeptidase Complex
Saccharomyces cerevisiae Proteins Cell Survival Macromolecular Substances Proteolysis Recombinant Fusion Proteins Cell Cycle Proteins Saccharomyces cerevisiae Ubiquitin-conjugating enzyme General Biochemistry Genetics and Molecular Biology Fungal Proteins Biopolymers Ubiquitin Multienzyme Complexes Stress Physiological Valosin Containing Protein ddc:570 medicine Humans Cloning Molecular E4 Ubiquitins chemistry.chemical_classification Adenosine Triphosphatases DNA ligase biology medicine.diagnostic_test Cell-Free System Biochemistry Genetics and Molecular Biology(all) Proteins biology.organism_classification Dictyostelium Yeast Cell biology Ubiquitin ligase Cysteine Endopeptidases Proteasome Biochemistry chemistry Multigene Family Ubiquitin-Conjugating Enzymes biology.protein Ubiquitin Ligase Protein Processing Post-Translational |
| Zdroj: | Cell. 96(5) |
| ISSN: | 0092-8674 |
| Popis: | Proteins modified by multiubiquitin chains are the preferred substrates of the proteasome. Ubiquitination involves a ubiquitin-activating enzyme, E1, a ubiquitin-conjugating enzyme, E2, and often a substrate-specific ubiquitin–protein ligase, E3. Here we show that efficient multiubiquitination needed for proteasomal targeting of a model substrate requires an additional conjugation factor, named E4. This protein, previously known as UFD2 in yeast, binds to the ubiquitin moieties of preformed conjugates and catalyzes ubiquitin chain assembly in conjunction with E1, E2, and E3. Intriguingly, E4 defines a novel protein family that includes two human members and the regulatory protein NOSA from Dictyostelium required for fruiting body development. In yeast, E4 activity is linked to cell survival under stress conditions, indicating that eukaryotes utilize E4-dependent proteolysis pathways for multiple cellular functions. |
| Databáze: | OpenAIRE |
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