Cell 1999,
PMID: 10089879
Koegl, M; Hoppe, T; Schlenker, S; Ulrich, H D; Mayer, T U; Jentsch, S
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.
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Text Mining Data
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Manually curated Databases
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Gene Ontology Complexes ubiquitin ligase complex:
ubiquitin ligase complex complex (WWP2-RNF11-UBE2D2-TSPAN17-HSPA1A-DYRK2-CBLL1-CBX8-GPR37-TOPORS-SUGT1-FBXL7-MIB2-FBXL12-FBXO25-FBXW4-ARIH1-TRAF7-BRCC3-UBE2E1-BRAP-UBR2-RNF20-UBE4A-DNAJA1-FBXL4-RING1-RNF144B-RNF8-RNF2-UBE2L3)
In total, 465 gene pairs are associated to this article in curated databases