A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly

Article Abstract:

A novel ubiquitination factor named E4 is described. This protein binds to the ubiquitin moieties of preformed conjugates and catalyzes ubiquitin chain assembly together with the ubiquitin-activating enzyme E1, the ubiquitin-conjugating enzyme E2 and the substrate-specific ubiquitin-protein ligase E3. E4 defines a a novel protein family that includes two human members, the yeast protein UFD2 and the regulatory protein NOSA from Dictyostelium. This seems to indicate that a number of substrates might be regulated by multi-ubiquitin chain assembly.

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Activation of a membrane-bound transportation factor by regulated ubiquitin/proteasome-dependent processing

Article Abstract:

Research demonstrates that two homologous yeast transcription factors SPT23 and MGA2 are activated in a ubiquitin/proteasome -dependent processing. Data indicate that the processing is mediated by fatty acid pools suggesting that membrane fluidity may have a role in the regulation of the processing event.

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Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(sup)UFD1/NPL4, a ubiquitin-selective chaperone

Article Abstract:

Results indicate that CDC48(sup)UFD1/NPL4, binds ubiquitinated substrates such as dimerized transcription factor SPT23, termed p90. Data suggest that CDC48(sup)UFD1/NPL4 is capable of removing ubiquitin conjugates from protein complexes.

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