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| Item Type: | Article |
|---|---|
| Title: | The CUE domain of Cue1 aligns growing ubiquitin chains with Ubc7 for rapid elongation |
| Creators Name: | von Delbrück, M., Kniss, A., Rogov, V.V., Pluska, L., Bagola, K., Löhr, F., Güntert, P., Sommer, T. and Dötsch, V. |
| Abstract: | Ubiquitin conjugation is an essential process modulating protein function in eukaryotic cells. Surprisingly, little is known about how the progressive assembly of ubiquitin chains is managed by the responsible enzymes. Only recently has ubiquitin binding activity emerged as an important factor in chain formation. The Ubc7 activator Cue1 carries a ubiquitin binding CUE domain that substantially stimulates K48-linked polyubiquitination mediated by Ubc7. Our results from NMR-based analysis and in vitro ubiquitination reactions point out that two parameters accelerate ubiquitin chain assembly: the increasing number of CUE binding sites and the position of CUE binding within a growing chain. In particular, interactions with a ubiquitin moiety adjacent to the acceptor ubiquitin facilitate chain elongation. These data indicate a mechanism for ubiquitin binding in which Cue1 positions Ubc7 and the distal acceptor ubiquitin for rapid polyubiquitination. Disrupting this mechanism results in dysfunction of the ERAD pathway by a delayed turnover of substrates. |
| Keywords: | alpha-Helical Protein Conformation, Carrier Proteins, Endoplasmic Reticulum-Associated Degradation, Fluorescence Spectrometry, Hydrophobic and Hydrophilic Interactions, Kinetics, Membrane Proteins, Molecular Models, Mutation, Polyubiquitin, Protein Binding, Protein Interaction Domains and Motifs, Proteolysis, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Structure-Activity Relationship, Substrate Specificity, Ubiquitin-Conjugating Enzymes, Ubiquitination |
| Source: | Molecular Cell |
| ISSN: | 1097-2765 |
| Publisher: | Cell Press / Elsevier |
| Volume: | 62 |
| Number: | 6 |
| Page Range: | 918-928 |
| Date: | 16 June 2016 |
| Official Publication: | https://doi.org/10.1016/j.molcel.2016.04.031 |
| PubMed: | View item in PubMed |
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