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| Item Type: | Article |
|---|---|
| Title: | The UBA domain of conjugating enzyme Ubc1/Ube2K facilitates assembly of K48/K63‐branched ubiquitin chains |
| Creators Name: | Pluska, L. and Jarosch, E. and Zauber, H. and Kniss, A. and Waltho, A. and Bagola, K. and von Delbrück, M. and Löhr, F. and Schulman, B.A. and Selbach, M. and Dötsch, V. and Sommer, T. |
| Abstract: | The assembly of a specific polymeric ubiquitin chain on a target protein is a key event in the regulation of numerous cellular processes. Yet, the mechanisms that govern the selective synthesis of particular polyubiquitin signals remain enigmatic. The homologous ubiquitin‐conjugating (E2) enzymes Ubc1 (budding yeast) and Ube2K (mammals) exclusively generate polyubiquitin linked through lysine 48 (K48). Uniquely among E2 enzymes, Ubc1 and Ube2K harbor a ubiquitin‐binding UBA domain with unknown function. We found that this UBA domain preferentially interacts with ubiquitin chains linked through lysine 63 (K63). Based on structural modeling, in vitro ubiquitination experiments, and NMR studies, we propose that the UBA domain aligns Ubc1 with K63‐linked polyubiquitin and facilitates the selective assembly of K48/K63‐branched ubiquitin conjugates. Genetic and proteomics experiments link the activity of the UBA domain, and hence the formation of this unusual ubiquitin chain topology, to the maintenance of cellular proteostasis. |
| Keywords: | Cell Stress, K48-Linked, K63-Linked, Polyubiquitin, Ubiquitin-Conjugating Enzymes |
| Source: | EMBO Journal |
| ISSN: | 0261-4189 |
| Publisher: | EMBO Press / Wiley |
| Volume: | 40 |
| Number: | 6 |
| Page Range: | e106094 |
| Date: | 15 March 2021 |
| Official Publication: | https://doi.org/10.15252/embj.2020106094 |
| PubMed: | View item in PubMed |
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