Reference - Detail
| RRC ID | 51559 |
|---|---|
| Author | Hellerschmied D, Roessler M, Lehner A, Gazda L, Stejskal K, Imre R, Mechtler K, Dammermann A, Clausen T. |
| Title | UFD-2 is an adaptor-assisted E3 ligase targeting unfolded proteins. |
| Journal | Nat Commun |
| Abstract |
Muscle development requires the coordinated activities of specific protein folding and degradation factors. UFD-2, a U-box ubiquitin ligase, has been reported to play a central role in this orchestra regulating the myosin chaperone UNC-45. Here, we apply an integrative in vitro and in vivo approach to delineate the substrate-targeting mechanism of UFD-2 and elucidate its distinct mechanistic features as an E3/E4 enzyme. Using Caenorhabditis elegans as model system, we demonstrate that UFD-2 is not regulating the protein levels of UNC-45 in muscle cells, but rather shows the characteristic properties of a bona fide E3 ligase involved in protein quality control. Our data demonstrate that UFD-2 preferentially targets unfolded protein segments. Moreover, the UNC-45 chaperone can serve as an adaptor protein of UFD-2 to poly-ubiquitinate unfolded myosin, pointing to a possible role of the UFD-2/UNC-45 pair in maintaining proteostasis in muscle cells. |
| Volume | 9(1) |
| Pages | 484 |
| Published | 2018-2-2 |
| DOI | 10.1038/s41467-018-02924-7 |
| PII | 10.1038/s41467-018-02924-7 |
| PMID | 29396393 |
| PMC | PMC5797217 |
| MeSH | Animals Caenorhabditis elegans Caenorhabditis elegans Proteins / metabolism* Molecular Chaperones / metabolism* Muscle Cells / metabolism* Myosins / metabolism* Proteostasis Ubiquitin / metabolism Ubiquitin-Protein Ligase Complexes / metabolism* Ubiquitin-Protein Ligases / metabolism* Ubiquitination Unfolded Protein Response |
| IF | 12.121 |
| Times Cited | 7 |
| Altmetric score |
オルトメトリクス指標項目
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| The most frequently cited source | X(Twitter) |
| Total number of mentions | 14 |
| Altmetric score changes over past 6months | 0.0 |
| Resource | |
| C.elegans | tm1380 |