Reference - Detail
| RRC ID | 54584 |
|---|---|
| Author | Jiang W, Yao X, Shan Z, Li W, Gao Y, Zhang Q. |
| Title | E3 ligase Herc4 regulates Hedgehog signalling through promoting Smoothened degradation. |
| Journal | J Mol Cell Biol |
| Abstract |
Hedgehog (Hh) signalling plays conserved roles in controlling embryonic development; its dysregulation causes many diseases including cancers. The G protein-coupled receptor Smoothened (Smo) is the key signal transducer of the Hh pathway, whose posttranslational regulation has been shown to be critical for its accumulation and activation. Ubiquitination has been reported an essential posttranslational regulation of Smo. Here, we identify a novel E3 ligase of Smo, Herc4, which binds to Smo, and regulates Hh signalling by controlling Smo ubiquitination and degradation. Interestingly, our data suggest that Herc4-mediated Smo degradation is regulated by Hh in PKA-primed phosphorylation-dependent and independent manners. |
| Volume | 11(9) |
| Pages | 791-803 |
| Published | 2019-9-19 |
| DOI | 10.1093/jmcb/mjz024 |
| PII | 5423495 |
| PMID | 30925584 |
| PMC | PMC7261483 |
| MeSH | Animals Drosophila Drosophila Proteins / genetics Drosophila Proteins / metabolism* Gene Knockdown Techniques Hedgehog Proteins / metabolism* Lysosomes / metabolism Phenotype Proteasome Endopeptidase Complex / metabolism Protein Binding Protein Stability Proteolysis Signal Transduction* Smoothened Receptor / metabolism* Ubiquitin-Protein Ligases / genetics Ubiquitin-Protein Ligases / metabolism* Ubiquitination |
| IF | 4.671 |
| Times Cited | 4 |
| Resource | |
| Drosophila | |