| First Author | Thomas Y | Year | 2018 |
| Journal | PLoS One | Volume | 13 |
| Issue | 6 | Pages | e0199197 |
| PubMed ID | 29958295 | Mgi Jnum | J:263752 |
| Mgi Id | MGI:6187820 | Doi | 10.1371/journal.pone.0199197 |
| Citation | Thomas Y, et al. (2018) The NEDD8 E3 ligase DCNL5 is phosphorylated by IKK alpha during Toll-like receptor activation. PLoS One 13(6):e0199197 |
| abstractText | The activity of Cullin-RING ubiquitin E3 ligases (CRL) is regulated by NEDD8 modification. DCN-like proteins promote Cullin neddylation as scaffold-like E3s. One DCNL, DCNL5, is highly expressed in immune tissue. Here, we provide evidence that DCNL5 may be involved in innate immunity, as it is a direct substrate of the kinase IKKalpha during immune signalling. We find that upon activation of Toll-like receptors, DCNL5 gets rapidly and transiently phosphorylated on a specific N-terminal serine residue (S41). This phosphorylation event is specifically mediated by IKKalpha and not IKKbeta. Our data for the first time provides evidence that DCNL proteins are post-translationally modified in an inducible manner. Our findings also provide the first example of a DCNL member as a kinase substrate in a signalling pathway, indicating that the activity of at least some DCNLs may be regulated. |
