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The NEDD8 E3 ligase DCNL5 is phosphorylated by IKK alpha during Toll-like receptor activation

by Yann Thomas, Daniel C. Scott, Yosua Adi Kristariyanto, Jesse Rinehart, Kristopher Clark, Philip Cohen, Thimo Kurz

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 IKKα 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 IKKα and not IKKβ. 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.

Autoren:   Yann Thomas; Daniel C. Scott; Yosua Adi Kristariyanto; Jesse Rinehart; Kristopher Clark; Philip Cohen; Thimo Kurz
Journal:   PLoS ONE
Band:   13
Ausgabe:   6
Jahrgang:   2018
Seiten:   e0199197
DOI:   10.1371/journal.pone.0199197
Erscheinungsdatum:   29.06.2018
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