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

Yann Thomas, Daniel C Scott, Yosua Adi Kristariyanto, Jesse Rinehart, Kristopher Clark, Philip Cohen, Thimo Kurz (Lead / Corresponding author)

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Abstract

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.

Original languageEnglish
Article numbere0199197
Pages (from-to)1-19
Number of pages19
JournalPLoS ONE
Volume13
Issue number6
DOIs
Publication statusPublished - 29 Jun 2018

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    Thomas, Y., Scott, D. C., Kristariyanto, Y. A., Rinehart, J., Clark, K., Cohen, P., & Kurz, T. (2018). The NEDD8 E3 ligase DCNL5 is phosphorylated by IKK alpha during Toll-like receptor activation. PLoS ONE, 13(6), 1-19. [e0199197]. https://doi.org/10.1371/journal.pone.0199197