English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Significance Selective autophagy is critical for the regulation of cellular homeostasis and physiology in mammals. Selective autophagy of invading pathogens and damaged mitochondria requires the TBK1 kinase and the autophagy receptors NDP52 and TAX1BP1, but with poorly understood mechanisms. In this study, we present the crystal structures of the SKIP carboxyl homology (SKICH) domains of NDP52 and TAX1BP1 in complex with NAP1, which not only uncover how NDP52 interacts with NAP1 for the recruitment of TBK1 but also provide an atomic picture showing how a SKICH domain functions as a protein–protein interaction module to interact with its binding partners. Furthermore, the determined complex structures also help to evaluate the currently known TBK1-mediated phosphorylation sites in the SKICH domains of NDP52 and TAX1BP1.

Mechanistic insights into the interactions of NAP1 with the SKICH domains of NDP52 and TAX1BP1