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

LC3 lipidation-mediated selective macroautophagy/autophagy helps eukaryotes to defend against endogenous dangers and foreign invaders. However, LC3 activation mechanisms of selective autophagy are still elusive. We previously determined that the V-ATPase-ATG16L1 axis is critical for LC3 recruitment to bacteria-residing vacuoles, whereas the  Salmonella  effector SopF directly targets V-ATPase to disrupt ATG16L1 interaction. Here we show that host ARF GTPase binding causes SopF-dependent ADP-ribosylation of the Gln124 site of the ATP6V0C/V0C subunit of V-ATPase. Furthermore, LC3 activation by pH perturbation of endolysosomes and the Golgi apparatus is also abolished by SopF or a ATP6V0C Q124A  mutation, illustrating that disruption of the proton gradient in acidic compartments is a universal signal that triggers V-ATPase-ATG16L1-induced LC3 lipidation.

Endomembrane damage sensing by V-ATPase recruits ATG16L1 for LC3 lipidation in situ