Ubiquitylation of lipopolysaccharide by RNF213 during bacterial infection.

ABSTRACT: Ubiquitylation is a widespread post-translational protein modification in eukaryotes and marks bacteria that invade the cytosol as cargo for antibacterial autophagy^1-3. The identity of the ubiquitylated substrate on bacteria is unknown. Here we show that the ubiquitin coat on Salmonella that invade the cytosol is formed through the ubiquitylation of a non-proteinaceous substrate, the lipid A moiety of bacterial lipopolysaccharide (LPS), by the E3 ubiquitin ligase ring finger protein 213 (RNF213). RNF213 is a risk factor for moyamoya disease^4,5, which is a progressive stenosis of the supraclinoid internal carotid artery that causes stroke (especially in children)^6,7. RNF213 restricts the proliferation of cytosolic Salmonella and is essential for the generati

SUBMITTER: Otten EG 

PROVIDER: S-EPMC7610904 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature