TECPR1 conjugates LC3 to damaged endomembranes upon detection of sphingomyelin exposure

ABSTRACT: Invasive bacteria enter the cytosol of host cells through initial uptake into bacteria-containing vacuoles (BCVs) and subsequent rupture of the BCV membrane, thereby exposing to the cytosol intraluminal, otherwise shielded danger signals such as glycans and sphingomyelin. The detection of glycans by galectin-8 triggers anti-bacterial autophagy but how cells sense and respond to cytosolically-exposed sphingomyelin remains unknown. Here we identify TECPR1 (Tectonin Beta-Propeller Repeat Containing 1) as a receptor for cytosolically-exposed sphingomyelin, which recruits ATG5 into an E3 ligase complex that mediates lipid conjugation of LC3 independently of ATG16L1. TECPR1 binds sphingomyelin through its N-terminal DysF domain (N'DysF), a feature not shared by other mammalian DysF domains. Solv

SUBMITTER: Dr. Felix Randow 

PROVIDER: S-SCDT-10_15252-EMBJ_2022113012 | biostudies-other |

REPOSITORIES: biostudies-other