RRC ID 56895
Author Arasaki K, Mikami Y, Shames SR, Inoue H, Wakana Y, Tagaya M.
Title Legionella effector Lpg1137 shuts down ER-mitochondria communication through cleavage of syntaxin 17.
Journal Nat Commun
Abstract During infection of macrophages, the pathogenic bacterium Legionella pneumophila secretes effector proteins that induce the conversion of the plasma membrane-derived vacuole into an endoplasmic reticulum (ER)-like replicative vacuole. These ER-like vacuoles are ultimately fused with the ER, where the pathogen replicates. Here we show that the L. pneumophila effector Lpg1137 is a serine protease that targets the mitochondria and their associated membranes. Lpg1137 binds to and cleaves syntaxin 17, a soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) protein that is known to participate in the regulation of mitochondrial dynamics through interaction with the mitochondrial fission factor Drp1 in fed cells and in autophagy through interaction with Atg14L and other SNAREs in starved cells. Cleavage of syntaxin 17 inhibits not only autophagy but also staurosporine-induced apoptosis occurring in a Bax, Drp1-dependent manner. Thus, L. pneumophila can shut down ER-mitochondria communication through cleavage of syntaxin 17.
Volume 8
Pages 15406
Published 2017-5-15
DOI 10.1038/ncomms15406
PII ncomms15406
PMID 28504273
PMC PMC5440676
MeSH Animals Apoptosis Autophagy Bacterial Proteins / metabolism* Endoplasmic Reticulum / microbiology* HEK293 Cells HeLa Cells Humans Immunoprecipitation Legionella pneumophila / metabolism* Macrophages / metabolism Macrophages / microbiology* Mice Mice, Inbred C57BL Mitochondria / metabolism* Mutation Qa-SNARE Proteins / metabolism* RNA Interference SNARE Proteins / metabolism Subcellular Fractions
IF 11.878
Times Cited 27
Human and Animal Cells HeLa(RCB0007) THP1(RCB1189)