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Mitochondria mediate septin cage assembly to promote autophagy of Shigella
Author(s) -
Sirianni Andrea,
Krokowski Sina,
LobatoMárquez Damián,
Buranyi Stephen,
Pfanzelter Julia,
Galea Dieter,
Willis Alexandra,
Culley Siân,
Henriques Ricardo,
LarrouyMaumus Gerald,
Hollinshead Michael,
SanchoShimizu Vanessa,
Way Michael,
Mostowy Serge
Publication year - 2016
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.15252/embr.201541832
Subject(s) - autophagy , septin , mitochondrion , microbiology and biotechnology , cage , shigella , biology , chemistry , genetics , cytokinesis , gene , escherichia coli , apoptosis , cell division , cell , mathematics , combinatorics
Septins, cytoskeletal proteins with well‐characterised roles in cytokinesis, form cage‐like structures around cytosolic Shigella flexneri and promote their targeting to autophagosomes. However, the processes underlying septin cage assembly, and whether they influence S. flexneri proliferation, remain to be established. Using single‐cell analysis, we show that the septin cages inhibit S. flexneri proliferation. To study mechanisms of septin cage assembly, we used proteomics and found mitochondrial proteins associate with septins in S. flexneri ‐infected cells. Strikingly, mitochondria associated with S. flexneri promote septin assembly into cages that entrap bacteria for autophagy. We demonstrate that the cytosolic GTP ase dynamin‐related protein 1 (Drp1) interacts with septins to enhance mitochondrial fission. To avoid autophagy, actin‐polymerising Shigella fragment mitochondria to escape from septin caging. Our results demonstrate a role for mitochondria in anti‐ Shigella autophagy and uncover a fundamental link between septin assembly and mitochondria.