BibTex format
@article{Sirianni:2016:10.15252/embr.201541832,
author = {Sirianni, A and Krokowski, S and Lobato-Márquez, D and Buranyi, S and Pfanzelter, J and Galea, D and Willis, A and Culley, S and Henriques, R and Larrouy-Maumus, G and Hollinshead, M and Sancho-Shimizu, V and Way, M and Mostowy, S},
doi = {10.15252/embr.201541832},
journal = {EMBO Reports},
pages = {1--15},
title = {Mitochondria mediate septin cage assembly to promote autophagy of Shigella},
url = {http://dx.doi.org/10.15252/embr.201541832},
volume = {17},
year = {2016}
}
RIS format (EndNote, RefMan)
TY - JOUR
AB - 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 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. flexneriinfected cells. Strikingly, mitochondria associated with S. flexneri promote septin assembly into the cages that entrap bacteria for autophagy. We demonstrate that the cytosolic GTPase 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 have demonstrated a role for mitochondria in anti-Shigella autophagy, and uncovered a fundamental link between septin assembly and mitochondria.
AU - Sirianni,A
AU - Krokowski,S
AU - Lobato-Márquez,D
AU - Buranyi,S
AU - Pfanzelter,J
AU - Galea,D
AU - Willis,A
AU - Culley,S
AU - Henriques,R
AU - Larrouy-Maumus,G
AU - Hollinshead,M
AU - Sancho-Shimizu,V
AU - Way,M
AU - Mostowy,S
DO - 10.15252/embr.201541832
EP - 15
PY - 2016///
SN - 1469-221X
SP - 1
TI - Mitochondria mediate septin cage assembly to promote autophagy of Shigella
T2 - EMBO Reports
UR - http://dx.doi.org/10.15252/embr.201541832
UR - https://www.embopress.org/doi/full/10.15252/embr.201541832
UR - http://hdl.handle.net/10044/1/32299
VL - 17
ER -
