المؤلفون: Lobato‐Márquez, Damián, Mostowy, Serge

المساهمون: Wellcome Trust

المصدر: EMBO reports ; volume 18, issue 9, page 1476-1477 ; ISSN 1469-221X 1469-3178

مصطلحات موضوعية: Genetics, Molecular Biology, Biochemistry

الإتاحة: https://doi.org/10.15252/embr.201744672Test

المؤلفون: Sirianni, Andrea, Krokowski, Sina, Lobato‐Márquez, Damián, Buranyi, Stephen, Pfanzelter, Julia, Galea, Dieter, Willis, Alexandra, Culley, Siân, Henriques, Ricardo, Larrouy‐Maumus, Gerald, Hollinshead, Michael, Sancho‐Shimizu, Vanessa, Way, Michael, Mostowy, Serge

المساهمون: Medical Research Council, Biotechnology and Biological Sciences Research Council, Wellcome Trust, Lister Institute of Preventive Medicine

المصدر: EMBO reports ; volume 17, issue 7, page 1029-1043 ; ISSN 1469-221X 1469-3178

مصطلحات موضوعية: Genetics, Molecular Biology, Biochemistry

الوصف: 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.

الإتاحة: https://doi.org/10.15252/embr.201541832Test