Atypical mitochondrial fission upon bacterial infection

Autor: Richard J. Youle, Amy E. Palmer, Fabrizia Stavru, Pascale Cossart, Chunxin Wang
Přispěvatelé: Institut National de la Recherche Agronomique (INRA), Interactions Bactéries-Cellules (UIBC), Institut National de la Recherche Agronomique (INRA)-Institut Pasteur [Paris] (IP)-Institut National de la Santé et de la Recherche Médicale (INSERM), University of Colorado [Boulder], National Institutes of Health [Bethesda] (NIH), Institut Pasteur Institut National de la Sant [604], Institut National de la Recherche Agronomique Unit, Nationale pour la Recherche, postdoctoral fellowships from European Molecular Biology Organization, recherche Medicale, Intramural Research Program of the National Institutes of Neurological Disorders and Stroke, National Institutes of Health, ProdInra, Migration, Institut National de la Recherche Agronomique (INRA)-Institut Pasteur [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM), National Institute of Neurological Disorders and Stroke, echerche Medicale
Jazyk: angličtina
Rok vydání: 2013
Předmět:
[SDV]Life Sciences [q-bio]
Fluorescent Antibody Technique
Mitochondrion
MESH: Heat-Shock Proteins
Endoplasmic Reticulum
MESH: Listeria monocytogenes
GTP Phosphohydrolases
Hemolysin Proteins
0302 clinical medicine
FUSION
MAMMALIAN-CELLS
Staurosporine
Listeriosis
LISTERIA-MONOCYTOGENES
MESH: Fluorescent Antibody Technique
Heat-Shock Proteins
0303 health sciences
Multidisciplinary
MESH: Real-Time Polymerase Chain Reaction
Listeriolysin O
PROTEIN HFIS1
MESH: Mitochondrial Proteins
Biological Sciences
Cell biology
APOPTOSIS
[SDV] Life Sciences [q-bio]
MESH: Hemolysin Proteins
Mitochondrial fission
Microtubule-Associated Proteins
actin
medicine.drug
Dynamins
endocrine system
MESH: GTP Phosphohydrolases
Bacterial Toxins
Blotting
Western

ENDOPLASMIC-RETICULUM
DRP1
Biology
Real-Time Polymerase Chain Reaction
Mitochondrial Proteins
03 medical and health sciences
MESH: Endoplasmic Reticulum
medicine
Humans
MESH: Blotting
Western

Fragmentation (cell biology)
PROTEOLYTIC CLEAVAGE
030304 developmental biology
MESH: Humans
Endoplasmic reticulum
Listeria monocytogenes
Molecular biology
Fusion protein
mitochondrial dynamics
MESH: Mitochondrial Dynamics
MESH: Dynamins
live cell imaging
MESH: Microtubule-Associated Proteins
MESH: Bacterial Toxins
MESH: Listeriosis
MESH: HeLa Cells
DNAJA3
MORPHOLOGY
OUTER-MEMBRANE
030217 neurology & neurosurgery
HeLa Cells
Zdroj: Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, 2013, 110 (40), pp.16003-16008. ⟨10.1073/pnas.1315784110⟩
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2013, 110 (40), pp.16003-16008. ⟨10.1073/pnas.1315784110⟩
Proceedings of the National Academy of Sciences
ISSN: 0027-8424
1091-6490
DOI: 10.1073/pnas.1315784110⟩
Popis: International audience; We recently showed that infection by Listeria monocytogenes causes mitochondrial network fragmentation through the secreted pore-forming toxin listeriolysin O (LLO). Here, we examine factors involved in canonical fusion and fission. Strikingly, LLOinduced mitochondrial fragmentation does not require the traditional fission machinery, as Drp1 oligomers are absent from fragmented mitochondria following Listeria infection or LLO treatment, as the dynamin-like protein 1 (Drp1) receptor Mff is rapidly degraded, and as fragmentation proceeds efficiently in cells with impaired Drp1 function. LLO does not cause processing of the fusion protein optic atrophy protein 1 (Opa1), despite inducing a decrease in the mitochondrial membrane potential, suggesting a unique Drp1-and Opa1-independent fission mechanism distinct from that triggered by uncouplers or the apoptosis inducer staurosporine. We show that the ER marks LLO-induced mitochondrial fragmentation sites even in the absence of functional Drp1, demonstrating that the ER activity in regulating mitochondrial fission can be induced by exogenous agents and that the ER appears to regulate fission by a mechanism independent of the canonical mitochondrial fission machinery.
Databáze: OpenAIRE