Articles by Audrey Salles in JoVE
Imaging intermediär filament och mikrotubuli med 2-dimensionell direkt stokastiska optiska återuppbyggnad mikroskopi Cécile Leduc1, Audrey Salles2, Spencer L. Shorte2, Sandrine Etienne-Manneville1 1Cell Polarity, Migration and Cancer Unit, UMR 3691, CNRS, Institut Pasteur, 2UTechS Photonic BioImaging (Imagopole) Citech, Institut Pasteur Det övergripande målet med denna metod är att ge de optimala experimentella förhållandena från provberedning till bild förvärv och återuppbyggnad för att utföra 2D tvåfärgad dSTORM bilder av mikrotubuli och mellanliggande glödtrådar i fasta celler
Other articles by Audrey Salles on PubMed
Drosophila Cells Use Nanotube-like Structures to Transfer DsRNA and RNAi Machinery Between Cells Scientific Reports. | Pubmed ID: 27255932 Tunnelling nanotubes and cytonemes function as highways for the transport of organelles, cytosolic and membrane-bound molecules, and pathogens between cells. During viral infection in the model organism Drosophila melanogaster, a systemic RNAi antiviral response is established presumably through the transport of a silencing signal from one cell to another via an unknown mechanism. Because of their role in cell-cell communication, we investigated whether nanotube-like structures could be a mediator of the silencing signal. Here, we describe for the first time in the context of a viral infection the presence of nanotube-like structures in different Drosophila cell types. These tubules, made of actin and tubulin, were associated with components of the RNAi machinery, including Argonaute 2, double-stranded RNA, and CG4572. Moreover, they were more abundant during viral, but not bacterial, infection. Super resolution structured illumination microscopy showed that Argonaute 2 and tubulin reside inside the tubules. We propose that nanotube-like structures are one of the mechanisms by which Argonaute 2, as part of the antiviral RNAi machinery, is transported between infected and non-infected cells to trigger systemic antiviral immunity in Drosophila.
α-Synuclein Transfer Between Neurons and Astrocytes Indicates That Astrocytes Play a Role in Degradation Rather Than in Spreading Acta Neuropathologica. | Pubmed ID: 28725967 Recent evidence suggests that disease progression in Parkinson's disease (PD) could occur by the spreading of α-synuclein (α-syn) aggregates between neurons. Here we studied the role of astrocytes in the intercellular transfer and fate of α-syn fibrils, using in vitro and ex vivo models. α-Syn fibrils can be transferred to neighboring cells; however, the transfer efficiency changes depending on the cell types. We found that α-syn is efficiently transferred from astrocytes to astrocytes and from neurons to astrocytes, but less efficiently from astrocytes to neurons. Interestingly, α-syn puncta are mainly found inside the lysosomal compartments of the recipient cells. However, differently from neurons, astrocytes are able to efficiently degrade fibrillar α-syn, suggesting an active role for these cells in clearing α-syn deposits. Astrocytes co-cultured with organotypic brain slices are able to take up α-syn fibrils from the slices. Altogether our data support a role for astrocytes in trapping and clearing α-syn pathological deposits in PD.
A Role for Septin 2 in Drp1-mediated Mitochondrial Fission EMBO Reports. May, 2016 | Pubmed ID: 27215606 Mitochondria are essential eukaryotic organelles often forming intricate networks. The overall network morphology is determined by mitochondrial fusion and fission. Among the multiple mechanisms that appear to regulate mitochondrial fission, the ER and actin have recently been shown to play an important role by mediating mitochondrial constriction and promoting the action of a key fission factor, the dynamin-like protein Drp1. Here, we report that the cytoskeletal component septin 2 is involved in Drp1-dependent mitochondrial fission in mammalian cells. Septin 2 localizes to a subset of mitochondrial constrictions and directly binds Drp1, as shown by immunoprecipitation of the endogenous proteins and by pulldown assays with recombinant proteins. Depletion of septin 2 reduces Drp1 recruitment to mitochondria and results in hyperfused mitochondria and delayed FCCP-induced fission. Strikingly, septin depletion also affects mitochondrial morphology in Caenorhabditis elegans, strongly suggesting that the role of septins in mitochondrial dynamics is evolutionarily conserved.