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"Actin stabilization prevents PrPSc synaptotoxicity: In this report, the authors used a specialized neuronal culture system to dissect the cellular and molecular mechanisms by which prions damage synapses. Their results define a stepwise molecular pathway mediated by p38 MAPK that is responsible for prion synaptic toxicity. A key step in this pathway involves collapse of the actin cytoskeleton within dendritic spines, causing functional deficits in synaptic transmission. In this image, cultured hippocampal neurons were exposed to purified PrPSc for 24 hours in the presence of SiR-actin, a fluorogenic, cell-permeable peptide that stabilizes and labels F-actin in dendritic spines. SiR-actin prevents collapse of dendritic spines (bright green spots), which normally occurs after PrPSc treatment. See Figure 11 of Fang et al." David A. Harris et al.

Image Credit: Cheng Fang 2018

Pearls

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Corrections

Correction: miRNA independent hepacivirus variants suggest a strong evolutionary pressure to maintain miR-122 dependence

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Correction: FAS-associated factor-1 positively regulates type I interferon response to RNA virus infection by targeting NLRX1

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Correction: Viral FGARAT ORF75A promotes early events in lytic infection and gammaherpesvirus pathogenesis in mice

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September 2018

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Prions activate a p38 MAPK synaptotoxic signaling pathway

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