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Cytoplasmic poly-GR/PR inclusions resemble stress granules in vitro.

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Presentation on theme: "Cytoplasmic poly-GR/PR inclusions resemble stress granules in vitro."— Presentation transcript:

1 Cytoplasmic poly-GR/PR inclusions resemble stress granules in vitro.
Cytoplasmic poly-GR/PR inclusions resemble stress granules in vitro. Immunofluorescence of stress granule markers in HEK293 cells and patient brain. DAPI visualizes nuclei. Single confocal planes were taken. Scale bar depicts 20 μm. (A) Co-localization of poly-GR/PR with the stress granule marker G3BP1 in HEK293 cells co-transfected with RFP-STAU1 or RFP control and DPR-GFP or GFP control. Left three columns show individual channels as indicated. The fourth columns show merge with additional nuclear DAPI staining in white. Arrows indicate cytoplasmic inclusions co-labeled with G3BP1. (B) Immunofluorescence of frontal cortex of a C9orf72 patient and a healthy control case to analyze co-localization of poly-GR with stress granule components TIAR, G3BP2, YBX1, and STAU2. Arrows indicate poly-GR aggregates. Source data are available for this figure. Hannelore Hartmann et al. LSA 2018;1:e © 2018 Hartmann et al.

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Figure 7. Interaction between C9orf72 dipeptides and ribonucleotides in vivo. The concentration of RNA extracted from immunoprecipitated samples from NSC34.

Figure 7. Interaction between C9orf72 dipeptides and ribonucleotides in vivo. The concentration of RNA extracted from immunoprecipitated samples from NSC34.
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STAU1/2 and YBX1 recruit poly-GR/PR into large cytoplasmic granules.

STAU1/2 and YBX1 recruit poly-GR/PR into large cytoplasmic granules.
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Exposure to stress and SGs formation.
NPM1 drives poly-GR into the nucleolus of primary neurons.

NPM1 drives poly-GR into the nucleolus of primary neurons.
Poly-GR and poly-PR co-aggregate with ribosomal proteins in C9orf72 patients. Poly-GR and poly-PR co-aggregate with ribosomal proteins in C9orf72 patients.

Poly-GR and poly-PR co-aggregate with ribosomal proteins in C9orf72 patients. Poly-GR and poly-PR co-aggregate with ribosomal proteins in C9orf72 patients.
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Characterization of DPR proteins in primary rat neurons and HEK293 cells. Characterization of DPR proteins in primary rat neurons and HEK293 cells. GFP,
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Poly-GR mainly co-localizes with nucleolar ribosomes.
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