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Fig. 1 | Acta Neuropathologica Communications

Fig. 1

From: Altered ribosomal function and protein synthesis caused by tau

Fig. 1

Proteomic analysis identifies altered abundance of select ribosomal proteins in K369I-hTau expressing primary neurons a FUNCAT-WB analysis confirms that global protein synthesis is decreased in K3 primary neurons compared to WT littermates. Primary cortical neurons were cultured from individual K3 and WT pups, before being treated with 4 mM AHA for 16 h at DIV17. The amount of new protein synthesis during this 16 h window was then quantified by using FUNCAT-WB to fluorescently tag AHA-labelled proteins. The human-tau specific Tau12 antibody was used to identify K3 positive pups. FUNCAT signal was normalised to the total protein stain REVERT. n = 4 animals, unpaired t-test. b 80 ribosomal proteins (RPs) were quantified in K3 and WT primary neurons using untargeted, label-free 1D-LC MS/MS analysis. Of these, 11 RPs (RPS2, RPS5, RPS14, RPS28, RPL5, RPL18, RPL23a, RPL35, RPL36 and MRPL12) were found to be significantly decreased (FC ≤ 0.66,  p≤ 0.05) in K3 primary neurons compared to WT littermates, whereas 1 RP (RPS6) was significantly increased (FC ≥ 1.5,  p ≤ 0.05) in K3 primary neurons. RPL22 is shown as an example of an RP unchanged in abundance between K3 and WT primary neurons. n = 4 animals, unpaired t-test. c Surface representation of the ribosome complex (PDB: 4ug0) with RPs found to have significantly decreased abundance in K3 primary neurons (FC ≤ 0.66,  p ≤ 0.05) shown in blue, and RPS6, which displayed significantly increased abundance (FC ≥ 1.5,  p ≤ 0.05) in K3 primary neurons shown in red. Unchanged RPs belonging to the 60S subunit are shown in orange, whereas unchanged RPs which form part of the 40S subunit are shown in green. d Western blot analysis reveals that the abundance of candidate RPs is decreased in 5 month-old K3 mice compared to WT littermates. Protein abundance was normalised to the total protein stain REVERT. n = 4 animals, unpaired t-test

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