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An N-terminal motif unique to primate tau enables differential protein-protein interactions.


ABSTRACT: Compared with other mammalian species, humans are particularly susceptible to tau-mediated neurodegenerative disorders. Differential interactions of the tau protein with other proteins are critical for mediating tau's physiological functions as well as tau-associated pathological processes. Primate tau harbors an 11-amino acid-long motif in its N-terminal region (residues 18-28), which is not present in non-primate species and whose function is unknown. Here, we used deletion mutagenesis to remove this sequence region from the longest human tau isoform, followed by glutathione S-transferase (GST) pulldown assays paired with isobaric tags for relative and absolute quantitation (iTRAQ) multiplex labeling, a quantitative method to measure protein abundance by mass spectrometry. Using t

SUBMITTER: Stefanoska K 

PROVIDER: S-EPMC5846163 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature

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