Accumulation of phosphorylated tau is a key pathological feature of Alzheimers disease. Phosphorylated tau accumulation causes synaptic impairment, neuronal dysfunction and formation of neurofibrillary tangles. The pathological actions of phosphorylated tau are mediated by surrounding neuronal proteins, however a comprehensive understanding of the proteins that phosphorylated tau interacts with in Alzheimers disease is surprisingly limited. Therefore, the aim of this study was to determine the phosphorylated tau interactome for the first time. To do this we used two complementary proteomics approaches: First, quantitative proteomics was performed on neurofibrillary tangles microdissected from patients with advanced Alzheimers disease. Second, affinity purification-mass spectrometry was used to identify which of these proteins specifically bound to phosphorylated tau.
[doi:10.25345/C52H7Z]
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: Tau ; neurofibrillary tangles ; affinity purifications ; laser capture microdissection ; label-free ; AD
Principal Investigators: (in alphabetical order) |
Beatrix Ueberheide, NYU School of Medicine, USA |
Submitting User: | Trixi |
Drummond E, Pires G, MacMurray C, Askenazi M, Nayak S, Bourdon M, Safar J, Ueberheide B, Wisniewski T.
Phosphorylated tau interactome in the human Alzheimer's disease brain.
Brain. Epub 2020 Aug 19.
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