Proteomics

Dataset Information

0

Neuronal interactome changes upon aggregation of Tau


ABSTRACT: To understand at molecular level how aggregation of Tau modulates its interactions with proteins we reveal key determinant for derailing Tau protein network. By performing quantitative AP-MS we define a new set of interactors which bind Tau upon fibril formation. These interactors contain disordered regions with a unique amino acidic footprint. Such regions are enriched in positively charged Arginines which can engage aberrant binding to Tau fibrils through their guanidinium group via pi-stacking. We also find that the Hsp90 chaperone stalls formation of Tau fibrils and reshapes their abnormal interactome.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Rattus Norvegicus (rat)

TISSUE(S): Brain

SUBMITTER: Riccardo Stucchi  

LAB HEAD: Casper Hoogenraad

PROVIDER: PXD015432 | Pride | 2020-01-30

REPOSITORIES: pride

Dataset's files

Source:
Action DRS
EXP_HSP90MaxQuantproteinGroups.txt Txt
Figure2B.xlsx Xlsx
Figure2C.xlsx Xlsx
Figure2D.xlsx Xlsx
Figure6B.xlsx Xlsx
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Publications


Aggregation of the Tau protein into fibrils defines progression of neurodegenerative diseases, including Alzheimer's Disease. The molecular basis for potentially toxic reactions of Tau aggregates is poorly understood. Here we show that π-stacking by Arginine side-chains drives protein binding to Tau fibrils. We mapped an aggregation-dependent interaction pattern of Tau. Fibrils recruit specifically aberrant interactors characterised by intrinsically disordered regions of atypical sequence featur  ...[more]

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