Proteomics

Dataset Information

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Analysis of the fragments from hTau degraded by proteasome 20s using mass spectrometry


ABSTRACT: We found two stable intermediates in the interaction of human Tau and proteasome 20s. The aim of this study is to determine the cleavage sites on hTau during this process.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Escherichia Coli

SUBMITTER: Pan Fang  

LAB HEAD: Henning Urlaub

PROVIDER: PXD015349 | Pride | 2020-04-22

REPOSITORIES: Pride

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Publications

Proteasomal degradation of the intrinsically disordered protein tau at single-residue resolution.

Ukmar-Godec T T   Fang P P   Ibáñez de Opakua A A   Henneberg F F   Godec A A   Pan K-T KT   Cima-Omori M-S MS   Chari A A   Mandelkow E E   Urlaub H H   Zweckstetter M M  

Science advances 20200722 30


Intrinsically disordered proteins (IDPs) can be degraded in a ubiquitin-independent process by the 20<i>S</i> proteasome. Decline in 20<i>S</i> activity characterizes neurodegenerative diseases. Here, we examine 20<i>S</i> degradation of IDP tau, a protein that aggregates into insoluble deposits in Alzheimer's disease. We show that cleavage of tau by the 20<i>S</i> proteasome is most efficient within the aggregation-prone repeat region of tau and generates both short, aggregation-deficient pepti  ...[more]

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