Systematic profiling of SH3-mediated Tau-Partner interaction network in Alzheimer's disease by integrating in silico analysis and in vitro assay.
Alzheimer's disease
Bioinformatics
Peptide
SH3 domain
Tau protein
Weighted source–target network
Journal
Journal of molecular graphics & modelling
ISSN: 1873-4243
Titre abrégé: J Mol Graph Model
Pays: United States
ID NLM: 9716237
Informations de publication
Date de publication:
07 2019
07 2019
Historique:
received:
12
03
2019
revised:
20
04
2019
accepted:
07
05
2019
pubmed:
22
5
2019
medline:
14
4
2020
entrez:
22
5
2019
Statut:
ppublish
Résumé
The aberrant assembly of microtubule-associated protein Tau (τ) into insoluble aggregates is closely related to Alzheimer's disease (AD), which is elicited from Tau phosphorylation events and regulated by the specific intermolecular recognition between the proline-rich PxxP motifs of Tau and the SH3 domains of its diverse partner proteins/kinases. Here, we attempt to create a systematic interaction profile for the 10 SH3 domains of previously reported Tau partners across all the 18 Tau PxxP peptides. A number of biologically functional SH3-PxxP interaction events are identified from the profile and then tested using fluorescence spectroscopy. It is revealed that (i) the region (residues 520-560) precedent to the tubulin-binding partial repeats of Tau protein is an important target of SH3 domains, where contains the three PxxP peptides τp
Identifiants
pubmed: 31112821
pii: S1093-3263(19)30161-5
doi: 10.1016/j.jmgm.2019.05.004
pii:
doi:
Substances chimiques
Peptides
0
Tubulin
0
tau Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
265-272Informations de copyright
Copyright © 2019 Elsevier Inc. All rights reserved.