The E3-Ubiquitin Ligase TRIM50 Interacts with HDAC6 and p62, and Promotes the Sequestration and Clearance of Ubiquitinated Proteins into the Aggresome.

Détails

Ressource 1Télécharger: BIB_6BC9845695E4.P001.pdf (3838.22 [Ko])
Etat: Public
Version: de l'auteur
ID Serval
serval:BIB_6BC9845695E4
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
The E3-Ubiquitin Ligase TRIM50 Interacts with HDAC6 and p62, and Promotes the Sequestration and Clearance of Ubiquitinated Proteins into the Aggresome.
Périodique
PLoS One
Auteur(s)
Fusco C., Micale L., Egorov M., Monti M., D'Addetta E.V., Augello B., Cozzolino F., Calcagnì A., Fontana A., Polishchuk R.S., Didelot G., Reymond A., Pucci P., Merla G.
ISSN
1932-6203 (Electronic)
ISSN-L
1932-6203
Statut éditorial
Publié
Date de publication
2012
Volume
7
Numéro
7
Pages
e40440
Langue
anglais
Résumé
In this study we report that, in response to proteasome inhibition, the E3-Ubiquitin ligase TRIM50 localizes to and promotes the recruitment and aggregation of polyubiquitinated proteins to the aggresome. Using Hdac6-deficient mouse embryo fibroblasts (MEF) we show that this localization is mediated by the histone deacetylase 6, HDAC6. Whereas Trim50-deficient MEFs allow pinpointing that the TRIM50 ubiquitin-ligase regulates the clearance of polyubiquitinated proteins localized to the aggresome. Finally we demonstrate that TRIM50 colocalizes, interacts with and increases the level of p62, a multifunctional adaptor protein implicated in various cellular processes including the autophagy clearance of polyubiquitinated protein aggregates. We speculate that when the proteasome activity is impaired, TRIM50 fails to drive its substrates to the proteasome-mediated degradation, and promotes their storage in the aggresome for successive clearance.
Pubmed
Web of science
Open Access
Oui
Création de la notice
18/08/2012 10:12
Dernière modification de la notice
20/08/2019 14:25
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