Titre
Ubiquitination of the Epstein-Barr virus-encoded latent membrane protein 1 depends on the integrity of the TRAF binding site.
Type
article
Institution
UNIL/CHUV/Unisanté + institutions partenaires
Périodique
Auteur(s)
Rothenberger, S.
Auteure/Auteur
Burns, K.
Auteure/Auteur
Rousseaux, M.
Auteure/Auteur
Tschopp, J.
Auteure/Auteur
Bron, C.
Auteure/Auteur
Liens vers les personnes
Liens vers les unités
ISSN
0950-9232[print], 0950-9232[linking]
Statut éditorial
Publié
Date de publication
2003
Volume
22
Numéro
36
Première page
5614
Dernière page/numéro d’article
5618
Langue
anglais
Résumé
The latent membrane protein 1 (LMP1) encoded by the Epstein-Barr virus functions as a constitutively activated receptor of the tumor necrosis factor receptor family. LMP1 is a short-lived protein that is ubiquitinated and degraded by the proteasome. We have previously shown that LMP1 recruits the adapter protein tumor necrosis factor receptor-associated factor 3 (TRAF3) to lipid rafts. To test if TRAFs are involved in LMP1's ubiquitination, we have mutated the LMP1 CTAR1 site that has been identified as a TRAF binding site. We show that the CTAR1 mutant (CTAR1(-)) is expressed after transfection at a similar level to wild-type LMP1, and behaves as wild-type LMP1 with respect to membrane localization. However, CTAR1(-) does not bind TRAF3. We demonstrate that ubiquitination of CTAR1(-) is significantly reduced when compared to wild-type LMP1. In addition, the expression of wild-type LMP1 induces the ubiquitination, an effect that is significantly reduced when the CTAR1(-) is expressed. Taken together, our results suggest that TRAF proteins are involved in the ubiquitination of LMP1, and that their binding to LMP1 may facilitate their own ubiquitination.
PID Serval
serval:BIB_9597D49B6CAE
PMID
Open Access
Oui
Date de création
2008-01-25T13:36:42.851Z
Date de création dans IRIS
2025-05-20T22:38:59Z