Role of the carboxyl terminal stop transfer sequence of UGT1A6 membrane protein in ER targeting and translocation of upstream lumenal domain.

Date publication

avril 2006

Auteurs

Membres identifiés du Cancéropôle Est :
Dr FOURNEL-GIGLEUX Sylvie , Pr MAGDALOU Jacques , Dr OUZZINE Mohamed

Tous les auteurs :
Ouzzine M, Barre L, Netter P, Magdalou J, Fournel-Gigleux S

Lien Pubmed

https://www.ncbi.nlm.nih.gov/pubmed/16529747

Résumé

We investigated the role of the stop transfer sequence of human UGT1A6 in ER assembly and enzyme activity. We found that this sequence was able to address and translocate the upstream lumenal domain into microsomal membranes in vitro co- and posttranslationally. The signal activity of this sequence was further demonstrated in HeLa cells by its ability to target and maintain the CD4 protein deleted from both the N-terminal signal peptide and C-terminal transmembrane domain into the ER. We showed that total or partial deletion of the stop transfer sequence of UGT1A6 severely impaired enzyme activity highlighting its importance in both membrane assembly and function.

Référence

FEBS Lett. 2006 Apr 3;580(8):1953-8