Retention and Degradation of N-Glycoproteins in the Rough Endoplasmic Reticulum |
| |
| Authors: | Sandrine Duvet Jean Dubuisson Myriam Ermonval René Cacan André Verbert |
| |
| Institution: | (1) Laboratoire de Chimie Biologique, UMR du CNRS, Université des Sciences et Technologies de Lille, no. 111, 59655 Villeneuve d'Ascq, Cedex, France;(2) Equipe Hépatite C, UMR du CNRS no. 319, Institut de Biologie de Lille et Institut Pasteur de Lille, 1 rue Calmette, 59021 Lille, Cedex, France;(3) Unité de Génétique Somatique, URA du CNRS no. 1960, Institut Pasteur de Paris, 25 rue du Docteur Roux, 75724 Paris, Cedex 15, France |
| |
| Abstract: | Recent studies have shown that newly synthesized proteins and glycoproteins are submitted to a quality control mechanism in the rough endoplasmic reticulum (ER). In this report we present two models: One model will illustrate a transient retention in rough ER leading to a further degradation of glycoproteins in the cytosol, (soluble alkaline phosphatase expressed in Man-P-Dol deficient CHO cells lines). The second model will illustrate a strict retention of glycoproteins in rough ER without degradation nor recycling through the Golgi (E1, E2 glycoproteins of Hepatitis C virus in stably transfected UHCV-11.4 cells and in infected Hep G2 cells).In both cases, oligomannoside structures are markers of these phenomena, either as free soluble released oligomannosides in the case of degradation, or as N-linked oligomannosides for strict retention in rough ER. |
| |
| Keywords: | Glycoprotein retention degradation |
| 本文献已被 PubMed SpringerLink 等数据库收录！ |
|
