Retention and degradation of N-glycoproteins in the rough endoplasmic reticulum.
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.
Duvet
S
S
Laboratoire de Chimie Biologique, UMR du CNRS no. 111, Université des Sciences et Technologies de Lille, Villeneuve d'Ascq, France.
Dubuisson
J
J
Ermonval
M
M
Cacan
R
R
Verbert
A
A
D000469:Alkaline Phosphatase / Q000378:metabolism; D000818:Animals; D016466:CHO Cells; D002846:Chromatography, Affinity; D002851:Chromatography, High Pressure Liquid; D006224:Cricetinae; D018870:Endoplasmic Reticulum, Rough / Q000737:chemistry / Q000378:metabolism*; D006023:Glycoproteins / Q000737:chemistry / Q000378:metabolism*; D006056:Golgi Apparatus / Q000378:metabolism; D009154:Mutation; D012995:Solubility; D014759:Viral Envelope Proteins / Q000378:metabolism
C087035:E1 protein, Hepatitis C virus; D006023:Glycoproteins; D014759:Viral Envelope Proteins; C091015:glycoprotein E2, Hepatitis C virus; D000469:Alkaline Phosphatase