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Titolo:
Mannosidase action, independent of glucose trimming, is essential for proteasome-mediated degradation of unassembled glycosylated Ig light chains
Autore:
Chillaron, J; Adan, C; Haas, IG;
Indirizzi:
Biochem Zentrum Heidelberg, D-69120 Heidelberg, Germany Biochem Zentrum Heidelberg Heidelberg Germany D-69120 eidelberg, Germany
Titolo Testata:
BIOLOGICAL CHEMISTRY
fascicolo: 12, volume: 381, anno: 2000,
pagine: 1155 - 1164
SICI:
1431-6730(200012)381:12<1155:MAIOGT>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
ENDOPLASMIC-RETICULUM MEMBRANE; ASIALOGLYCOPROTEIN RECEPTOR SUBUNITS; CELL ANTIGEN-RECEPTOR; GLYCOPROTEIN GLUCOSYLTRANSFERASE; PROTEIN-DEGRADATION; QUALITY-CONTROL; ER DEGRADATION; SACCHAROMYCES-CEREVISIAE; INFLUENZA HEMAGGLUTININ; LINKED OLIGOSACCHARIDES;
Keywords:
calnexin; calreticulin; ER-associated degradation (ERAD); ER mannosidases; UDP : glucose glycoprotein glucosyl transferase; short-lived protein in glycoprotein ERAD;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
64
Recensione:
Indirizzi per estratti:
Indirizzo: Haas, IG Biochem Zentrum Heidelberg, Neuenheimer Feld 328, D-69120 Heidelberg, Germany Biochem Zentrum Heidelberg Neuenheimer Feld 328 Heidelberg Germany D-69120
Citazione:
J. Chillaron et al., "Mannosidase action, independent of glucose trimming, is essential for proteasome-mediated degradation of unassembled glycosylated Ig light chains", BIOL CHEM, 381(12), 2000, pp. 1155-1164

Abstract

In order to study the role of N-glycans in the ER-associated degradation of unassembled immunoglobulin light (Ig L) chains, we introduced N-glycan acceptor sites into the variable domain of the murine Ig L chain kappa (NS1) which is unfolded in unassembled molecules. We investigated the fate of kappa (NS1) glycosylated at position 70 (kappa 70) and of a double mutant (kappa 18/70) in stably transfected HeLa cells. Degradation of both chains was impaired by lactacystin, a specific inhibitor of the proteasome. The mannosidase inhibitor dMNJ also blocked degradation in a step preceding proteasome action, as did two protein synthesis inhibitors, cycloheximide and puromycin. In contrast, ER glucosidase inhibitors dramatically accelerated the degradation of the chains when added either pre- or posttranslationally. The accelerated degradation was sensitive to lactacystin, dMNJ and cycloheximide, too. None of these drugs, except lactacystin, affected the degradation of unglycosylated kappa (NS1) chains. We conclude that ER mannosidases and proteasome activities, but not glucose trimming (and therefore, most likely not the calnexin/calreticulin UDP:glucose glycoprotein glucosyl transferasecycle), are essential for ER-associated degradation (ERAD) of soluble glycoproteins. A role for a short-lived protein, acting before or simultaneously to ER mannosidases, is suggested.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/09/20 alle ore 12:09:43