Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Ubiquitination is essential for human cytomegalovirus US11-mediated dislocation of MHC class I molecules from the endoplasmic reticulum to the cytosol
Autore:
Kikkert, M; Hassink, G; Barel, M; Hirsch, C; van der Wal, FJ; Wiertz, E;
Indirizzi:
Leiden Univ, Med Ctr, Dept Med Microbiol, NL-2300 RC Leiden, Netherlands Leiden Univ Leiden Netherlands NL-2300 RC NL-2300 RC Leiden, Netherlands Harvard Univ, Sch Med, Dept Pathol, Boston, MA 02115 USA Harvard Univ Boston MA USA 02115 h Med, Dept Pathol, Boston, MA 02115 USA
Titolo Testata:
BIOCHEMICAL JOURNAL
, volume: 358, anno: 2001,
parte:, 2
pagine: 369 - 377
SICI:
0264-6021(20010901)358:<369:UIEFHC>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL ANTIGEN RECEPTOR; N-TERMINAL RESIDUE; PROTEASOME PATHWAY; PROTEIN-DEGRADATION; HEAVY-CHAINS; MEMBRANE-PROTEINS; SECRETORY PROTEIN; ER; EXPRESSION; REDUCTASE;
Keywords:
degradation; E1 enzyme; proteasome; retrotranslocation; ubiquitin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: Wiertz, E Leiden Univ, Med Ctr, Dept Med Microbiol, POB 9600, NL-2300 RC Leiden, Netherlands Leiden Univ POB 9600 Leiden Netherlands NL-2300 RC Netherlands
Citazione:
M. Kikkert et al., "Ubiquitination is essential for human cytomegalovirus US11-mediated dislocation of MHC class I molecules from the endoplasmic reticulum to the cytosol", BIOCHEM J, 358, 2001, pp. 369-377

Abstract

Human cytomegalovirus encodes two glycoproteins, US2 and US11, which causerapid degradation of MHC class I molecules, thus preventing recognition ofvirus-infected cells by the immune system. This degradation process involves retrograde transport or 'dislocation' of MHC class I molecules from the endoplasmic reticulum (ER) to the cytosol, where they are deglycosylated byan N-glycanase and degraded by the proteasome. At present it is unknown whether ubiquitination is required for US2- and US11-mediated dislocation anddegradation of MHC class I molecules. Here, we show that in E36ts20 hamster cells, which contain a temperature-sensitive mutation in the E1 ubiquitin-activating enzyme, US11-mediated degradation of MHC class I molecules is strongly impaired at the non-permissive temperature, indicating the necessity for ubiquitination in this process. We next addressed the question of whether ubiquitination is a condition for the retrograde movement of MHC classI molecules from the ER to the cytosol, or whether ubiquitination is merely required for recognition of dislocated MHC class I molecules by the proteasome. In the absence of a functional ubiquitin system, complexes of US11 and MHC class I molecules accumulate in the ER. In this state the membrane topology of MHC class I molecules does not significantly change, as judged from proteinase K digestions. Thus the results indicate that a functional ubiquitin system is essential for dislocation of MHC class I molecules from the ER to the cytosol.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 03:05:36