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Titolo:
A novel quality control compartment derived from the endoplasmic reticulum
Autore:
Kamhi-Nesher, S; Shenkman, M; Tolchinsky, S; Fromm, SV; Ehrlich, R; Lederkremer, GZ;
Indirizzi:
Tel Aviv Univ, George S Wise Fac Life Sci, Dept Cell Res & Immunol, IL-69978 Tel Aviv, Israel Tel Aviv Univ Tel Aviv Israel IL-69978 mmunol, IL-69978 Tel Aviv, Israel
Titolo Testata:
MOLECULAR BIOLOGY OF THE CELL
fascicolo: 6, volume: 12, anno: 2001,
pagine: 1711 - 1723
SICI:
1059-1524(200106)12:6<1711:ANQCCD>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
ASIALOGLYCOPROTEIN RECEPTOR SUBUNITS; I HEAVY-CHAINS; GOLGI INTERMEDIATE COMPARTMENT; UBIQUITIN-PROTEASOME PATHWAY; CELL-SURFACE EXPRESSION; ER DEGRADATION; INTRACELLULAR DEGRADATION; ANTIGEN RECEPTOR; SECRETED FORMS; H2 SUBUNIT;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
51
Recensione:
Indirizzi per estratti:
Indirizzo: Lederkremer, GZ Tel Aviv Univ, George S Wise Fac Life Sci, Dept Cell Res &Immunol, IL-69978 Tel Aviv, Israel Tel Aviv Univ Tel Aviv Israel IL-69978 Tel Aviv, Israel
Citazione:
S. Kamhi-Nesher et al., "A novel quality control compartment derived from the endoplasmic reticulum", MOL BIOL CE, 12(6), 2001, pp. 1711-1723

Abstract

Degradation of proteins that, because of improper or suboptimal processing, are retained in the endoplasmic reticulum (ER) involves retrotranslocation to reach the cytosolic ubiquitin-proteasome machinery. We found that substrates of this pathway, the precursor of human asialoglycoprotein receptor H2a and free heavy chains of murine class I major histocompatibility complex (MHC), accumulate in a novel preGolgi compartment that is adjacent to butnot overlapping with the centrosome, the Golgi complex, and the ER-to-Golgi intermediate compartment (ERGIC). On its way to degradation, H2a associated increasingly after synthesis with the ER translocon Sec61. Nevertheless,it remained in the secretory pathway upon proteasomal inhibition, suggesting that its retrotranslocation must be tightly coupled to the degradation process. In the presence of proteasomal inhibitors, the ER chaperones calreticulin and calnexin, but not BiP, PDI, or glycoprotein glucosyltransferase,concentrate in the subcellular region of the novel compartment. The "quality control" compartment is possibly a subcompartment of the ER. It depends on microtubules but is insensitive to brefeldin A. We discuss the possibility that it is also the site for concentration and retrotranslocation of proteins that, like the mutant cystic fibrosis transmembrane conductance regulator, are transported to the cytosol, where they form large aggregates, the"aggresomes."

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/04/20 alle ore 00:21:35