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Titolo:
Proteasome inhibitors block a late step in lysosomal transport of selectedmembrane but not soluble proteins
Autore:
van Kerkhof, P; dos Santos, CMA; Sachse, M; Klumperman, J; Bu, GJ; Strous, GJ;
Indirizzi:
Washington Univ, Sch Med, Dept Pediat, St Louis, MO 63110 USA Washington Univ St Louis MO USA 63110 Dept Pediat, St Louis, MO 63110 USA Washington Univ, Sch Med, Dept Cell Biol & Physiol, St Louis, MO 63110 USAWashington Univ St Louis MO USA 63110 l & Physiol, St Louis, MO 63110 USA Univ Med Ctr Utrecht, Dept Cell Biol, NL-3584 CX Utrecht, Netherlands UnivMed Ctr Utrecht Utrecht Netherlands NL-3584 CX Utrecht, Netherlands Inst Biomembranes, NL-3584 CX Utrecht, Netherlands Inst Biomembranes Utrecht Netherlands NL-3584 CX CX Utrecht, Netherlands
Titolo Testata:
MOLECULAR BIOLOGY OF THE CELL
fascicolo: 8, volume: 12, anno: 2001,
pagine: 2556 - 2566
SICI:
1059-1524(200108)12:8<2556:PIBALS>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
GROWTH-HORMONE RECEPTOR; LIGAND-INDUCED INTERNALIZATION; DOA4 DEUBIQUITINATING ENZYME; TYROSINE KINASE; LIPOPROTEIN-RECEPTOR; ENDOCYTIC PATHWAY; UBIQUITIN; DEGRADATION; SYSTEM; CELLS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
54
Recensione:
Indirizzi per estratti:
Indirizzo: Strous, GJ Washington Univ, Sch Med, Dept Pediat, St Louis, MO 63110 USA Washington Univ St Louis MO USA 63110 , St Louis, MO 63110 USA
Citazione:
P. van Kerkhof et al., "Proteasome inhibitors block a late step in lysosomal transport of selectedmembrane but not soluble proteins", MOL BIOL CE, 12(8), 2001, pp. 2556-2566

Abstract

The ubiquitin-proteasome pathway acts as a regulator of the endocytosis ofselected membrane proteins. Recent evidence suggests that it may also function in the intracellular trafficking of membrane proteins. In this study, several models were used to address the role of the ubiquitin-proteasome pathway in sorting of internalized proteins to the lysosome. We found that lysosomal degradation of ligands, which remain bound to their receptors within the endocytic pathway, is blocked in the presence of specific proteasome inhibitors. In contrast, a ligand that dissociates from its receptor upon endosome acidification is degraded under the same conditions. Quantitative electron microscopy showed that neither the uptake nor the overall distribution of the endocytic marker bovine serum albumin-gold is substantially altered in the presence of a proteasome inhibitor. The data suggest that the ubiquitin-proteasome pathway is involved in an endosomal sorting step of selected membrane proteins to lysosomes, thereby providing a mechanism for regulated degradation.

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Documento generato il 04/12/20 alle ore 09:55:03