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Titolo:
Ubiquitin sorts proteins into the intralumenal degradative compartment of the late-endosome/vacuole
Autore:
Urbanowski, JL; Piper, RC;
Indirizzi:
Univ Iowa, Dept Physiol & Biophys, Iowa City, IA 52442 USA Univ Iowa IowaCity IA USA 52442 ysiol & Biophys, Iowa City, IA 52442 USA
Titolo Testata:
TRAFFIC
fascicolo: 9, volume: 2, anno: 2001,
pagine: 622 - 630
SICI:
1398-9219(200109)2:9<622:USPITI>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
GROWTH-FACTOR RECEPTOR; PLASMA-MEMBRANE; VACUOLAR MEMBRANE; SACCHAROMYCES-CEREVISIAE; MULTIVESICULAR BODY; COUPLED RECEPTOR; GENE-PRODUCTS; LATE-GOLGI; YEAST; ENDOCYTOSIS;
Keywords:
degradation; down-regulation; lysosome; late-endosome; MVB; MVE; ubiquitin; vacuole; vesicle budding;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
36
Recensione:
Indirizzi per estratti:
Indirizzo: Piper, RC Univ Iowa, Dept Physiol & Biophys, Iowa City, IA 52442 USA Univ Iowa Iowa City IA USA 52442 ophys, Iowa City, IA 52442 USA
Citazione:
J.L. Urbanowski e R.C. Piper, "Ubiquitin sorts proteins into the intralumenal degradative compartment of the late-endosome/vacuole", TRAFFIC, 2(9), 2001, pp. 622-630

Abstract

Many studies have demonstrated a role for ubiquitin (Ub) in the down-regulation of cell surface proteins. In yeast, down-regulation is marked by the internalization of proteins, followed by their delivery to the lumen of thevacuole where both the cytosolic and lumenal domains are degraded. It is generally believed that the regulatory step of this process is internalization from the plasma membrane and that protein delivery to the lysosome or vacuole is by default. By separating the process of internalization from degradation, we demonstrate that incorporation of proteins into intralumenal vesicles represents a distinct sorting step along the endocytic pathway that is controlled by recognition of ubiquitin. We show that attachment of a single ubiquitin can serve as a specific sorting signal for the degradative pathway by redirecting recycling Golgi proteins and resident vacuolar proteins into intralumenal vesicles of the yeast vacuole. This pathway is independent of PtdIns(3,5) P2 and does not rely on the specific composition of transmembrane domain segments. These data provide a physiological basis for howubiquitination of cell surface proteins guides their degradation and removal from the recycling pathway.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 08/08/20 alle ore 08:55:22