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Titolo:
Distinct retrieval and retention mechanisms are required for the quality control of endoplasmic reticulum protein folding
Autore:
Vashist, S; Kim, W; Belden, WJ; Spear, ED; Barlowe, C; Ng, DTW;
Indirizzi:
Penn State Univ, Dept Biochem & Mol Biol, University Pk, PA 16802 USA PennState Univ University Pk PA USA 16802 l, University Pk, PA 16802 USA Dartmouth Coll Sch Med, Dept Biochem, Hanover, NH 03755 USA Dartmouth CollSch Med Hanover NH USA 03755 iochem, Hanover, NH 03755 USA
Titolo Testata:
JOURNAL OF CELL BIOLOGY
fascicolo: 3, volume: 155, anno: 2001,
pagine: 355 - 367
SICI:
0021-9525(20011029)155:3<355:DRARMA>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
UBIQUITIN-PROTEASOME PATHWAY; SACCHAROMYCES-CEREVISIAE; HEMAGGLUTININ-NEURAMINIDASE; SECRETORY PATHWAY; MEMBRANE-PROTEIN; PLASMA-MEMBRANE; MOLECULAR CHAPERONES; GOLGI TRANSPORT; O-GLYCOSYLATION; ER DEGRADATION;
Keywords:
endoplasmic reticulum; vesicular transport; protein degradation; misfolded proteins; glycosylation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
74
Recensione:
Indirizzi per estratti:
Indirizzo: Ng, DTW Penn State Univ, Dept Biochem & Mol Biol, University Pk, PA 16802 USA Penn State Univ University Pk PA USA 16802 rsity Pk, PA 16802 USA
Citazione:
S. Vashist et al., "Distinct retrieval and retention mechanisms are required for the quality control of endoplasmic reticulum protein folding", J CELL BIOL, 155(3), 2001, pp. 355-367

Abstract

Proteins destined for the secretory pathway must first fold and assemble in the lumen of endoplasmic reticulum (ER). The pathway maintains a quality control mechanism to assure that aberrantly processed proteins are not delivered to their sites of function. As part of this mechanism, misfolded proteins are returned to the cytosol via the ER protein translocation pore where they are ubiquitinated and degraded by the 26S proteasome. Previously, little was known regarding the recognition and targeting of proteins before degradation, By tracking the fate of several mutant proteins subject to quality control, we demonstrate the existence of two distinct sorting mechanisms. In the ER, substrates are either sorted for retention in the ER or are transported to the Golgi apparatus via COPII-coated vesicles. Proteins transported to the Golgi are retrieved to the ER via the retrograde transport system. Ultimately, both retained and retrieved proteins converge at a commonmachinery at the ER for degradation. Furthermore, we report the identification of a gene playing a novel role specific to the retrieval pathway. The gene, BST1, is required for the transport of misfolded proteins to the Golgi, although dispensable for the transport of many normal cargo proteins.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/01/21 alle ore 02:58:19