Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Proteolytic function of GPI-anchored plasma membrane protease Yps1p in theyeast vacuole and Golgi
Autore:
Sievi, E; Suntio, T; Makarow, M;
Indirizzi:
Univ Helsinki, Viikki Bioctr, Inst Biotechnol, Program Cellular Biotechnol, FIN-00014 Helsinki, Finland Univ Helsinki Helsinki Finland FIN-00014 ol, FIN-00014 Helsinki, Finland
Titolo Testata:
TRAFFIC
fascicolo: 12, volume: 2, anno: 2001,
pagine: 896 - 907
SICI:
1398-9219(200112)2:12<896:PFOGPM>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
NONANCHORED YAPSIN-1 YAP3P; SACCHAROMYCES-CEREVISIAE; ENDOPLASMIC-RETICULUM; ASPARTYL PROTEASE; SECRETORY PATHWAY; BETA-LACTAMASE; CARBOXYPEPTIDASE-Y; CELL-SURFACE; GENE; DEGRADATION;
Keywords:
ergosterol; Golgi; GPI-anchored proteins; sorting; vacuole; yeast; Yps1p;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Makarow, M Univ Helsinki, Viikki Bioctr, Inst Biotechnol, Program CellularBiotechnol, POB 56, FIN-00014 Helsinki, Finland Univ Helsinki POB 56 Helsinki Finland FIN-00014 sinki, Finland
Citazione:
E. Sievi et al., "Proteolytic function of GPI-anchored plasma membrane protease Yps1p in theyeast vacuole and Golgi", TRAFFIC, 2(12), 2001, pp. 896-907

Abstract

Yps1p is a member of the GPI-anchored aspartic proteases which reside at the plasma membrane of Saccharomyces cerevisiae, Here we show that in Delta erg6 cells, where a late biosynthetic step of the membrane lipid ergosterolis blocked, part of Yps1p was targeted to the vacuole. There it overtook proteolytic functions of the Pep4p protease, resulting in processing of pro-CPY to CPY in cells lacking the PEP4 gene. Yps1p was enriched in membrane microdomains, as it could be isolated in detergent-insoluble complexes from both normal and Delta erg6 cells. Vacuolar Yps1 caused degradation of a mammalian sialyltransferase ectodomain fusion protein (ST6Ne), which was directed from the Golgi to the vacuole in both normal and Delta erg6 cells. Unexpectedly, ST6Ne was degraded also when arrested in the Golgi in a temperature-sensitive sec7-1 mutant. Newly synthesized Yps1p, in transit to the plasma membrane, was also involved in the Golgi-associated degradation. These data show that GPI-anchored proteases, whose biological roles are unknown, may reside and function in different subcellular locations.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/03/20 alle ore 23:21:50