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Titolo:
TRANSMEMBRANE TOPOLOGY OF THE MAMMALIAN KDEL RECEPTOR
Autore:
SINGH P; TANG BL; WONG SH; HONG WJ;
Indirizzi:
NATL UNIV SINGAPORE,INST MOLEC & CELL BIOL,MEMBRANE BIOL LAB SINGAPORE 0511 SINGAPORE NATL UNIV SINGAPORE,INST MOLEC & CELL BIOL,MEMBRANE BIOL LAB SINGAPORE 0511 SINGAPORE
Titolo Testata:
Molecular and cellular biology
fascicolo: 10, volume: 13, anno: 1993,
pagine: 6435 - 6441
SICI:
0270-7306(1993)13:10<6435:TTOTMK>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
LUMINAL ER PROTEINS; ENDOPLASMIC-RETICULUM; MEMBRANE-PROTEIN; HDEL RECEPTOR; RETENTION; OVEREXPRESSION; RETRIEVAL; SEQUENCE; SYSTEM; CELLS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
27
Recensione:
Indirizzi per estratti:
Citazione:
P. Singh et al., "TRANSMEMBRANE TOPOLOGY OF THE MAMMALIAN KDEL RECEPTOR", Molecular and cellular biology, 13(10), 1993, pp. 6435-6441

Abstract

The mammalian KDEL receptor is an integral membrane protein with seven hydrophobic regions. Fusion proteins comprising a 37-kDa N-glycosylation reporter fused downstream of amino-terminal fragments of the KDELreceptor with varying numbers of hydrophobic regions were synthesizedin an in vitro translation system containing canine pancreatic microsomes. The luminal or cytosolic orientation of the reporter, and hence of the hydrophilic region to which it is fused, was inferred from the presence or absence of glycosylation, which occurs only in the lumen of the microsomes. The cytosolic orientation of the N and C termini wasalso confirmed immunocytochemically. Our results suggest that the KDEL receptor is inserted into the membrane with only six transmembrane domains and that both the amino and carboxy termini are located in the cytoplasm.

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Documento generato il 02/10/20 alle ore 01:44:03