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Titolo:
THE MAMMALIAN PROTEIN (RBET1) HOMOLOGOUS TO YEAST BET1P IS PRIMARILY ASSOCIATED WITH THE PRE-GOLGI INTERMEDIATE COMPARTMENT AND IS INVOLVEDIN VESICULAR TRANSPORT FROM THE ENDOPLASMIC-RETICULUM TO THE GOLGI-APPARATUS
Autore:
ZHANG T; WONG SH; TANG BL; XU Y; PETER F; SUBRAMANIAM VN; HONG WJ;
Indirizzi:
INST MOL & CELL BIOL,MEMBRANE BIOL LAB,15 LOWER KENT RIDGE RD SINGAPORE 119076 SINGAPORE INST MOL & CELL BIOL,MEMBRANE BIOL LAB SINGAPORE 119076 SINGAPORE
Titolo Testata:
The Journal of cell biology
fascicolo: 5, volume: 139, anno: 1997,
pagine: 1157 - 1168
SICI:
0021-9525(1997)139:5<1157:TMP(HT>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
INTEGRAL MEMBRANE-PROTEIN; CIS-GOLGI; BREFELDIN-A; BIOCHEMICAL REQUIREMENTS; MONOCLONAL-ANTIBODY; KDEL RECEPTOR; COMPLEX; ER; VESICLES; FUSION;
Tipo documento:
Article
Natura:
Periodico
Citazioni:
74
Recensione:
Indirizzi per estratti:
Citazione:
T. Zhang et al., "THE MAMMALIAN PROTEIN (RBET1) HOMOLOGOUS TO YEAST BET1P IS PRIMARILY ASSOCIATED WITH THE PRE-GOLGI INTERMEDIATE COMPARTMENT AND IS INVOLVEDIN VESICULAR TRANSPORT FROM THE ENDOPLASMIC-RETICULUM TO THE GOLGI-APPARATUS", The Journal of cell biology, 139(5), 1997, pp. 1157-1168

Abstract

Yeast Bet1p participates in vesicular transport from the endoplasmic reticulum to the Golgi apparatus and functions as a soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) associatedwith ER-derived vesicles. A mammalian protein (rbet1) homologous to Bet1p was recently identified, and it was concluded that rbet1 is associated with the Golgi apparatus based on the subcellular localization of transiently expressed epitope-tagged rbet1. In the present study using rabbit antibodies raised against the cytoplasmic domain of rbet1, we found that the majority of rbet1 is not associated with the Golgi apparatus as marked by the Golgi mannosidase II in normal rat kidney cells. Rather, rbet1 is predominantly associated with vesicular spotty structures that concentrate in the peri-Golgi region but are also present throughout the cytoplasm. These structures colocalize with the KDEL receptor and ERGIC-53, which are known to be enriched in the intermediate compartment. When the Golgi apparatus is fragmented by nocodazole treatment: a significant portion of rbet1 is not colocalized with structures marked by Golgi mannosidase II or the KDEL receptor. Association of rbet1 in cytoplasmic spotty structures is apparently not altered by preincubation of cells at 15 degrees C. However, upon warming up from 15 to 37 degrees C, rbet1 concentrates into the peri-Golgi region. Furthermore, rbet1 colocalizes with vesicular stomatitis virus G-protein en route from the ER to the Golgi. Antibodies against rbet1 inhibitin vitro transport of G-protein from the ER to the Golgi apparatus ina dose-dependent manner. This inhibition can be neutralized by preincubation of antibodies with recombinant rbet1. EGTA is known to inhibitER-Golgi transport at a stage after vesicle docking but before the actual fusion event. Antibodies against rbet1 inhibit ER-Golgi transportonly when they are added before the EGTA-sensitive stage. These results suggest that rbet1 may be involved in the docking process of ER derived vesicles with the cis-Golgi membrane.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/09/20 alle ore 00:30:23