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Titolo:
LOCALIZATION OF THE LYS, ASP, GLU, LEU TETRAPEPTIDE RECEPTOR TO THE GOLGI-COMPLEX AND THE INTERMEDIATE COMPARTMENT IN MAMMALIAN-CELLS
Autore:
GRIFFITHS G; ERICSSON M; KRIJNSELOCKER J; NILSSON T; GOUD B; SOLING HD; TANG BL; WONG SH; HONG WJ;
Indirizzi:
EUROPEAN MOLEC BIOL LAB,MEYERHOFSTR 1 D-69102 HEIDELBERG GERMANY IMPERIAL CANC RES FUND LONDON WC2A 3PX ENGLAND INST PASTEUR,CNRS,URA 361,UNITE GENET SOMAT F-75724 PARIS 15 FRANCE UNIV GOTTINGEN,MED CTR,DEPT CLIN BIOCHEM W-3400 GOTTINGEN GERMANY NATL UNIV SINGAPORE,INST MOLEC & CELL BIOL,MEMBRANE BIOL LAB SINGAPORE 0511 SINGAPORE
Titolo Testata:
The Journal of cell biology
fascicolo: 6, volume: 127, anno: 1994,
parte:, 1
pagine: 1557 - 1574
SICI:
0021-9525(1994)127:6<1557:LOTLAG>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
LUMINAL ER PROTEINS; NEURONAL ENDOMEMBRANE SYSTEM; CLATHRIN-COATED VESICLES; HUMAN KDEL RECEPTOR; ENDOPLASMIC-RETICULUM; CIS-GOLGI; BETA-COP; RETROGRADE TRANSPORT; BREFELDIN-A; MEMBRANE GLYCOPROTEIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
81
Recensione:
Indirizzi per estratti:
Citazione:
G. Griffiths et al., "LOCALIZATION OF THE LYS, ASP, GLU, LEU TETRAPEPTIDE RECEPTOR TO THE GOLGI-COMPLEX AND THE INTERMEDIATE COMPARTMENT IN MAMMALIAN-CELLS", The Journal of cell biology, 127(6), 1994, pp. 1557-1574

Abstract

The carboxyl-terminal Lys-Asp-Glu-Leu (KDEL), or a closely-related sequence, is important for ER localization of both lumenal as well as type II membrane proteins. This sequence functions as a retrieval signalat post-ER compartment(s), but the exact compartment(s) where the retrieval occurs remains unresolved. With an affinity-purified antibody against the carboxyl-terminal sequence of the mammalian KDEL receptor, we have investigated its subcellular localization using immunogold labeling on thawed cryosections of different tissues, such as mouse spermatids and rat pancreas, as well as HeLa, Vero, NRK, and mouse L cells. We show that rab1 is an excellent marker of the intermediate compartment, and we use this marker, as well as budding profiles of the mouse hepatitis virus (MHV) in cells infected with this virus, to identify this compartment. Our results demonstrate that the KDEL receptor is concentrated in the intermediate compartment, as well as in the Golgi stack. Lower but significant labeling was detected in the rough ER. In general, only small amounts of the receptor were detected on the trans side of the Golgi stack, including the trans-Golgi network (TGN) of normal cells and tissues. However, some stress conditions, such as infection with vaccinia virus or vesicular stomatitis virus, as well as 20 degrees C or 43 degrees C treatment, resulted in a significant shift ofthe distribution towards the trans-TGN side of the Golgi stack. This shift could be quantified in HeLa cells stably expressing a TGN marker. No significant labeling was detected in structures distal to the TGNunder all conditions tested. After GTP gamma S treatment of permeabilized cells, the receptor was detected in the beta-COP-containing buds/vesicles that accumulate after this treatment, suggesting that these vesicles may transport the receptor between compartments. We propose that retrieval of KDEL-containing proteins occurs at multiple post-ER compartments up to the TGN along the exocytotic pathway, and that withinthis pathway, the amounts of the receptor in different compartments varies according to physiological conditions.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/09/20 alle ore 09:42:59