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Titolo:
SEGREGATION OF ERGIC53 AND THE MAMMALIAN KDEL RECEPTOR UPON EXIT FROMTHE 15-DEGREES-C COMPARTMENT
Autore:
TANG BL; LOW SH; HAURI HP; HONG WJ;
Indirizzi:
NATL UNIV SINGAPORE,INST MOLEC & CELL BIOL,MEMBRANE BIOL LAB,10 KENT RIDGE CRESCENT SINGAPORE 0511 SINGAPORE NATL UNIV SINGAPORE,INST MOLEC & CELL BIOL,MEMBRANE BIOL LAB SINGAPORE 0511 SINGAPORE UNIV CALIF SAN FRANCISCO,DEPT ANAT SAN FRANCISCO CA 94143 UNIV BASEL,DEPT PHARMACOL BASEL SWITZERLAND
Titolo Testata:
European journal of cell biology
fascicolo: 4, volume: 68, anno: 1995,
pagine: 398 - 410
SICI:
0171-9335(1995)68:4<398:SOEATM>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
GOLGI INTERMEDIATE COMPARTMENT; ENDOPLASMIC-RETICULUM; RETROGRADE TRANSPORT; PROTEIN-TRANSPORT; CIS-GOLGI; MEMBRANE-GLYCOPROTEINS; VESICULAR TRANSPORT; RECYCLING PATHWAY; BETA-COP; ER;
Keywords:
ERGIC53; KDEL RECEPTOR; 15-DEGREES-C COMPARTMENT; RETROGRADE TRANSPORT;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
48
Recensione:
Indirizzi per estratti:
Citazione:
B.L. Tang et al., "SEGREGATION OF ERGIC53 AND THE MAMMALIAN KDEL RECEPTOR UPON EXIT FROMTHE 15-DEGREES-C COMPARTMENT", European journal of cell biology, 68(4), 1995, pp. 398-410

Abstract

Protein trafficking along the exocytotic pathway occurs by vesicular transport between successive membranous compartments. Transport from the endoplasmic reticulum (ER) to the Golgi apparatus has been proposedto be bridged by a morphologically defined ER-Golgi intermediate compartment (ERGIC). Using the subcellular dynamics of two markers for theERGIC, the 53 kDa protein ERGIC53 and the mammalian KDEL receptor (KDEL-R), we have investigated the biochemical and physiological characteristics of ER-Golgi anterograde and retrograde transport. The KDEL-R at steady state is mainly con fined to the perinuclear Golgi region while the ERGIC53 has a more elaborate distribution, including the ER. Both proteins can be colocalized to spotty structures distributed throughout the cytoplasm by incubating the cells at 15 degrees C. Upon returning the cells to 37 degrees C, the direction of transport for the twoproteins diverged. KDEL-R was seen to emanate into tubular structureswhich eventually culminated in a focused, perinuclear staining. Thesedynamic changes are consistent with the anterograde transport processfrom the ER to the Golgi apparatus. ERGIC53, on the other hand, was distributed into an extended reticular network as well as the nuclear envelope, a staining pattern characteristic of the ER. With time, ERGIC53 was seen to return to the spotty structures again. The ER retrievalof ERGIC53 is consistent with the fact that the protein contains a dilysine motif which may function as an ER retrieval signal. The movement of ERGIC53 into the ER is not affected by microtubule disrupting agents, which inhibit the movement of KDEL-R to the Golgi. Both the processes are, however, sensitive to the alkylating agent N-ethylmaleimide. When reconstituted in vitro using digitonin permeabilized cells, the movement of ERGIC53 into the ER has a requirement for metabolic energy, is partially inhibited by the nonhydrolyzable guanine nucleotide analog GTP gamma S but could not be made to be cytosol dependent. These results documented the convergence of anterograde transport and retrograde transport at the 15 degrees C compartment and implied the existence of a segregation or a sorting process that would result in the segregation of proteins with different targeting signals in the structure.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/09/20 alle ore 13:42:36