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Titolo:
Rab7: A key to lysosome biogenesis
Autore:
Bucci, C; Thomsen, P; Nicoziani, P; McCarthy, J; van Deurs, B;
Indirizzi:
Univ Copenhagen, Panum Inst, Dept Med Anat, Struct Cell Biol Unit, DK-2200Copenhagen, Denmark Univ Copenhagen Copenhagen Denmark DK-2200 t, DK-2200Copenhagen, Denmark Univ Naples Federico II, CNR, Dipartimento Biol & Patol Cellulare & Mol L Calif, I-80131 Naples, Italy Univ Naples Federico II Naples Italy I-80131alif, I-80131 Naples, Italy Univ Naples Federico II, CNR, Ctr Endocrinol Oncol Sperimentale G Salvatore, I-80131 Naples, Italy Univ Naples Federico II Naples Italy I-80131 tore, I-80131 Naples, Italy
Titolo Testata:
MOLECULAR BIOLOGY OF THE CELL
fascicolo: 2, volume: 11, anno: 2000,
pagine: 467 - 480
SICI:
1059-1524(200002)11:2<467:RAKTLB>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
GREEN FLUORESCENT PROTEIN; LATE ENDOSOMES; MULTIVESICULAR ENDOSOMES; ENDOCYTIC PATHWAY; TRANSPORT; COMPARTMENT; ORGANELLE; RECEPTOR; FUSION; MATURE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
52
Recensione:
Indirizzi per estratti:
Indirizzo: van Deurs, B Univ Copenhagen, Panum Inst, Dept Med Anat, Struct Cell Biol Unit, DK-2200Copenhagen, Denmark Univ Copenhagen Copenhagen Denmark DK-2200 enhagen, Denmark
Citazione:
C. Bucci et al., "Rab7: A key to lysosome biogenesis", MOL BIOL CE, 11(2), 2000, pp. 467-480

Abstract

The molecular machinery behind lysosome biogenesis and the maintenance of the perinuclear aggregate of late endocytic structures is not well understood. A Likely candidate for being part of this machinery is the small GTPaseRab7, but it is unclear whether this protein is associated with lysosomes or plays any role in the regulation of the perinuclear lysosome compartment. Previously, Rab7 has mainly been implicated in transport from early to late endosomes. We have now used a new approach to analyze the role of Rab7: transient expression of Enhanced Green Fluorescent Protein (EGFP)-tagged Rab7 wt and mutant proteins in HeLa cells. EGFP-Rab7 wt was associated with late endocytic structures, mainly lysosomes, which aggregated and fused in the perinuclear region. The size of the individual lysosomes as well as the degree of perinuclear aggregation increased with the expression levels of EGFP-Rab7 wt and, more dramatically, the active EGFP-Rab7Q67L mutant. In contrast, upon expression of the dominant-negative mutants EGFP-Rab7T22N and EGFP-Rab7N125I, which localized mainly to the cytosol, the perinuclear lysosome aggregate disappeared and lysosomes, identified by colocalization of cathepsin D and lysosome-associated membrane protein-1, became dispersed throughout the cytoplasm, they were inaccessible to endocytosed molecules such as low-density lipoprotein, and their acidity was strongly reduced, as determined by decreased accumulation of the acidotropic probe LysoTracker Red. Ln contrast, early endosomes associated with Rab5 and the transferrin receptor, late endosomes enriched in the cation-independent mannose 6-phosphate receptor, and the trans-Golgi network, identified by its enrichment in TGN-38, were unchanged. These data demonstrate for the first time that Rab7, controlling aggregation and fusion of late endocytic structures/lysosomes, isessential for maintenance of the perinuclear lysosome compartment.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/07/20 alle ore 14:30:56