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Vol. 11, Issue 2, 467-480, February 2000
and
*Structural Cell Biology Unit, Department of Medical Anatomy, The
Panum Institute, University of Copenhagen, DK-2200 Copenhagen, Denmark;
and 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 GTPase Rab7, 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. In 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, is essential for maintenance of the perinuclear lysosome compartment.
Dipartimento di Biologia e Patologia Cellulare e
Molecolare "L. Califano" and Centro di Endocrinologia ed Oncologia
Sperimentale "G. Salvatore" del Consiglio Nazionale delle
Richerche, Università of Napoli "Federico II," 80131 Napoli,
Italy
Online version of this article contains
video material. Online version available at www.molbiolcell.org.
These authors contributed equally to this work.
§
Corresponding author. E-mail address:
b.v.deurs{at}mai.ku.dk.
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