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(Received for publication, January 31, 1997, and in revised form, March 12, 1997)
From the Washington University School of Medicine, Department of
Cell Biology & Physiology, St. Louis, Missouri 63110
Rab7 has been shown to localize to late endosomes
and to mediate transport from early to late endosome/lysosome in
mammalian cells and in yeast. We developed a novel assay to quantify
transport from early to late endosomes using the Xenopus
oocyte. Oocytes were pulsed with avidin after which the oocytes were
incubated to allow avidin transport to a late compartment. The oocytes
were then allowed to internalize biotin-horseradish peroxidase (HRP). The oocytes were then injected with test proteins and incubated further
to allow transport of biotin-HRP from early endosomes to late
endosomal/lysosomal compartments. Transport was quantified by assessing
the formation of HRP-biotin-avidin complexes. Injection of
Rab7:wild-type (WT) and Rab7:Q67L, a GTPase defective mutant, stimulated transport. Rab5:WT had no effect. Rab7:WT-stimulated transport was inhibited by nocodazole, suggesting a role for intact microtubules. Wortmannin, a phosphatidylinositol 3-kinase inhibitor, blocked Rab7:WT-stimulated transport, but Rab7:Q67L-stimulated transport was unaffected by the drug. Rab7:Q67L is constitutively activated and may not require phosphatidylinositol 3-kinase activity for activation. Rab7-stimulated transport requires
N-ethylmaleimide-sensitive factor (NSF) activity as transport was
blocked by N-ethylmaleimide and ATPase defective NSF
mutants. Our results indicate that sequentially acting endocytic Rab
GTPases utilize similar factors although their modes of action may be
different.
Volume 272, Number 20,
Issue of May 16, 1997
pp. 13055-13059
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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