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Vol. 11, Issue 1, 227-239, January 2000
School of Biological Sciences, University of Manchester, Manchester
M13 9PT, United Kingdom
The yeast vacuolar sorting protein Vps4p is an ATPase required for
endosomal trafficking that couples membrane association to its ATPase
cycle. To investigate the function of mammalian VPS4 in
endosomal trafficking, we have transiently expressed wild-type or
ATPase-defective human VPS4 (hVPS4) in cultured cells. Wild-type hVPS4
was cytosolic, whereas a substantial fraction of hVPS4 that was unable
to either bind or hydrolyze ATP was localized to membranes, including
those of specifically induced vacuoles. Vacuoles were exclusively
endocytic in origin, and subsets of enlarged vacuoles stained with
markers for each stage of the endocytic pathway. Sorting of receptors
from the early endosome to the recycling compartment or to the
trans-Golgi network was not significantly affected, and no mutant hVPS4 associated with these compartments. However, many hVPS4-induced vacuoles were substantially enriched in
cholesterol relative to the endosomal compartments of untransfected cells, indicating that expression of mutant hVPS4 gives rise to a
kinetic block in postendosomal cholesterol sorting. The phenotype described here is largely consistent with the defects in vacuolar sorting associated with class E vps mutants in yeast,
and a role for mammalian VPS4 is discussed in this context.
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