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J. Biol. Chem., Vol. 277, Issue 1, 609-617, January 4, 2002
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§,
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, and
¶
From the We examined the intracellular
transport of sterol in living cells using a naturally fluorescent
cholesterol analog, dehydroergosterol (DHE), which has been shown to
mimic many of the properties of cholesterol. By using DHE loaded on
methyl-
Department of Biochemistry, Weill Medical
College of Cornell University, New York, New York 10021 and the
§ Department of Chemistry and Chemical Biology, Cornell
University, Ithaca, New York 14853
-cyclodextrin, we followed this cholesterol analog in
pulse-chase studies. At steady state, DHE co-localizes extensively with
transferrin (Tf), a marker for the endocytic recycling compartment
(ERC), and redistributes with Tf in cells with altered ERC morphology.
Expression of a dominant-negative mutation of an ERC-associated
protein, mRme-1 (G429R), results in the slowing of both DHE and Tf
receptor return to the cell surface.
[3H]Cholesterol is found in the same fraction as
125I-Tf on sucrose density gradients, and this fraction can
be specifically shifted to a higher density based on the presence of
horseradish peroxidase-conjugated Tf in the same organelle. Whereas
vesicular transport of Tf and efflux of DHE from the ERC are entirely
blocked in energy-depleted cells, delivery of DHE to the ERC from the plasma membrane is only slightly affected. Biochemical studies performed using [3H]cholesterol show that the energy
dependence of cholesterol transport to and from the ERC is similar to
DHE transport. We propose that a large portion of intracellular
cholesterol is localized in the ERC, and this pool might be important
in maintaining cellular cholesterol homeostasis.
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