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Vol. 12, Issue 8, 2556-2566, August 2001
and
*Department of Cell Biology, University Medical Center Utrecht and
Institute of Biomembranes, 3584CX Utrecht, The Netherlands; and
The ubiquitin-proteasome pathway acts as a regulator of the
endocytosis of selected membrane proteins. Recent evidence suggests that it may also function in the intracellular trafficking of membrane
proteins. In this study, several models were used to address the role
of the ubiquitin-proteasome pathway in sorting of internalized proteins
to the lysosome. We found that lysosomal degradation of ligands, which
remain bound to their receptors within the endocytic pathway, is
blocked in the presence of specific proteasome inhibitors. In contrast,
a ligand that dissociates from its receptor upon endosome acidification
is degraded under the same conditions. Quantitative electron microscopy
showed that neither the uptake nor the overall distribution of the
endocytic marker bovine serum albumin-gold is substantially altered in
the presence of a proteasome inhibitor. The data suggest that the ubiquitin-proteasome pathway is involved in an endosomal sorting step
of selected membrane proteins to lysosomes, thereby providing a
mechanism for regulated degradation.
Departments of Pediatrics and Cell Biology and
Physiology, Washington University School of Medicine, St. Louis,
Missouri 63110
Corresponding author. E-mail address:
strous{at}med.uu.nl.
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