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Vol. 12, Issue 5, 1293-1301, May 2001
Chain to Late Endocytic Compartments
Unité de Biologie des Interactions Cellulaires, Unité
de Recherche Associée Centre National de la Recherche
Scientifique 1960, Institut Pasteur, 75724 Paris Cedex 15, France
Down-regulation of cell surface growth factor receptors plays a key
role in the tight control of cellular responses. Recent reports suggest
that the ubiquitin system, in addition to participating in degradation
by the proteasome of cytosolic and nuclear proteins, might also be
involved in the down-regulation of various membrane receptors. We have
previously characterized a signal in the cytosolic part of the
interleukin 2 receptor 
chain (IL2R) responsible for its
targeting to late endosomes/lysosomes. In this report, the role of the
ubiquitin/proteasome system on the intracellular fate of IL2R was
investigated. Inactivation of the cellular ubiquitination machinery in
ts20 cells, which express a thermolabile ubiquitin-activating enzyme
E1, leads to a significant decrease in the degradation rate of IL2R,
with little effect on its internalization. In addition, we show that a
fraction of IL2R can be monoubiquitinated. Furthermore, mutation of
the lysine residues of the cytosolic region of a chimeric receptor
carrying the IL2R targeting signal resulted in a decreased degradation rate. When cells expressing IL2R were treated either by
proteasome or lysosome inhibitors, a significant decrease in receptor
degradation was observed. Our data show that ubiquitination is required
for the sorting of IL2R toward degradation. They also indicate that
impairment of proteasome function might more generally affect
intracellular routing.
Corresponding author. E-mail address:
adautry{at}pasteur.fr.
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