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J. Biol. Chem., Vol. 277, Issue 52, 50219-50222, December 27, 2002
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and
From the Departments of Psychiatry and Cellular and Molecular
Pharmacology, University of California, San Francisco, California
94143-0984
Ubiquitination of cytoplasmic lysine residues can
target G protein-coupled receptors (GPCRs) to proteasomes and has
recently been shown to also be required for sorting of certain GPCRs to lysosomes following ligand-induced endocytosis. We addressed the generality of this mechanism by examining regulated proteolysis of the
murine 
opioid receptor (DOR) expressed in human embryonic kidney 293 cells, a well characterized model system in which
receptors are sorted to lysosomes. Incubation of cells in the presence
of the highly specific proteasome inhibitor lactacystin did not
detectably affect ligand-induced proteolysis of DOR but significantly
delayed ligand-induced proteolysis of epidermal growth factor
receptors. Mutation of all cytoplasmic lysine residues in DOR, creating
a mutant opioid receptor that is unable to be ubiquitinated, did not
detectably inhibit either ligand-induced endocytosis or
proteolytic degradation of endocytosed receptors. Furthermore, the
lysine-mutated DOR, like its wild type counterpart, colocalized
extensively with lysosomes after ligand-induced endocytosis.
These results demonstrate that ubiquitination of DOR is not required
either for its ligand-induced endocytosis or for postendocytic
trafficking to lysosomes.
To whom correspondence should be addressed: Dept. of Psychiatry,
University of California, San Francisco, Box 0984 IRE, Room LP-A104
LPPI, 401 Parnassus Ave., San Francisco, CA 94143-0984. Tel.:
415-476-7855; Fax: 415-476-7884; E-mail: mbt2m@itsa.ucsf.edu.
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