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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Von Zastrow, Mark Hislop, James N. Henry, Anastasia G. Marchese, Adriano |
| Description | Author Affiliation: Hislop JN ( Departments of Psychiatry and Cellular and Molecular Pharmacology, University of California, San Francisco, California 94158, USA. james.hislop@ucsf.edu) |
| Abstract | Ubiquitination is essential for the endocytic sorting of various G protein-coupled receptors to lysosomes. Here we identify a distinct function of this covalent modification in controlling the later proteolytic processing of receptors. Mutation of all cytoplasmic lysine residues in the murine delta-opioid receptor blocked receptor ubiquitination without preventing ligand-induced endocytosis of receptors or their subsequent delivery to lysosomes, as verified by proteolysis of extramembrane epitope tags and down-regulation of radioligand binding to the transmembrane helices. Surprisingly, a functional screen revealed that the E3 ubiquitin ligase AIP4 specifically controls down-regulation of wild type receptors measured by radioligand binding without detectably affecting receptor delivery to lysosomes defined both immunochemically and biochemically. This specific AIP4-dependent regulation required direct ubiquitination of receptors and was also regulated by two deubiquitinating enzymes, AMSH and UBPY, which localized to late endosome/lysosome membranes containing internalized delta-opioid receptor. These results identify a distinct function of AIP4-dependent ubiquitination in controlling the later proteolytic processing of G protein-coupled receptors, without detectably affecting their endocytic sorting to lysosomes. We propose that ubiquitination or ubiquitination/deubiquitination cycling specifically regulates later proteolytic processing events required for destruction of the receptor's hydrophobic core. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 29 |
| Volume Number | 284 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2009-07-17 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Lysosomes Metabolism Receptors, G-Protein-Coupled Ubiquitination Binding, Competitive Biotinylation Cell Line Electrophoresis, Polyacrylamide Gel Endosomes Green Fluorescent Proteins Genetics Immunoblotting Microscopy, Fluorescence Models, Biological Mutation Protein Processing, Post-Translational Protein Transport Radioligand Assay Recombinant Fusion Proteins Transfection Ubiquitin Ubiquitin-Protein Ligases Research Support, N.I.H., Extramural Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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