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A more recent version of this article appeared on November 1, 2005
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Submitted on July 13, 2005
Revised on August 29, 2005
Accepted on September 1, 2005
*University of Cambridge, Cambridge Institute for Medical Research, Wellcome Trust, Cambridge CB2 2XY, United Kingdom; Department of Pathology and Laboratory Medicine, University of Pennsylvania, Philadelphia, PA 19104; Institut Curie, CNRS-UMR 144, Paris 75248, France; Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892; ||Genentech, South San Francisco, CA 94080; ¶Department of Basic Medical Sciences, St. George’s Hospital Medical School, London SW17 ORE, United Kingdom; #MRC Laboratory for Molecular Cell Biology, Cell Biology Unit, and Department of Biochemistry and Molecular Biology, University College London, London WC1E BT, United Kingdom
Monitoring Editor: Sandra Schmid
Specialized cells exploit adaptor protein complexes for unique post-Golgi sorting events, providing a unique model system to specify adaptor function. Here, we show that AP-3 and AP-1 function independently in sorting of the melanocyte-specific protein, tyrosinase, from endosomes to the melanosome, a specialized lysosome-related organelle distinguishable from lysosomes. AP-3 and AP-1 localize in melanocytes primarily to clathrin-coated buds on tubular early endosomes near melanosomes. Both adaptors recognize the tyrosinase dileucine-based melanosome sorting signal, and tyrosinase largely colocalizes with each adaptor on endosomes. In AP-3-deficient melanocytes, tyrosinase accumulates inappropriately in vacuolar and multivesicular endosomes. Nevertheless, a substantial fraction still accumulates on melanosomes, concomitant with increased association with endosomal AP-1. Our data indicate that AP-3 and AP-1 function in partially redundant pathways to transfer tyrosinase from distinct endosomal subdomains to melanosomes, and that the AP-3 pathway ensures that tyrosinase averts entrapment on internal membranes of forming MVBs.
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