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Functions of Adaptor Protein (AP)-3 and AP-1 in Tyrosinase Sorting from Endosomes to Melanosomes

Theos, Alexander C., Tenza, Danièle, Martina, José A., Hurbain, Ilse, Peden, Andrew A., Sviderskaya, Elena V., Stewart, Abigail, Robinson, Margaret S., Bennett, Dorothy C., Cutler, Daniel F., Bonifacino, Juan S., Marks, Michael S., Raposo, Graça·2005·Molecular Biology of the Cell
DOI 10.1091/mbc.e05-07-0626
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Abstract

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 multivesicular bodies.

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  • The partial reduction in crystal formation in rab32a and ap3m2 mutants is consistent with known redundancy and compensatory trafficking pathways in LRO biology.

    “The phenotypes we observed for rab32a and ap3m2 mutants show partial yet statistically significant reduction in crystal formation, a feature that is consistent with known redundancy and compensatory trafficking pathways in LRO biology (41, 48, 89).”

    From Lysosome-related organelles orchestrate guanine crystal formation in pigment cells (2026) · cites this paper as [89]

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Authors
Theos, A. C., Tenza, D., Martina, J. A., Hurbain, I., Peden, A. A., Sviderskaya, E. V., Stewart, A., Robinson, M. S., Bennett, D. C., Cutler, D. F., Bonifacino, J. S., Marks, M. S., & Raposo, G.
Affiliations
  • Cambridge Institute for Medical Research, University of Cambridge, Wellcome Trust, Cambridge CB2 2XY, United Kingdom
  • Institut Curie, Centre National de la Recherche Scientifique-Unité Mixte de Recherche 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
  • Department of Pathology and Laboratory Medicine, University of Pennsylvania, Philadelphia, PA 19104
Venue
Molecular Biology of the Cell
Publisher
American Society for Cell Biology (ASCB)
Published
2005-11
Volume
16
Issue
11
Pages
5356-5372
ISSN
  • 1059-1524
  • 1939-4586
DOI
10.1091/mbc.e05-07-0626
Cited by
260
References
3
Language
en

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