期刊
MOLECULAR BIOLOGY OF THE CELL
卷 16, 期 11, 页码 5356-5372出版社
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E05-07-0626
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资金
- NCI NIH HHS [T32 CA 09140, T32 CA009140] Funding Source: Medline
- NEI NIH HHS [EY015625, R01 EY015625] Funding Source: Medline
- NIAMS NIH HHS [AR048155, R01 AR048155] Funding Source: Medline
- Wellcome Trust Funding Source: Medline
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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