期刊
MOLECULAR BIOLOGY OF THE CELL
卷 17, 期 9, 页码 4027-4038出版社
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E06-05-0379
关键词
-
类别
资金
- NCI NIH HHS [CA16042, P30 CA016042] Funding Source: Medline
- NEI NIH HHS [R01 EY015625-03, EY015625, R01 EY015625, R01 EY015143, EY015143] Funding Source: Medline
- NHLBI NIH HHS [HL068117, R01 HL068117] Funding Source: Medline
- NIAID NIH HHS [P30 AI028697, AI28697] Funding Source: Medline
The adaptor protein (AP)-3 complex is a component of the cellular machinery that controls protein sorting from endosomes to lysosomes and specialized related organelles such as melanosomes. Mutations in an AP-3 subunit underlie a form of Hermansky-Pudlak syndrome (HPS), a disorder characterized by abnormalities in lysosome-related organelles. HPS in humans can also be caused by mutations in genes encoding subunits of three complexes of unclear function, named biogenesis of lysosome-related organelles complex (BLOC)-1, -2, and -3. Here, we report that BLOC-1 interacts physically and functionally with AP-3 to facilitate the trafficking of a known AP-3 cargo, CD63, and of tyrosinase-related protein 1 (Tyrp1), a melanosomal membrane protein previously thought to traffic only independently of AP-3. BLOC-1 also interacts with BLOC-2 to facilitate Tyrpl trafficking by a mechanism apparently independent of AP-3 function. Both BLOC-1 and -2 localize mainly to early endosome-associated tubules as determined by immunoelectron microscopy. These findings support the idea that BLOC-1 and -2 represent hitherto unknown components of the endosomal protein trafficking machinery.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据