Association of the AP-3 adaptor complex with clathrin
Association of the AP-3 adaptor complex with clathrin
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DOI：
10.1126/science.280.5362.431
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发表时间：
1998-04-17
期刊：
影响因子：
56.9
通讯作者：
Bonifacino, JS
中科院分区：
文献类型：
--
作者：
Dell'Angelica, EC;Klumperman, J;Bonifacino, JS
一种称为AP-3的异四聚体复合体参与了信号介导的蛋白向内溶酶体细胞器的分选。AP-3被认为是非网格蛋白外壳的组成部分。体外结合实验表明，哺乳动物AP-3通过其β 3亚基的附件结构域与网格蛋白重链的氨基末端结构域相互作用与网格蛋白结合。β 3附件结构域包含一个保守的一致基序，用于网格蛋白结合。免疫荧光和免疫电镜观察到AP-3在细胞中与网格蛋白共定位。因此，AP-3在蛋白质分选中的功能可能依赖于网格蛋白。
A heterotetrameric complex termed AP-3 is involved in signal-mediated protein sorting to endosomal-lysosomal organelles. AP-3 has been proposed to be a component of a nonclathrin coat. In vitro binding assays showed that mammalian AP-3 did associate with clathrin by interaction of the appendage domain of its beta 3 subunit with the amino-terminal domain of the clathrin heavy chain. The beta 3 appendage domain contained a conserved consensus motif for clathrin binding. AP-3 colocalized with clathrin in cells as observed by immunofluorescence and immunoelectron microscopy. Thus, AP-3 function in protein sorting may depend on clathrin.