γ-adaptin appendage domain:: Structure and binding site for Eps15 and γ-synergin
γ-adaptin appendage domain:: Structure and binding site for Eps15 and γ-synergin
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DOI：
10.1016/s0969-2126(02)00801-8
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发表时间：
2002-08-01
期刊：
影响因子：
5.7
通讯作者：
Owen, DJ
中科院分区：
文献类型：
--
作者：
Kent, HM;McMahon, HT;Owen, DJ
AP 1复合物是一个异源四聚体网格蛋白-接头复合物家族，参与高尔基体和内体之间的囊泡运输。该复合物有两个大的亚基，γ和β 1，可分为躯干，铰链和附属结构域。给出了伽玛附件的1.8埃分辨率结构。已知的γ附属配体γ-协同蛋白的结合位点通过基于结构设计的点突变的产生来映射。我们还表明，Eps 15，蛋白质被认为是参与囊泡形成在质膜上，也是一个配体的γ附属物，并结合到相同的网站作为γ-协同。这一观察结果解释了所证明的布雷菲德菌素A（BFA）敏感的Eps 15和AP 1在高尔基复合体的共定位。
The AP1 complex is one of a family of heterotetrameric clathrin-adaptor complexes involved in vesicular trafficking between the Golgi and endosomes. The complex has two large subunits, gamma and beta1, which can be divided into to trunk, hinge, and appendage domains. The 1.8 Angstrom resolution structure of the gamma appendage is presented. The binding site for the known gamma appendage ligand gamma-synergin is mapped through creation of point mutations designed on the basis of the structure. We also show that Eps15, a protein believed to be involved in vesicle formation at the plasma membrane, is also a ligand of gamma appendage and binds to the same site as gamma-synergin. This observation explains the demonstrated brefeldinA (BFA)-sensitive colocalization of Eps15 and AP1 at the Golgi complex.