Two distinct interaction motifs in amphiphysin bind two independent sites on the clathrin terminal domain β-propeller
Two distinct interaction motifs in amphiphysin bind two independent sites on the clathrin terminal domain β-propeller
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DOI：
10.1038/nsmb736
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发表时间：
2004-03-01
影响因子：
16.8
通讯作者：
Owen, DJ
中科院分区：
文献类型：
--
作者：
Miele, AE;Watson, PJ;Owen, DJ
在网格蛋白包被囊泡的组装过程中，许多外周膜蛋白，包括 amphiphysins，利用LLDLD型网格蛋白盒基序与网格蛋白的N端β -螺旋桨结构域（TD）相互作用。网格蛋白TD与来自amphiphysin 1的TLPWDLWTT肽复合物的2.3埃分辨率结构描绘了第二个网格蛋白结合基序PWXXW（W盒），它结合在TD上远离网格蛋白盒结合位点的位置。amphiphysins的无结构区域内同时存在这两种序列基序，使得它们与游离的TDs结合比仅含网格蛋白盒基序的其他内吞蛋白更紧密。这种特性，连同N端BAR结构域结合弯曲膜的倾向，将优先使amphiphysin及其伙伴动力蛋白定位在凹陷的网格蛋白晶格的周边。
During the assembly of clathrin-coated vesicles, many peripheral membrane proteins, including the amphiphysins, use LLDLD-type clathrin-box motifs to interact with the N-terminal beta-propeller domain (TD) of clathrin. The 2.3 Angstrom resolution structure of the clathrin TD in complex with a TLPWDLWTT peptide from amphiphysin 1 delineates a second clathrin-binding motif, PWXXW ( the W box), that binds at a site on the TD remote from the clathrin box binding site. The presence of both sequence motifs within the unstructured region of the amphiphysins allows them to bind more tightly to free TDs than do other endocytic proteins that contain only clathrin-box motifs. This property, along with the propensity of the N-terminal BAR domain to bind curved membranes, will preferentially localize amphiphysin and its partner, dynamin, to the periphery of invaginated clathrin lattices.