Structural basis for ubiquitin recognition by the human ESCRT-II EAP45 GLUE domain
Structural basis for ubiquitin recognition by the human ESCRT-II EAP45 GLUE domain
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DOI：
10.1038/nsmb1160
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发表时间：
2006-11-01
影响因子：
16.8
通讯作者：
Sundquist, Wesley I.
中科院分区：
文献类型：
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作者：
Alam, Steven L.;Langelier, Charles;Sundquist, Wesley I.
ESCRT-I和ESCRT-II复合物有助于将泛素化蛋白分选到多泡体（MVB）内积累的囊泡中。晶体学和生物化学分析显示，人ESCRT-Ⅱ EAP 45（也称为VPS 36）亚基的GLUE结构域是一个分裂的普列克底物蛋白同源结构域，它沿着b-夹心结构的沿着结合泛素。该结构表明，人ESCRT-II如何在MVB蛋白分选过程中将遍在蛋白化货物和内体磷脂的识别结合起来。
The ESCRT-I and ESCRT-II complexes help sort ubiquitinated proteins into vesicles that accumulate within multivesicular bodies (MVBs). Crystallographic and biochemical analyses reveal that the GLUE domain of the human ESCRT-II EAP45 (also called VPS36) subunit is a split pleckstrin-homology domain that binds ubiquitin along one edge of the b-sandwich. The structure suggests how human ESCRT-II can couple recognition of ubiquitinated cargoes and endosomal phospholipids during MVB protein sorting.