ESCRT-II, an endosome-associated complex required for protein sorting:: Crystal structure and interactions with ESCRT-III and membranes

被引:179
作者
Teo, H [1 ]
Perisic, O [1 ]
González, B [1 ]
Williams, RL [1 ]
机构
[1] MRC, Mol Biol Lab, Cambridge CB2 2QH, England
基金
英国医学研究理事会;
关键词
D O I
10.1016/j.devcel.2004.09.003
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
ESCRT-I, -II, and -III protein complexes are sequentially recruited to endosomal membranes, where they orchestrate protein sorting and MVB biogenesis. In addition, they play a critical role in retrovirus budding. Structural understanding of ESCRT interaction networks is largely lacking. The 3.6 Angstrom structure of the yeast ESCRT-II core presented here reveals a trilobal complex containing two copies of Vps25, one copy of Vps22, and the C-terminal region of Vps36. Unexpectedly, the entire ESCRT-II core consists of eight repeats of a common building block, a "winged helix" domain. Two PPXY-motifs from Vps25 are involved in contacts with Vps22 and Vps36, and their mutation leads to ESCRT-II disruption. We show that purified ESCRT-II binds directly to the Vps20 component of ESCRT-III. Surprisingly, this binding does not require the protruding N-terminal coiled-coil of Vps22. Vps25 is the chief subunit responsible for Vps20 recruitment. This interaction dramatically increases binding of both components to lipid vesicles in vitro.
引用
收藏
页码:559 / 569
页数:11
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