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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.
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页码:559 / 569
页数:11
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