Journal
DEVELOPMENTAL CELL
Volume 7, Issue 4, Pages 559-569Publisher
CELL PRESS
DOI: 10.1016/j.devcel.2004.09.003
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Funding
- MRC [MC_U105184308] Funding Source: UKRI
- Medical Research Council [MC_U105184308] Funding Source: Medline
- Medical Research Council [MC_U105184308] Funding Source: researchfish
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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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