Structure and function of the ESCRT-II-III interface in multivesicular body biogenesis.

Structure and function of the ESCRT-II-III interface in multivesicular body biogenesis.
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DOI:
10.1016/j.devcel.2009.07.008
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发表时间:
2009-08
期刊:
影响因子:
11.8
通讯作者:
Hurley, James H.
Hurley, James H.
中科院分区:
生物学1区
文献类型:
--
作者:
Im, Young Jun;Wollert, Thomas;Boura, Evzen;Hurley, James H.

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The ESCRT-II-ESCRT-III interaction coordinates the sorting of ubiquitinated cargo with the budding and scission of intralumenal vesicles into multivesicular bodies. The interacting regions of these complexes were mapped to the second winged-helix domain of human ESCRT-II subunit VPS25 and the first helix of ESCRT-III subunit VPS20. The crystal structure of this complex was determined at 2.0 Å resolution. Residues involved in structural interactions explain the specificity of ESCRT-II for Vps20, and are critical for cargo sorting in vivo. ESCRT-II directly activates ESCRT-III driven vesicle budding and scission in vitro via these structural interactions. VPS20 and ESCRT-II bind membranes with nanomolar affinity, explaining why binding to ESCRT-II is dispensable for the recruitment of Vps20 to membranes. Docking of the ESCRT-II -VPS202 supercomplex reveals a convex membrane-binding surface, suggesting a hypothesis for negative membrane curvature induction in the nascent intralumenal vesicle.
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