Helical structures of ESCRT-III are disassembled by VPS4.
Helical structures of ESCRT-III are disassembled by VPS4.
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DOI：
10.1126/science.1161070
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发表时间：
2008-09-05
期刊：
影响因子：
--
通讯作者：
Weissenhorn W
中科院分区：
文献类型：
--
作者：
Lata S;Schoehn G;Jain A;Pires R;Piehler J;Gottlinger HG;Weissenhorn W
在细胞内膜运输和重塑过程中，被称为ESCRT的蛋白质复合体与膜相互作用，是脱离细胞质的萌发过程所必需的，包括腔内小泡的萌发形成多囊泡体，一些被包裹的病毒的萌发，以及胞质分裂中的子细胞分裂。在这里，我们发现ESCRT-III蛋白CHMP2A和CHMP3可以在体外组装成螺旋管结构，暴露出它们在管外部的膜相互作用部位，而AAA型ATPase Vps4可以结合到管的内部，并在ATP水解时分解管。CHMP2A和CHMP3在溶液中共聚，并协同增强其在平面脂质双层上的膜靶向性。因此，这种螺旋CHMP结构可以在向内发芽的小泡的颈部内组装，在Vps4的控制下催化发芽的后期步骤。
During intracellular membrane trafficking and remodeling, protein complexes known as the ESCRTs interact with membranes and are required for budding processes directed away from the cytosol, including the budding of intralumenal vesicles to form multivesicular bodies, for the budding of some enveloped viruses, and for daughter cell scission in cytokinesis. Here we found that the ESCRT-III proteins CHMP2A and CHMP3 could assemble in vitro into helical tubular structures that expose their membrane interaction sites on the outside of the tubule while the AAA-type ATPase VPS4 could bind on the inside of the tubule and disassemble the tubes upon ATP hydrolysis. CHMP2A and CHMP3 co-polymerized in solution and their membrane targeting was cooperatively enhanced on planar lipid bilayers. Such helical CHMP structures could thus assemble within the neck of an inwardly-budding vesicle, catalyzing late steps in budding under the control of VPS4.
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