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Structural analysis and modeling reveals new mechanisms governing ESCRT-III spiral filament assembly | |
2014 | |
发表期刊 | JOURNAL OF CELL BIOLOGY |
ISSN | 0021-9525 |
EISSN | 1540-8140 |
卷号 | 206期号:6页码:763-777 |
发表状态 | 已发表 |
DOI | 10.1083/jcb.201403108 |
摘要 | The scission of biological membranes is facilitated by a variety of protein complexes that bind and manipulate lipid bilayers. ESCRT-III (endosomal sorting complex required for transport III) filaments mediate membrane scission during the ostensibly disparate processes of multivesicular endosome biogenesis, cytokinesis, and retroviral budding. However, mechanisms by which ESCRT-III subunits assemble into a polymer remain unknown. Using cryogenic electron microscopy (cryo-EM), we found that the full-length ESCRT-III subunit Vps32/CHMP4B spontaneously forms single-stranded spiral filaments. The resolution afforded by two-dimensional cryo-EM combined with molecular dynamics simulations revealed that individual Vps32/CHMP4B monomers within a filament are flexible and able to accommodate a range of bending angles. In contrast, the interface between monomers is stable and refractory to changes in conformation. We additionally found that the carboxyl terminus of Vps32/CHMP4B plays a key role in restricting the lateral association of filaments. Our findings highlight new mechanisms by which ESCRT-III filaments assemble to generate a unique polymer capable of membrane remodeling in multiple cellular contexts. |
URL | 查看原文 |
收录类别 | SCI |
WOS研究方向 | Cell Biology |
WOS类目 | Cell Biology |
WOS记录号 | WOS:000342384300006 |
WOS关键词 | MOLECULAR-DYNAMICS SIMULATIONS ; MEMBRANE NECK CONSTRICTION ; GENERALIZED BORN MODEL ; VESICLE FORMATION ; COMPLEX ; PROTEINS ; VPS4 ; SYSTEM ; AUTOINHIBITION ; VISUALIZATION |
原始文献类型 | Article |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/120039 |
专题 | 个人在本单位外知识产出 |
通讯作者 | Audhya, Anjon |
作者单位 | 1.Univ Wisconsin, Sch Med & Publ Hlth, Dept Biomol Chem, Madison, WI 53706 USA 2.Univ Wisconsin, Dept Bot, Madison, WI 53706 USA 3.Univ Wisconsin, Dept Genet, Madison, WI 53706 USA 4.Univ Wisconsin, Dept Chem, Madison, WI 53706 USA 5.Univ Wisconsin, Grad Program Biophys, Madison, WI 53706 USA 6.Univ Wisconsin, Dept Math, Madison, WI 53706 USA 7.Univ Wisconsin, Dept Biochem, Madison, WI 53706 USA 8.Univ Wisconsin, Inst Mol Virol, Madison, WI 53706 USA 9.Univ Wisconsin, Howard Hughes Med Inst, Madison, WI 53706 USA 10.Univ Wisconsin, Morgridge Inst Res, Madison, WI 53706 USA |
推荐引用方式 GB/T 7714 | Shen, Qing-Tao,Schuh, Amber L.,Zheng, Yuqing,et al. Structural analysis and modeling reveals new mechanisms governing ESCRT-III spiral filament assembly[J]. JOURNAL OF CELL BIOLOGY,2014,206(6):763-777. |
APA | Shen, Qing-Tao.,Schuh, Amber L..,Zheng, Yuqing.,Quinney, Kyle.,Wang, Lei.,...&Audhya, Anjon.(2014).Structural analysis and modeling reveals new mechanisms governing ESCRT-III spiral filament assembly.JOURNAL OF CELL BIOLOGY,206(6),763-777. |
MLA | Shen, Qing-Tao,et al."Structural analysis and modeling reveals new mechanisms governing ESCRT-III spiral filament assembly".JOURNAL OF CELL BIOLOGY 206.6(2014):763-777. |
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