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学科主题: 生命有机化学
题名: Structural Basis of Molecular Recognition between ESCRT-III-like Protein Vps60 and AAA-ATPase Regulator Vta1 in the Multivesicular Body Pathway
其他题名: ESCRT-III体系复合物Vta1NTD-Vps60溶液结构测定
作者: Yang ZZ(杨中正) ; Cody Vild ; JU JIAYING ; ZHANG XU ; LIU JIANPING ; SHEN JIE ; ZHAO BIN ; Lan WX(蓝文贤) ; GONG FUCHUN ; LIU MAILI ; Cao CY(曹春阳) ; XU ZHAOHUI
通讯作者: 曹春阳 ; XU ZHAOHUI
刊名: J. Biol. Chem.
发表日期: 2012
卷: 287, 期:52, 页:43899-43908
收录类别: SCI
部门归属: 中科院上海有机化学研究所; 中科院武汉物理与数学研究所; 美国密西根大学; 长沙科技大学
英文摘要: The AAA-ATPase Vps4 is critical for function of the multivesicular body sorting pathway, which impacts cellular phenomena ranging from receptor down-regulation to viral budding to cytokinesis. Vps4 activity is stimulated by the interaction between Vta1 and Vps60, but the structural basis for this interaction is unclear. The fragment Vps60(128-186) was reported to display the full activity of Vps60. Vta1 interacts with Vps60 using its N-terminal domain (Vta1NTD). In this work, the structure of Vps60(128-186) in complex with Vta1NTD was determined using NMR techniques, demonstrating a novel recognition mode of the microtubule-interacting and transport (MIT) domain in which Vps60(128-186) interacts with Vta1NTD through helices alpha 4' and alpha 5', extending over Vta1NTD MIT2 domain helices 1-3. The Vps60 binding does not result in Vta1 conformational changes, further revealing the fact that Vps4 ATPase is enhanced by the interaction between Vta1 and Vps60 in an unanticipated manner.
语种: 英语
相关网址: 查看原文
WOS记录号: WOS:000312940800066
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内容类型: 期刊论文
URI标识: http://ir.sioc.ac.cn/handle/331003/28489
Appears in Collections:生命有机化学国家重点实验室_期刊论文

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Recommended Citation:
Yang ZZ,Cody Vild,JU JIAYING,et al. Structural Basis of Molecular Recognition between ESCRT-III-like Protein Vps60 and AAA-ATPase Regulator Vta1 in the Multivesicular Body Pathway[J]. J. Biol. Chem.,2012,287(52):43899-43908.
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