Structural basis of molecular recognition between ESCRT-III-like protein Vps60 and AAA-ATPase regulator Vta1 in the multivesicular body pathway.

Zhongzheng Yang, Cody Vild, Jiaying Ju, Xu Zhang, Jianping Liu, Jie Shen, Bin Zhao, Wenxian Lan, Fuchun Gong, Maili Liu, Chunyang Cao, Zhaohui Xu

The Journal of biological chemistry 2012 Dec 21

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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 α4' and α5', 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.

Citation

Zhongzheng Yang, Cody Vild, Jiaying Ju, Xu Zhang, Jianping Liu, Jie Shen, Bin Zhao, Wenxian Lan, Fuchun Gong, Maili Liu, Chunyang Cao, Zhaohui Xu. Structural basis of molecular recognition between ESCRT-III-like protein Vps60 and AAA-ATPase regulator Vta1 in the multivesicular body pathway. The Journal of biological chemistry. 2012 Dec 21;287(52):43899-908