Structural basis of Vta1 function in the multivesicular body sorting pathway.

@article{Xiao2008StructuralBO,
  title={Structural basis of Vta1 function in the multivesicular body sorting pathway.},
  author={Junyu Xiao and Hengchuan Xia and Jiahai Zhou and Ishara F Azmi and Brian A. Davies and David J. Katzmann and Zhaohui Xu},
  journal={Developmental cell},
  year={2008},
  volume={14 1},
  pages={37-49}
}
The MVB pathway plays essential roles in several eukaryotic cellular processes. Proper function of the MVB pathway requires reversible membrane association of the ESCRTs, a process catalyzed by Vps4 ATPase. Vta1 regulates the Vps4 activity, but its mechanism of action was poorly understood. We report the high-resolution crystal structures of the Did2- and Vps60-binding N-terminal domain and the Vps4-binding C-terminal domain of S. cerevisiae Vta1. The C-terminal domain also mediates Vta1… CONTINUE READING

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