Vps20p and Vta1p interact with Vps4p and function in multivesicular body sorting and endosomal transport in Saccharomyces cerevisiae.

@article{Yeo2003Vps20pAV,
  title={Vps20p and Vta1p interact with Vps4p and function in multivesicular body sorting and endosomal transport in Saccharomyces cerevisiae.},
  author={Sebastian C L Yeo and Linghui Xu and Jihui Ren and Victoria J Boulton and Mahendra D. Wagle and Cong Liu and Gang Ren and Peisze Wong and Regina Zahn and Piriya Sasajala and Hongyuan Yang and Robert C Piper and Alan L. Munn},
  journal={Journal of cell science},
  year={2003},
  volume={116 Pt 19},
  pages={3957-70}
}
Vps4p (End13p) is an AAA-family ATPase that functions in membrane transport through endosomes, sorting of soluble vacuolar proteins to the vacuole, and multivesicular body (MVB) sorting of membrane proteins to the vacuole lumen. In a yeast two-hybrid screen with Vps4p as bait we isolated VPS20 (YMR077c) and the novel open reading frame YLR181c, for which the name VTA1 has recently been assigned (Saccharomyces Genome Database). Vps4p directly binds Vps20p and Vta1p in vitro and binding is not… CONTINUE READING
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