作者: Björn D.M. Bean , Samantha K. Dziurdzik , Kathleen L. Kolehmainen , Claire M.S. Fowler , Waldan K. Kwong
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摘要: The regulated expansion of membrane contact sites, which mediate the nonvesicular exchange lipids between organelles, requires recruitment additional site proteins. Yeast Vps13 dynamically localizes to contacts that connect ER, mitochondria, endosomes, and vacuoles is recruited prospore in meiosis, but its targeting mechanism unclear. In this study, we identify sorting nexin Ypt35 as a novel adaptor recruits endosomal vacuolar membranes. We characterize an interaction motif N terminus related motifs Spo71 mitochondrial protein Mcp1. find Mcp1 for Vps13, Vps13–Mcp1 interaction, not Ypt35, required when ER-mitochondria are lost. All three adaptors compete binding conserved six-repeat region implicated human disease. Our results support competition-based model regulating localization at cellular