西亚试剂：Epsin N-terminal homology domains bind on opposite sides of

Epsin N-terminal homology domains bind on opposite sides of two SNAREs

Wang, Jing; Gossing, Michael; Fang, Pengfei; Zimmermann, Jana; Li, Xu; von Mollard, Gabriele Fischer; Niu, Liwen; Teng, Maikun

SNARE proteins are crucial for membrane fusion in vesicular transport. To ensure efficient and accurate fusion, SNAREs needto be sorted into different budding vesicles. This process is usually regulated by specific recognition between SNAREs andtheir adaptor proteins. How different pairs of SNAREs and adaptors achieve their recognition is unclear. Here, we report therecognition between yeast SNARE Vti1p and its adaptor Ent3p derived from three crystal structures. Surprisingly, this yeastpair Vti1p/Ent3p interacts through a distinct binding site compared to their homologues vti1b/epsinR in mammals. An oppositesurface on Vti1p_Habc domain binds to a conserved area on the epsin N-terminal homology (ENTH) domain of Ent3p. Two-hybrid,in vitro pull-down and in vivo experiments indicate this binding interface is important for correct localization of Vti1pin the cell. This previously undescribed discovery that a cargo and adaptor pair uses different binding sites across speciessuggests the diversity of SNARE-adaptor recognition in vesicular transport.

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