Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10747957 | Biochemical and Biophysical Research Communications | 2016 | 8 Pages |
Abstract
Clathrin-coated vesicles (CCVs) play critical roles in multiple cellular processes, including nutrient uptake, endosome/lysosome biogenesis, pathogen invasion, regulation of signalling receptors, etc. Saccharomyces cerevisiae Ent5 (ScEnt5) is one of the two major adaptors supporting the CCV-mediated TGN/endosome traffic in yeast cells. However, the classification and phosphoinositide binding characteristic of ScEnt5 remain elusive. Here we report the crystal structures of the ScEnt5 N-terminal domain, and find that ScEnt5 contains an insertion αⲠhelix that does not exist in other ENTH or ANTH domains. Furthermore, we investigate the classification of ScEnt5-N31â191 by evolutionary history analyses and structure comparisons, and find that the ScEnt5 N-terminal domain shows different phosphoinositide binding property from rEpsin1 and rCALM. Above results facilitate the understanding of the ScEnt5-mediated vesicle coat formation process.
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Biochemistry
Authors
Fan Zhang, Yang Song, Mohammad Ebrahimi, Liwen Niu, Maikun Teng, Xu Li,