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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Epsin N-terminal homology domains bind on opposite sides of two SNAREs
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Epsin N-terminal homology domains bind on opposite sides of two SNAREs

机译：Epsin N端同源域结合在两个SNARE的相对侧

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摘要

SNARE proteins are crucial for membrane fusion in vesicular transport. To ensure efficient and accurate fusion, SNAREs need to be sorted into different budding vesicles. This process is usually regulated by specific recognition between SNAREs and their adaptor proteins. How different pairs of SNAREs and adaptors achieve their recognition is unclear. Here, we report the recognition between yeast SNARE Vtilp and its adaptor Ent3p derived from three crystal structures. Surprisingly, this yeast pair Vti1p/Ent3p interacts through a distinct binding site compared to their homologues vtiib/epsinR in mammals. An opposite surface 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 Vtilp in the cell. This previously undescribed discovery that a cargo and adaptor pair uses different binding sites across species suggests the diversity of SNARE-adaptor recognition in vesicular transport.
机译：SNARE蛋白对于囊泡运输中的膜融合至关重要。为了确保有效和准确的融合，需要将SNARE分为不同的出芽小泡。此过程通常由SNARE及其衔接蛋白之间的特异性识别来调节。尚不清楚不同的SNARE和适配器对如何实现识别。在这里，我们报告酵母SNARE Vtilp及其从三个晶体结构衍生的适配器Ent3p之间的识别。出乎意料的是，与哺乳动物中的同系物vtiib / epsinR相比，该酵母对Vti1p / Ent3p通过不同的结合位点相互作用。 Vti1p_Habc域的相对表面与Ent3p的epsin N末端同源性（ENTH）域上的保守区域结合。两次杂交，体外下拉和体内实验表明，这种结合界面对于Vtilp在细胞中的正确定位很重要。货物和适配器对在物种间使用不同的结合位点的这一先前未描述的发现表明，囊泡运输中SNARE适配器识别的多样性。

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  • 作者

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

  • 作者单位

    Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230026, China,Key Laboratory of Structural Biology, Chinese Academy of Sciences, 96 Jinzhai Road, Hefei, Anhui 230026, China;

    Biochemie III, Fa ku I tat fur Chemie, Universitatstrasse 25, Universitat Bielefeld, 33615 Bielefeld, Germany;

    Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230026, China,Key Laboratory of Structural Biology, Chinese Academy of Sciences, 96 Jinzhai Road, Hefei, Anhui 230026, China;

    Biochemie III, Fa ku I tat fur Chemie, Universitatstrasse 25, Universitat Bielefeld, 33615 Bielefeld, Germany;

    Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230026, China,Key Laboratory of Structural Biology, Chinese Academy of Sciences, 96 Jinzhai Road, Hefei, Anhui 230026, China;

    Biochemie III, Fa ku I tat fur Chemie, Universitatstrasse 25, Universitat Bielefeld, 33615 Bielefeld, Germany;

    Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230026, China,Key Laboratory of Structural Biology, Chinese Academy of Sciences, 96 Jinzhai Road, Hefei, Anhui 230026, China;

    Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230026, China,Key Laboratory of Structural Biology, Chinese Academy of Sciences, 96 Jinzhai Road, Hefei, Anhui 230026, China;

  • 收录信息 美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

    cargo recogniton; vtilp sorting; crystallography;

    机译：货物识别;贵宾分拣;晶体学;

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