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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Molecular mechanism of membrane constriction and tubulation mediated by the F-BAR protein Pacsin/Syndapin
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Molecular mechanism of membrane constriction and tubulation mediated by the F-BAR protein Pacsin/Syndapin

机译：F-BAR蛋白Pacsin / Syndapin介导的膜收缩和管形成的分子机制

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摘要

Peripheral membrane proteins of the Bin/amphiphysin/Rvs (BAR) and Fer-CIP4 homology-BAR (F-BAR) family participate in cellular membrane trafficking and have been shown to generate membrane tubules. The degree of membrane bending appears to be encoded in the structure and immanent curvature of the particular protein domains, with BAR and F-BAR domains inducing high- and low-curvature tubules, respectively. In addition, oligomerization and the formation of ordered arrays influences tubule stabilization. Here, the F-BAR domain-containing protein Pacsin was found to possess a unique activity, creating small tubules and tubule constrictions, in addition to the wide tubules characteristic for this subfamily. Based on crystal structures of the F-BAR domain of Pacsin and mutagenesis studies, vesiculation could be linked to the presence of unique structural features distinguishing it from other F-BAR proteins. Tubulation was suppressed in the context of the full-length protein, suggesting that Pacsin is autoinhibited in solution. The regulated deformation of membranes and promotion of tubule constrictions by Pacsin suggests a more versatile function of these proteins in vesiculation and endocytosis beyond their role as scaffold proteins.
机译：Bin / amphiphysin / Rvs（BAR）和Fer-CIP4同源性BAR（F-BAR）家族的外周膜蛋白参与细胞膜运输，并已显示会产生膜小管。膜弯曲的程度似乎编码在特定蛋白质结构域的结构和内在曲率中，BAR和F-BAR结构域分别诱导高曲率和低曲率小管。另外，低聚和有序阵列的形成影响小管稳定性。在这里，发现含有F-BAR结构域的蛋白Pacsin具有独特的活性，除了该亚科的宽小管外，还产生了小管和小管收缩。基于Pacsin的F-BAR结构域的晶体结构和诱变研究，囊泡化可能与独特的结构特征（与其他F-BAR蛋白质区分开）有关。在全长蛋白质的情况下，管形被抑制，表明帕金森蛋白在溶液中被自动抑制。 Pacsin调节的膜变形和肾小管收缩的促进表明，这些蛋白质在囊泡化和内吞作用中具有更广泛的功能，而不仅仅是它们作为支架蛋白的作用。

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  • 作者

    Qi Wang; Marcos V. A. S. Navarro; Gary Peng; Evan Molinelli; Shih Lin Goh; Bret L. Judson; Kanagalaghatta R. Rajashankar; Holger Sondermann;

  • 作者单位

    Department of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853;

    Department of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853;

    Department of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853;

    Department of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853;

    Department of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853;

    Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY 14853;

    Northeastern Collaborative Access Team, Building 436, Argonne National Laboratory, Argonne, IL 60439;

    Department of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853;

  • 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

    endocytosis; membrane trafficking; protein structure;

    机译：内吞膜运输蛋白质结构;

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