IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v11y2020i1d10.1038_s41467-020-15459-7.html
   My bibliography  Save this article

Structural insights into tetraspanin CD9 function

Author

Listed:
  • Rie Umeda

    (The University of Tokyo)

  • Yuhkoh Satouh

    (Gunma University
    Osaka University)

  • Mizuki Takemoto

    (The University of Tokyo
    Preferred Networks, Inc.)

  • Yoshiko Nakada-Nakura

    (Kyoto University)

  • Kehong Liu

    (Kyoto University)

  • Takeshi Yokoyama

    (RIKEN Center for Biosystems Dynamics Research)

  • Mikako Shirouzu

    (RIKEN Center for Biosystems Dynamics Research)

  • So Iwata

    (Kyoto University
    RIKEN SPring-8 Center)

  • Norimichi Nomura

    (Kyoto University)

  • Ken Sato

    (Gunma University
    Gunma University)

  • Masahito Ikawa

    (Osaka University)

  • Tomohiro Nishizawa

    (The University of Tokyo
    Japan Science and Technology)

  • Osamu Nureki

    (The University of Tokyo)

Abstract

Tetraspanins play critical roles in various physiological processes, ranging from cell adhesion to virus infection. The members of the tetraspanin family have four membrane-spanning domains and short and large extracellular loops, and associate with a broad range of other functional proteins to exert cellular functions. Here we report the crystal structure of CD9 and the cryo-electron microscopic structure of CD9 in complex with its single membrane-spanning partner protein, EWI-2. The reversed cone-like molecular shape of CD9 generates membrane curvature in the crystalline lipid layers, which explains the CD9 localization in regions with high membrane curvature and its implications in membrane remodeling. The molecular interaction between CD9 and EWI-2 is mainly mediated through the small residues in the transmembrane region and protein/lipid interactions, whereas the fertilization assay revealed the critical involvement of the LEL region in the sperm-egg fusion, indicating the different dependency of each binding domain for other partner proteins.

Suggested Citation

  • Rie Umeda & Yuhkoh Satouh & Mizuki Takemoto & Yoshiko Nakada-Nakura & Kehong Liu & Takeshi Yokoyama & Mikako Shirouzu & So Iwata & Norimichi Nomura & Ken Sato & Masahito Ikawa & Tomohiro Nishizawa & O, 2020. "Structural insights into tetraspanin CD9 function," Nature Communications, Nature, vol. 11(1), pages 1-11, December.
  • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-15459-7
    DOI: 10.1038/s41467-020-15459-7
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-020-15459-7
    File Function: Abstract
    Download Restriction: no

    File URL: https://libkey.io/10.1038/s41467-020-15459-7?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Raviv Dharan & Yuwei Huang & Sudheer Kumar Cheppali & Shahar Goren & Petr Shendrik & Weisi Wang & Jiamei Qiao & Michael M. Kozlov & Li Yu & Raya Sorkin, 2023. "Tetraspanin 4 stabilizes membrane swellings and facilitates their maturation into migrasomes," Nature Communications, Nature, vol. 14(1), pages 1-9, December.
    2. Wenyi Zheng & Julia Rädler & Helena Sork & Zheyu Niu & Samantha Roudi & Jeremy P. Bost & André Görgens & Ying Zhao & Doste R. Mamand & Xiuming Liang & Oscar P. B. Wiklander & Taavi Lehto & Dhanu Gupta, 2023. "Identification of scaffold proteins for improved endogenous engineering of extracellular vesicles," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    3. Jinyi Zhu & Qian Qiao & Yujing Sun & Yuanpeng Xu & Haidong Shu & Zhichao Zhang & Fan Liu & Haonan Wang & Wenwu Ye & Suomeng Dong & Yan Wang & Zhenchuan Ma & Yuanchao Wang, 2023. "Divergent sequences of tetraspanins enable plants to specifically recognize microbe-derived extracellular vesicles," Nature Communications, Nature, vol. 14(1), pages 1-14, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-15459-7. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.