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Updated: Dec 25, 2025

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Structural insights into tetraspanin CD9 function.

Rie Umeda1, Yuhkoh Satouh2,3, Mizuki Takemoto1,4

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|April 2, 2020
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Tetraspanins like CD9 have unique shapes influencing cell membrane curvature and remodeling. Their interaction with EWI-2 and the large extracellular loop are crucial for sperm-egg fusion.

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Area of Science:

  • Molecular and Cellular Biology
  • Structural Biology

Background:

  • Tetraspanins are crucial cell surface proteins involved in diverse physiological processes.
  • They possess a characteristic structure with four transmembrane domains and extracellular loops.
  • Tetraspanins associate with various proteins to mediate cellular functions.

Purpose of the Study:

  • To elucidate the structural basis of CD9 function.
  • To investigate the molecular interaction between CD9 and its partner protein EWI-2.
  • To understand the role of different CD9 domains in cellular processes like fertilization.

Main Methods:

  • X-ray crystallography was used to determine the structure of CD9.
  • Cryo-electron microscopy was employed to visualize the CD9-EWI-2 complex.
  • Fertilization assays were conducted to assess functional roles.

Main Results:

  • The crystal structure of CD9 revealed a reversed cone-like molecular shape.
  • CD9's shape induces membrane curvature, explaining its localization and role in membrane remodeling.
  • CD9-EWI-2 interaction is mediated by transmembrane residues and protein/lipid interactions.
  • The large extracellular loop (LEL) of CD9 is critical for sperm-egg fusion.

Conclusions:

  • CD9's unique structure drives membrane curvature and remodeling.
  • Distinct domains of CD9 mediate interactions with partner proteins and have specific functional roles.
  • Understanding CD9-EWI-2 interactions provides insights into tetraspanin-mediated cellular processes.