Structure of IZUMO1-JUNO reveals sperm-oocyte recognition during mammalian fertilization

Umeharu Ohto, Hanako Ishida, Elena Krayukhina, Susumu Uchiyama, Naokazu Inoue, Toshiyuki Shimizu

研究成果: Article査読

78 被引用数 (Scopus)

抄録

Fertilization is a fundamental process in sexual reproduction, creating a new individual through the combination of male and female gametes. The IZUMO1 sperm membrane protein and its counterpart oocyte receptor JUNO have been identified as essential factors for sperm-oocyte interaction and fusion. However, the mechanism underlying their specific recognition remains poorly defined. Here, we show the crystal structures of human IZUMO1, JUNO and the IZUMO1-JUNO complex, establishing the structural basis for the IZUMO1-JUNO-mediated sperm-oocyte interaction. IZUMO1 exhibits an elongated rod-shaped structure comprised of a helical bundle IZUMO domain and an immunoglobulin-like domain that are each firmly anchored to an intervening β-hairpin region through conserved disulfide bonds. The central β-hairpin region of IZUMO1 provides the main platform for JUNO binding, while the surface located behind the putative JUNO ligand binding pocket is involved in IZUMO1 binding. Structure-based mutagenesis analysis confirms the biological importance of the IZUMO1-JUNO interaction. This structure provides a major step towards elucidating an essential phase of fertilization and it will contribute to the development of new therapeutic interventions for fertility, such as contraceptive agents.

本文言語English
ページ(範囲)566-569
ページ数4
ジャーナルNature
534
7608
DOI
出版ステータスPublished - 2016 6月 15
外部発表はい

ASJC Scopus subject areas

  • 一般

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