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Structural basis for semaphorin signalling through the plexin receptor

Author

Listed:
  • Terukazu Nogi

    (Laboratory of Protein Synthesis and Expression, Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan)

  • Norihisa Yasui

    (Laboratory of Protein Synthesis and Expression, Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan
    Present address: Department of Biochemistry and Molecular Biology, The University of Chicago, 929 East 57th Street, W234, Chicago, Illinois 60637, USA.)

  • Emiko Mihara

    (Laboratory of Protein Synthesis and Expression, Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan)

  • Yukiko Matsunaga

    (Laboratory of Protein Synthesis and Expression, Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan)

  • Masanori Noda

    (Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka 565-0871, Japan)

  • Naoya Yamashita

    (Yokohama City University Graduate School of Medicine, 3-9 Fukuura, Kanazawa, Yokohama 236-0004, Japan)

  • Toshihiko Toyofuku

    (Immunology Frontier Research Center, Research Institute for Microbial Diseases, Osaka University, 3-1 Yamadaoka, Suita, Osaka 565-0871, Japan)

  • Susumu Uchiyama

    (Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka 565-0871, Japan)

  • Yoshio Goshima

    (Yokohama City University Graduate School of Medicine, 3-9 Fukuura, Kanazawa, Yokohama 236-0004, Japan)

  • Atsushi Kumanogoh

    (Immunology Frontier Research Center, Research Institute for Microbial Diseases, Osaka University, 3-1 Yamadaoka, Suita, Osaka 565-0871, Japan)

  • Junichi Takagi

    (Laboratory of Protein Synthesis and Expression, Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan)

Abstract

Plexin signalling in cell guidance The semaphorin–plexin signalling system is an important cell-guidance cue. It has a central role in the development and homeostasis of a broad range of tissues, and is widely studied for its role in neural connectivity, cancer, cell migration and immune responses. In this issue of Nature, two groups report crystal structures of key components of the semaphorin–plexin system, and propose a mechanism for plexin signalling based on their findings. Janssen et al. determined the crystal structures of complexes of the semaphorin-binding regions of plexins B1 and A2 with their cognate semaphorin ectodomains. Nogi et al. present crystal structures of complexes of semaphorin 6A and plexin A2 ectodomains.

Suggested Citation

  • Terukazu Nogi & Norihisa Yasui & Emiko Mihara & Yukiko Matsunaga & Masanori Noda & Naoya Yamashita & Toshihiko Toyofuku & Susumu Uchiyama & Yoshio Goshima & Atsushi Kumanogoh & Junichi Takagi, 2010. "Structural basis for semaphorin signalling through the plexin receptor," Nature, Nature, vol. 467(7319), pages 1123-1127, October.
    • Handle: RePEc:nat:nature:v:467:y:2010:i:7319:d:10.1038_nature09473
    DOI: 10.1038/nature09473
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    Cited by:

    1. Gergely N. Nagy & Xiao-Feng Zhao & Richard Karlsson & Karen Wang & Ramona Duman & Karl Harlos & Kamel El Omari & Armin Wagner & Henrik Clausen & Rebecca L. Miller & Roman J. Giger & E. Yvonne Jones, 2024. "Structure and function of Semaphorin-5A glycosaminoglycan interactions," Nature Communications, Nature, vol. 15(1), pages 1-16, December.

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