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Structural insights into auxin recognition and efflux by Arabidopsis PIN1

Author

Listed:
  • Zhisen Yang

    (University of Science and Technology of China)

  • Jing Xia

    (University of Science and Technology of China)

  • Jingjing Hong

    (University of CAS, Chinese Academy of Sciences (CAS))

  • Chenxi Zhang

    (University of Science and Technology of China)

  • Hong Wei

    (University of Science and Technology of China)

  • Wei Ying

    (University of Science and Technology of China)

  • Chunqiao Sun

    (University of Science and Technology of China)

  • Lianghanxiao Sun

    (University of Science and Technology of China)

  • Yanbo Mao

    (University of Science and Technology of China)

  • Yongxiang Gao

    (University of Science and Technology of China)

  • Shutang Tan

    (University of Science and Technology of China)

  • Jiří Friml

    (Institute of Science and Technology Austria (IST Austria))

  • Dianfan Li

    (University of CAS, Chinese Academy of Sciences (CAS))

  • Xin Liu

    (University of Science and Technology of China
    University of Science and Technology of China)

  • Linfeng Sun

    (University of Science and Technology of China
    University of Science and Technology of China)

Abstract

Polar auxin transport is unique to plants and coordinates their growth and development1,2. The PIN-FORMED (PIN) auxin transporters exhibit highly asymmetrical localizations at the plasma membrane and drive polar auxin transport3,4; however, their structures and transport mechanisms remain largely unknown. Here, we report three inward-facing conformation structures of Arabidopsis thaliana PIN1: the apo state, bound to the natural auxin indole-3-acetic acid (IAA), and in complex with the polar auxin transport inhibitor N-1-naphthylphthalamic acid (NPA). The transmembrane domain of PIN1 shares a conserved NhaA fold5. In the substrate-bound structure, IAA is coordinated by both hydrophobic stacking and hydrogen bonding. NPA competes with IAA for the same site at the intracellular pocket, but with a much higher affinity. These findings inform our understanding of the substrate recognition and transport mechanisms of PINs and set up a framework for future research on directional auxin transport, one of the most crucial processes underlying plant development.

Suggested Citation

  • Zhisen Yang & Jing Xia & Jingjing Hong & Chenxi Zhang & Hong Wei & Wei Ying & Chunqiao Sun & Lianghanxiao Sun & Yanbo Mao & Yongxiang Gao & Shutang Tan & Jiří Friml & Dianfan Li & Xin Liu & Linfeng Su, 2022. "Structural insights into auxin recognition and efflux by Arabidopsis PIN1," Nature, Nature, vol. 609(7927), pages 611-615, September.
    • Handle: RePEc:nat:nature:v:609:y:2022:i:7927:d:10.1038_s41586-022-05143-9
    DOI: 10.1038/s41586-022-05143-9
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