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2022-08-02 15:23:22 By : Mr. jiang longjie

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Polar auxin transport (PAT) is unique to plants and coordinates their growth and development1,2. The PIN-FORMED (PIN) auxin transporters with remarkable asymmetrical localizations at the plasma membrane drive PAT3,4, however, their structures and transport mechanisms remain largely unknown. Here, we report three inward-facing conformation structures of the major member of the PIN family, PIN1 in Arabidopsis thaliana (AtPIN1): (i) in the apo state, (ii) in the natural auxin, indole-3-acetic acid (IAA)-bound state, and (iii) in complex with the PAT inhibitor N-1-naphthylphthalamic acid (NPA). The transmembrane domain of AtPIN1 shares a conserved NhaA-fold5. In the substrate-bound structure, IAA is coordinated through both hydrophobic stacking and hydrogen bonding. The inhibitor NPA competes with IAA for the same site of the intracellular pocket with a much higher affinity. These findings facilitate our understanding of the substrate recognition and transport mechanisms of PINs, and set up a framework for future research on the directional auxin movement, one of the most crucial processes underlying plant development.

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These authors contributed equally: Zhisen Yang, Jing Xia, Jingjing Hong

The First Affiliated Hospital of USTC, MOE Key Laboratory for Membraneless Organelles and Cellular Dynamics, Hefei National Laboratory for Physical Sciences at the Microscale, School of Life Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, China

Zhisen Yang, Jing Xia, Chenxi Zhang, Hong Wei, Wei Ying, Chunqiao Sun, Xin Liu & Linfeng Sun

CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, University of CAS, Chinese Academy of Sciences (CAS), Shanghai, China

Jingjing Hong & Dianfan Li

MOE Key Laboratory for Membraneless Organelles and Cellular Dynamics, Hefei National Laboratory for Physical Sciences at the Microscale, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, China

Lianghanxiao Sun, Yanbo Mao & Shutang Tan

Cryo-EM Center, Core Facility Center for Life Sciences, University of Science and Technology of China, Hefei, China

Institute of Science and Technology Austria (IST Austria), Am Campus 1, Klosterneuburg, Austria

Biomedical Sciences and Health Laboratory of Anhui Province, University of Science and Technology of China, Hefei, China

Xin Liu & Linfeng Sun

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Correspondence to Xin Liu or Linfeng Sun.

Uncropped western blot or Coomassie-blue staining SDS-PAGE gel scans.

Yang, Z., Xia, J., Hong, J. et al. Structural insights into auxin recognition and efflux by Arabidopsis PIN1. Nature (2022). https://doi.org/10.1038/s41586-022-05143-9

DOI: https://doi.org/10.1038/s41586-022-05143-9

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Nature (Nature) ISSN 1476-4687 (online) ISSN 0028-0836 (print)

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