Structures and mechanisms of the Arabidopsis auxin transporter PIN3

Nannan Su, Aiqin Zhu, Xin Tao, Zhong Jie Ding, Shenghai Chang, Fan Ye, Yan Zhang, Cheng Zhao, Qian Chen, Jiangqin Wang, Chen Yu Zhou, Yirong Guo, Shasha Jiao, Sufen Zhang, Han Wen, Lixin Ma, Sheng Ye, Shao Jian Zheng, Fan Yang (), Shan Wu () and Jiangtao Guo ()
Additional contact information
Nannan Su: Zhejiang University School of Medicine
Aiqin Zhu: Zhejiang University School of Medicine
Xin Tao: Hubei University
Zhong Jie Ding: College of Life Sciences, Zhejiang University
Shenghai Chang: Zhejiang University School of Medicine
Fan Ye: Zhejiang University School of Medicine
Yan Zhang: Zhejiang University School of Medicine
Cheng Zhao: Zhejiang University School of Medicine
Qian Chen: Zhejiang University School of Medicine
Jiangqin Wang: Zhejiang University School of Medicine
Chen Yu Zhou: College of Life Sciences, Zhejiang University
Yirong Guo: Zhejiang University
Shasha Jiao: Zhejiang University
Sufen Zhang: Zhejiang University
Han Wen: DP Technology
Lixin Ma: Hubei University
Sheng Ye: Tianjin University
Shao Jian Zheng: College of Life Sciences, Zhejiang University
Fan Yang: Zhejiang University School of Medicine
Shan Wu: Hubei University
Jiangtao Guo: Zhejiang University School of Medicine

Nature, 2022, vol. 609, issue 7927, 616-621

Abstract: Abstract The PIN-FORMED (PIN) protein family of auxin transporters mediates polar auxin transport and has crucial roles in plant growth and development1,2. Here we present cryo-electron microscopy structures of PIN3 from Arabidopsis thaliana in the apo state and in complex with its substrate indole-3-acetic acid and the inhibitor N-1-naphthylphthalamic acid (NPA). A. thaliana PIN3 exists as a homodimer, and its transmembrane helices 1, 2 and 7 in the scaffold domain are involved in dimerization. The dimeric PIN3 forms a large, joint extracellular-facing cavity at the dimer interface while each subunit adopts an inward-facing conformation. The structural and functional analyses, along with computational studies, reveal the structural basis for the recognition of indole-3-acetic acid and NPA and elucidate the molecular mechanism of NPA inhibition on PIN-mediated auxin transport. The PIN3 structures support an elevator-like model for the transport of auxin, whereby the transport domains undergo up–down rigid-body motions and the dimerized scaffold domains remain static.

Date: 2022
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DOI: 10.1038/s41586-022-05142-w

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