Structures and mechanism of the plant PIN-FORMED auxin transporter

Nature. 2022 Sep;609(7927):605-610. doi: 10.1038/s41586-022-04883-y. Epub 2022 Jun 29.


Auxins are hormones that have central roles and control nearly all aspects of growth and development in plants1-3. The proteins in the PIN-FORMED (PIN) family (also known as the auxin efflux carrier family) are key participants in this process and control auxin export from the cytosol to the extracellular space4-9. Owing to a lack of structural and biochemical data, the molecular mechanism of PIN-mediated auxin transport is not understood. Here we present biophysical analysis together with three structures of Arabidopsis thaliana PIN8: two outward-facing conformations with and without auxin, and one inward-facing conformation bound to the herbicide naphthylphthalamic acid. The structure forms a homodimer, with each monomer divided into a transport and scaffold domain with a clearly defined auxin binding site. Next to the binding site, a proline-proline crossover is a pivot point for structural changes associated with transport, which we show to be independent of proton and ion gradients and probably driven by the negative charge of the auxin. The structures and biochemical data reveal an elevator-type transport mechanism reminiscent of bile acid/sodium symporters, bicarbonate/sodium symporters and sodium/proton antiporters. Our results provide a comprehensive molecular model for auxin recognition and transport by PINs, link and expand on a well-known conceptual framework for transport, and explain a central mechanism of polar auxin transport, a core feature of plant physiology, growth and development.

MeSH terms

  • Antiporters / metabolism
  • Arabidopsis Proteins* / chemistry
  • Arabidopsis Proteins* / metabolism
  • Arabidopsis* / chemistry
  • Arabidopsis* / metabolism
  • Bicarbonates / metabolism
  • Bile Acids and Salts / metabolism
  • Binding Sites
  • Biological Transport
  • Herbicides / metabolism
  • Indoleacetic Acids* / chemistry
  • Indoleacetic Acids* / metabolism
  • Membrane Transport Proteins* / chemistry
  • Membrane Transport Proteins* / metabolism
  • Phthalimides / metabolism
  • Plant Growth Regulators / chemistry
  • Plant Growth Regulators / metabolism
  • Proline / metabolism
  • Protein Domains
  • Protein Multimerization
  • Protons
  • Sodium / metabolism
  • Symporters / metabolism


  • Antiporters
  • Arabidopsis Proteins
  • Bicarbonates
  • Bile Acids and Salts
  • Herbicides
  • Indoleacetic Acids
  • Membrane Transport Proteins
  • PIN8 protein, Arabidopsis
  • Phthalimides
  • Plant Growth Regulators
  • Protons
  • Symporters
  • alpha-naphthylphthalamic acid
  • Proline
  • Sodium