Structures and mechanism of the plant PIN-FORMED auxin transporter

Auxins are hormones that have central roles and control nearly all aspects of growth and development in plants(1-3). The proteins in the PIN-FORMED (PIN) family (also known asthe auxin efflux carrier family) are key participants in this process and control auxin export from the cytosol to the extracellular space(4-9). 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.

Automated summary

This study reveals the molecular mechanism of PIN-mediated auxin transport through biophysical analysis and structural illustrations. The structure of Arabidopsis thaliana PIN8 is shown to form a homodimer with a clear auxin binding site. Additionally, the study reveals the characteristic of this transport mechanism, which resembles other transport proteins. These results provide a comprehensive molecular model for auxin recognition and transport and explain the core mechanism of polar auxin transport.