Structural basis of auxin binding and transport by Arabidopsis thaliana AUX1
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Abstract
Indole-3-acetic acid (IAA), the major form of auxin, is essential for plant growth. Auxin resistant 1 (AUX1), the first identified auxin importer, plays a crucial role in polar auxin transport (PAT). Here, we present cryo-EM structures of Arabidopsis thaliana AUX1 in the IAA-free and IAA-bound states. AUX1 exists as a monomer that contains 11 transmembrane helices (TMs). TMs 1 to 5 and 6 to 10 constitute the two halves of a classic LeuT-fold, and TM11 interacts with both halves at the interface. In the IAA-bound state, IAA is specifically recognized in a central pocket formed by TM1, TM3, TM6, and TM8. In the presence of IAA, TM1 and TM6 undergo marked conformational changes that are critical for IAA transport. His249 stands out to be a key residue for substrate uptake and release. Our structures reveal the molecular basis for AUX1-mediated IAA binding and transport.
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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works
Accurate structure prediction of biomolecular interactions with AlphaFold 3
Abramson, J., Adler, J., Dunger, J., Evans, R., Green, T., Pritzel, A., Ronneberger, O., Willmore, L., Ballard, A. J., Bambrick, J., et al. (2024) · Nature · doi:10.1038/s41586-024-07487-w · Cited by 15,861 · see citing works
Cryo-EM structure of the human Asc-1 transporter complex
Li, Y., Guo, Y., Bröer, A., Dai, L., Brӧer, S., & Yan, R. (2024) · Nature Communications · doi:10.1038/s41467-024-47468-1 · Cited by 12 · see citing works
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- Authors
- Jing, D., Kong, F., Lu, X., Huang, G., Huang, J., Wang, H., Shi, Y., & Wang, C.
- Affiliations
- Westlake University (CN)
- Center for Life Sciences (CN)
- Corresponding author
- Jing, Dan
- Kong, Fang
- Shi, Yigong
- Wang, Chengcheng
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2025-07-28
- Volume
- 122
- Issue
- 31
- Pages
- e2513424122-e2513424122
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC12337342
- OpenAlex
- W4412703965
- Cited by
- 4
- References
- 3
- Citations by year
- 2026: 4
- FWCI
- 2.16
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion, cc-by-nc-nd)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc)
- PubMed (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- Funders
- Key Research and Development Program of Zhejiang Province (2020C04001)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- AUX1, indole-3-acetic acid, auxin transport, polar auxin transport, transmembrane helices, conformational change, Arabidopsis thaliana, cryo-EM structure
- MeSH terms
- Biological Transport, Indoleacetic Acids, Models, Molecular, Protein Binding, Arabidopsis, Cryoelectron Microscopy, Arabidopsis Proteins
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