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TitleStructural basis of auxin binding and transport by AUX1.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 122, Issue 31, Page e2513424122, Year 2025
Publish dateAug 5, 2025
AuthorsDan Jing / Fang Kong / Xiaoli Lu / Gaoxingyu Huang / Jing Huang / Haolin Wang / Yigong Shi / Chengcheng Wang /
PubMed AbstractIndole-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). ...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 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.
External linksProc Natl Acad Sci U S A / PubMed:40720658 / PubMed Central
MethodsEM (single particle)
Resolution3.52 - 3.97 Å
Structure data

63417

9lva

EMDB-63417, PDB-9lva:
IAA-bound AUX1
Method: EM (single particle) / Resolution: 3.52 Å

63418

9lvb

EMDB-63418, PDB-9lvb:
IAA-free AUX1
Method: EM (single particle) / Resolution: 3.97 Å

Chemicals

ChemComp-IAC:
1H-INDOL-3-YLACETIC ACID / hormone*YM

Source
  • arabidopsis thaliana (thale cress)
  • homo sapiens (human)
  • lama glama (llama)
  • escherichia coli (E. coli)
KeywordsPROTEIN TRANSPORT / transport / LeuT-fold / PROTEIN TRANSPORT/IMMUNE SYSTEM / PROTEIN TRANSPORT-IMMUNE SYSTEM complex

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