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Structure paper

TitleStructures and mechanism of the plant PIN-FORMED auxin transporter.
Journal, issue, pagesNature, Vol. 609, Issue 7927, Page 605-610, Year 2022
Publish dateJun 29, 2022
AuthorsKien Lam Ung / Mikael Winkler / Lukas Schulz / Martina Kolb / Dorina P Janacek / Emil Dedic / David L Stokes / Ulrich Z Hammes / Bjørn Panyella Pedersen /
PubMed AbstractAuxins are hormones that have central roles and control nearly all aspects of growth and development in plants. The proteins in the PIN-FORMED (PIN) family (also known as the auxin efflux carrier ...Auxins are hormones that have central roles and control nearly all aspects of growth and development in plants. 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 space. 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.
External linksNature / PubMed:35768502 / PubMed Central
MethodsEM (single particle)
Resolution2.89 - 3.44 Å
Structure data

14115

7qp9

EMDB-14115, PDB-7qp9:
Outward-facing apo-form of auxin transporter PIN8
Method: EM (single particle) / Resolution: 2.89 Å

14116

7qpa

EMDB-14116, PDB-7qpa:
Outward-facing auxin bound form of auxin transporter PIN8
Method: EM (single particle) / Resolution: 3.18 Å

14117

7qpc

EMDB-14117, PDB-7qpc:
Inward-facing NPA bound form of auxin transporter PIN8
Method: EM (single particle) / Resolution: 3.44 Å

EMDB-14118: Outward-facing apo-form of auxin transporter PIN8 in detergent
Method: EM (single particle) / Resolution: 3.27 Å

Chemicals

ChemComp-DLP:
1,2-DILINOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE / phospholipid*YM

ChemComp-HOH:
WATER

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

ChemComp-E7O:
2-(naphthalen-1-ylcarbamoyl)benzoic acid

Source
  • arabidopsis thaliana (thale cress)
KeywordsMEMBRANE PROTEIN / Auxin transport / AEC family / BART superfamily

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