221117 nanion 1026x196 03Research Ins]i[ghts: Nanion’s Transporter Webinar Series 2022

Join us over the course of a year as we dive into a series of 3 sessions (a collection of scientific presentations/talks; representing academia & industry alike) scheduled across 2022. Whether you join us from an academic or industry setting, we invite you to join us a cross the course of the year to dive deep into all things transporters. Our aim is to provide a unique platform for researchers globally to share their work and engage in meaningful active discussions. All talks will be live and accessible on-demand upon completion of the scheduled event.


28.06.2022 - Structures and mechanism of the plant PIN-FORMED auxin transporter

Session Abstract: 

Plant transporters need to transport a broad spectrum of substrates across membranes to regulate growth, development, defense, and survival. Auxines were the first of the major plant hormones to be discovered. In session one of our Transporter Webinar Series 2022, Bjørn Panyella Pedersen and Ulrich Hammes will present structural and electrophysiological data from their collaborative work on the auxin influx carrier PIN8.

Speakers: 

Asc prof. Bjørn Panyella Pedersen. Dept of Molecular Biology and Genetics
Aarhus University, Denmark

Asc prof. Ulrich Hammes. Plant Systems Biology
Technical University of Munich, Germany

Title: Structures and mechanism of the plant PIN-FORMED auxin transporter

Abstract: 

Auxins are central hormones in all plants and controls virtually all aspects of growth and development. The PIN-FORMED (PIN) protein family is a key player in this process. Here we present biophysical analysis and structures of Arabidopsis thaliana PIN8 at 2.9-3.4 Å resolution; two outward facing conformations with and without auxin bound, and one inward facing conformation with the known inhibitor and herbicide naphthylphthalamic acid (NPA) bound. The structure forms a homo-dimer 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 by biophysical analysis to be independent of proton and ion gradients and likely driven by the negative charge of the auxin. Our results provide the first comprehensive molecular model for auxin recognition and transport by PINs.

Watch On-Demand Here


Access the Q&A from the webinar here

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