Flexibility of intrinsically disordered degrons in AUX/IAA proteins reinforces auxin co-receptor assemblies

Michael Niemeyer, Elena Moreno Castillo, Christian H. Ihling, Claudio Iacobucci, Verona Wilde, Antje Hellmuth, Wolfgang Hoehenwarter, Sophia L. Samodelov, Matias D. Zurbriggen, Panagiotis L. Kastritis, Andrea Sinz and Luz Irina A. Calderón Villalobos ()
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Michael Niemeyer: Leibniz Institute of Plant Biochemistry (IPB)
Elena Moreno Castillo: Leibniz Institute of Plant Biochemistry (IPB)
Christian H. Ihling: Martin Luther University Halle-Wittenberg
Claudio Iacobucci: Martin Luther University Halle-Wittenberg
Verona Wilde: Leibniz Institute of Plant Biochemistry (IPB)
Antje Hellmuth: Leibniz Institute of Plant Biochemistry (IPB)
Wolfgang Hoehenwarter: Leibniz Institute of Plant Biochemistry (IPB)
Sophia L. Samodelov: Heinrich-Heine University of Düsseldorf
Matias D. Zurbriggen: Heinrich-Heine University of Düsseldorf
Panagiotis L. Kastritis: Martin Luther University Halle-Wittenberg
Andrea Sinz: Martin Luther University Halle-Wittenberg
Luz Irina A. Calderón Villalobos: Leibniz Institute of Plant Biochemistry (IPB)

Nature Communications, 2020, vol. 11, issue 1, 1-18

Abstract: Abstract Cullin RING-type E3 ubiquitin ligases SCFTIR1/AFB1-5 and their AUX/IAA targets perceive the phytohormone auxin. The F-box protein TIR1 binds a surface-exposed degron in AUX/IAAs promoting their ubiquitylation and rapid auxin-regulated proteasomal degradation. Here, by adopting biochemical, structural proteomics and in vivo approaches we unveil how flexibility in AUX/IAAs and regions in TIR1 affect their conformational ensemble allowing surface accessibility of degrons. We resolve TIR1·auxin·IAA7 and TIR1·auxin·IAA12 complex topology, and show that flexible intrinsically disordered regions (IDRs) in the degron’s vicinity, cooperatively position AUX/IAAs on TIR1. We identify essential residues at the TIR1 N- and C-termini, which provide non-native interaction interfaces with IDRs and the folded PB1 domain of AUX/IAAs. We thereby establish a role for IDRs in modulating auxin receptor assemblies. By securing AUX/IAAs on two opposite surfaces of TIR1, IDR diversity supports locally tailored positioning for targeted ubiquitylation, and might provide conformational flexibility for a multiplicity of functional states.

Date: 2020
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DOI: 10.1038/s41467-020-16147-2

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