Article
Flexibility of intrinsically disordered degrons in AUX/IAA proteins reinforces auxin co-receptor assemblies.
Nature communications - 8 May 2020
Niemeyer Michael, Moreno Castillo Elena, Ihling Christian H, Iacobucci Claudio, Wilde Verona, Hellmuth Antje, Hoehenwarter Wolfgang, Samodelov Sophia L, Zurbriggen Matias D, Kastritis Panagiotis L, Sinz Andrea, Calderón Villalobos Luz Irina A
Abstract excerpt
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...
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