Flexibility of intrinsically disordered degrons in AUX/IAA proteins reinforces auxin receptor assemblies.
In their recently released preprint, Niemeyer et al. from the Calderón Lab together with collaborators including researchers from the Martin Luther University Halle-Wittenberg show, how intrinsically disordered proteins modulate auxin receptor assembly. The authors resolve complex topology, and show that flexible intrinsically disordered regions in the targets (AUX/IAAs) cooperatively position them on the receptor. Based on their findings, the authors postulate that intrinsically disordered regions in the studied target proteins serve as signature for protein interaction and as initiation region for proteasome recruitment.
Flexibility of intrinsically disordered degrons in AUX/IAA proteins reinforces auxin 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, Luz Irina A. Calderón Villalobos
bioRxiv 787770; doi: https://doi.org/10.1101/787770