Florine Dupeux

TL;DR: In this article, PYL5, PYL6 and PYL8 were identified as a cytosolic and nuclear ABA receptor that activates ABA signaling through direct inhibition of clade A PP2Cs.

TL;DR: The crystal structure of Arabidopsis thaliana PYR1 is presented, which consists of a dimer in which one of the subunits is bound to ABA, indicating that conformational changes in these loops have a critical role in the stabilization of the hormone–receptor complex.

TL;DR: Two distinct classes of receptors are identified, dimeric and monomeric, with different intrinsic affinities for ABA and whose differential properties are determined by the oligomeric state of their apo forms, illustrating how receptor oligomerization can modulate hormonal responses and more generally, the sensitivity of a ligand‐dependent signalling system.

TL;DR: The utility of nanobodies to trap and characterize intermediates of β2-microglobulin (β2m) amyloidogenesis by X-ray crystallography is demonstrated and domain swapping is identified as a plausible mechanism of self-association of this amyloidsogenic protein.

TL;DR: A new family of soluble ABA receptors, named PYR/PYL/RCAR, has emerged as ABA sensors able to inhibit the activity of specific protein phosphatases type-2C (PP2Cs) in an ABA-dependent manner.