N. Sibille

LIPIDS MODULATE THE DYNAMICS OF GPCR:β-ARRESTIN INTERACTION

This study shows that PI(4,5)P2 modulates the orientation and receptor interaction of β-arrestin 1 through its interaction with the C-edge loop.

Phosphorylation motif dictates GPCR C-terminal domain conformation and arrestin interaction

The paper investigates how phosphorylation of GPCR C-terminal domains affects their conformation and arrestin interaction, revealing phosphorylation-dependent structural changes that influence signaling outcomes.

A single domain intrabody targeting the follicle-stimulating hormone receptor (FSHR) impacts FSH-induced G protein-dependent signalling

The paper characterizes an intrabody that modulates FSHR signaling by reducing cAMP production without affecting Gs recruitment.

Site-Specific Introduction of Alanines for the NMR Investigation of Low-Complexity Regions and Large Biomolecular Assemblies

This paper introduces a method to site-specifically incorporate isotopically labeled alanines into proteins for NMR studies, enabling structural analysis of large biomolecular assemblies and low-complexity regions.

The structure of pathogenic huntingtin exon-1 defines the bases of its aggregation propensity

This study investigates how the structure of pathogenic huntingtin exon-1 with expanded poly-Q tracts influences its aggregation propensity and fibril formation.

Structure of the vasopressin hormone-V2 receptor-β-arrestin1 ternary complex

The paper reports the cryo-EM structure of the V2 receptor-{beta}-arrestin1 complex, revealing structural variability in GPCR-arrestin interactions.

Structural insights into the cooperative interaction of the intrinsically disordered co-activator TIF2 with retinoic acid receptor heterodimer (RXR/RAR)

The paper determines the structural features of TIF2NRID and its cooperative binding to RXR/RAR, revealing partially structured regions and the role of flanking sequences.

Multivalent interactions between eIF4G1, Pub1 and Pab1 drive the formation of protein condensates

The paper studies interactions between eIF4G1, Pub1, and Pab1 using NMR and SAXS, revealing their role in forming protein condensates and regulating stress granule formation.

Interplay of protein disorder in retinoic acid receptor heterodimer and its corepressor regulates gene expression

This study shows that the structural dynamics of the H12 helix in RXR/RAR heterodimers and the intrinsic disorder of N-CoR regulate gene expression through conformational changes and corepressor complex formation.