Ernesto Arias-Palomo

TL;DR: The structure of Epac2 in complex with a cAMP analogue (Sp-cAMPS) and RAP1B by X-ray crystallography and single particle electron microscopy shows that cAMP binding causes conformational changes that allow the cyclic nucleotide binding domain to swing from a position blocking the Rap binding site towards a docking site at the Ras exchange motif domain.

TL;DR: Large-scale conformational changes induced by SMG-8 afterSMG-9-mediated recruitment tune SMG -1 kinase activity to modulate NMD.

TL;DR: The target of rapamycin (TOR) is a large (281 kDa) conserved Ser/Thr protein kinase that functions as a central controller of cell growth that assembles into two distinct multiprotein complexes: TORC1 and TORC2.

TL;DR: This structure of endogenously assembled pontin/reptin complexes is different than previously described structures, suggesting that pontin and reptin could acquire distinct structural states to regulate their broad functions as molecular motors and scaffolds for nucleic acids and proteins.

TL;DR: Cryo-EM structures of the protoxin and the protease-activated state of Vip3Aa are presented which shed light on the molecular basis for Vip2 activation and function and serves as a strong foundation for the development of more efficient insecticidal proteins.