Ana J. García-Sáez

TL;DR: It is shown that peptides including any of the two α‐helix fragments of the hairpin of Bcl2 associated protein X (Bax) can independently induce release of large labelled dextrans from synthetic lipid vesicles, showing a parallel between the permeabilization mechanism of a complex regulated protein system, such as Bax, and the much simpler pore‐forming antibiotic peptides.

TL;DR: It is shown that model membranes formed from yeast total lipid extracts possess an inherent self-organization potential resulting in liquid-disordered-liquid-ordered phase coexistence at physiologically relevant temperature and provides a mechanistic explanation for lipid raft-dependent lipid and protein sorting in yeast.

TL;DR: A molecular architecture formed by a rhombus-shaped heterotetramer, which is bound to two different interacting heterotrimeric G proteins (Gi and Gs), is proposed, an important advance in understanding the molecular intricacies involved in GPCR function.

TL;DR: The poration activity of fragments from Bax and Bid are reported, containing the first alpha-helix of a colicinlike hydrophobic hairpin and the existence of two helical stretches of different orientations for the membrane-bound peptide suggest that it forms mixed lipidic/peptidic pores of toroidal structure.

TL;DR: It is shown that phosphatidylinositol 4,5-bisphosphate-dependent membrane recruitment causes FGF2 to oligomerize, which in turn triggers the formation of a lipidic membrane pore with a putative toroidal structure, suggesting a novel self-sustained mechanism of protein translocation across membranes with a transient translocation intermediate.