Ana J. García-Sáez

TL;DR: The membrane-insertion properties of different segments from antiapoptotic Bcl-x(L) and proap optotic Bax and Bid, that correspond to defined alpha helices in the structure of their soluble forms, suggest a synergistic insertion and folding of the two helices of the hairpin that could be due to charge complementarity and additional stability provided by turn-inducing residues present at the interhelical region.

TL;DR: The decrease of line tension due to peptide binding both at the domain interface in phase-separated lipid bilayers and at the pore edge in atomic force microscopy film-rupture experiments suggests that a decrease in line tension may be a general strategy of pore-forming peptides and proteins, as it affects the energetics of the pores and stabilizes the open state.

TL;DR: The results demonstrate that Bax and BakΔC21 follow similar mechanisms of membrane permeabilization characterized by the formation of protein-permeable pores of dynamic size, in agreement with the proteolipidic nature of these apoptotic pores.

TL;DR: Using fluorescence correlation spectroscopy to quantify the molecular interactions of BH3-interacting domain death agonist (BID) and its truncated form tBID with the B cell lymphoma extra-large protein truncated at the C terminus (BCLXLΔCt) in solution and in membranes, it is found that only the active form t BID binds to BCLXL΢Ct and that the membrane strongly promotes binding between them.

TL;DR: The observations demonstrate the importance of phase boundaries for Equinatoxin II activity and suggest a double role of sphingomyelin as a specific receptor for the toxin and as a promoter of the membrane organization necessary for EquInat toxin II action.