Richard M. Epand

TL;DR: The purification of DGKε permits detailed analyses of this unique enzyme's enzymatic and conformational properties and will improve the understanding of DGkε-related diseases.

TL;DR: Liposomal assays show that the DGKalpha and, to a lesser extent, DGKzeta preferentially act on substrates containing an arachidonoyl group when this group is incorporated into alkylacylglycerols, demonstrating that the acyl chain specificity is affected by the structure of the lipid headgroup.

TL;DR: Tetraethylpyrazine, the largest and the most hydrophobic of the three drugs, elicited the most potent effect in a concentration-dependent manner, which could be attributed to the amount of incorporation of these pyrazine derivative into the liposomes, an interaction which occurs more favourably at temperatures above the gel to liquid crystalline phase-transition temperature.

TL;DR: The hypothesis that actin polymerization provides the mechanical force needed to change membrane shape nearby ER-PM contact sites, which will transiently trigger DGKε and, therefore, link enzymatic catalysis and lipid transfer in the PI-cycle is focused on.

TL;DR: The results indicate that ATP binds to GLUT 1 and destabilizes the native structure, leading to a lowering of the thermal denaturation temperature and an increase in acrylamide quenching.