Hsp70 is known to bind directly to Bax, suppressing apoptosis. However, the mechanisms by which Bax dissociates from Hsp70 during apoptosis have remained largely unknown. In a recent study, researchers developed an efficient fluorescence resonance energy transfer (FRET) system using Hsp70-YFP and a fluorescent amino acid (ANAP)-incorporated Bax, generated through genetic code expansion technology. This FRET system was applied to understand how apoptosis-inducing substances dissociate Bax from Hsp70. The study found that Bax activators binding to specific Bax trigger sites inhibited the Bax-Hsp70 interaction, whereas Bax activators blocking phosphorylation at the S184 site did not affect this interaction. Additionally, an inhibitor of the Hsp70-Hsp40 interaction blocked the Bax-Hsp70 interaction. p53 activators and death ligands enhanced Bax dissociation from Hsp70 by activating BH3-only proteins. These findings suggest that FRET systems with ANAP-incorporated and YFP fusion proteins are valuable tools for studying various protein-protein interactions.-Scientific Journal cover design by scapiens
[Scientific Journal cover design] Low-Thermal-Budget Fluorite-Structure Ferroelectrics for Future Electronic Device Applications
In article number 2100028, Jiyoung Kim, Si Joon Kim, and their team review key factors involved in developing fluorite-structure ferroelectrics
