Reposted by Deepanshi Gahlot
@deepanshigahlot.bsky.social, @jesucastin.bsky.social, @lipithukral.bsky.social and colleagues identify a lipid-triggered allosteric site in LC3 that remodels its receptor binding interface upon membrane interaction
dlvr.it
A programmable lipid-triggered allosteric site modulates LC3 LIR receptor binding activity - Nature Communications
The allosteric mechanisms by which lipid binding controls protein activity remain poorly understood. Here, the authors identify a lipid-triggered allosteric site in LC3 that remodels its receptor-binding interface upon membrane interaction. This site can be engineered to precisely tune LC3-LIR interactions, offering a new strategy to regulate selective autophagy.