Abstract
Caspases were identified to play an important role in apoptotic pathways and the inflammatory response. Caspase2 (C2) is the most conserved caspase among the species and belongs to the initiator and executive caspases.
Activation of C2 is rigorously regulated and happens by a maintained mechanism. Phosphorylation of procaspase2 (proC2) and its interaction with 14-3-3 protein suppresses its activity, inhibits the auto-cleavage and blocks the apoptosis.
We recently confirmed proC2:14-3-3 interaction, determined stoichiometry and identified two crucial phosphosites [1]. For biophysical characterization of proC2:14-3-3 complex we used time-resolved fluorescence spectroscopy, tryptophan fluorescence quenching and SAXS.
This work was supported by the Czech Science Foundation (Project 17-00726S).