의과학과/박사[한글]
[영문]The reversible acetylation by HDAC and HAT is known to be crucial for the stability of p53 and p53-dependent apoptotic signaling. To unravel the functional significance of HDAC3 involved in apoptosis, the yeast-two hybrid assay was performed, and finally identified the proapototic protein, PDCD5 as a novel-HDAC3 interacting protein. Diverse protein-protein interacting analysis found that PDCD5 selectively interacts with HDAC3 among class I HDACs. This study shows that PDCD5-mediated HDAC3 cleavage upon apoptotic stress is dependent on caspase-3. Depletion of either PDCD5 or caspase-3 failed to induce the HDAC3-cleavage and diverse apototic event, indicating that PDCD5-capspase-3 cascade is generally essential for apoptosis. Furthermore, PDCD3-caspase-3 complex directly mediates the ectoposide-induced HDAC3 cleavage and reduction of histone deacetylase activity, and finally increase of cytoplasmic accumulation of HDAC3. More importantly, caspase-3-dependent HDAC3 cleavage by PDCD5 act as a modulator for the maintenance of p53 acetylation and stability.prohibitio
