Figure 4
From: ZBP-89 reduces histone deacetylase 3 by degrading IkappaB in the presence of Pin1
ZBP-89 reduced HDAC3 via stimulating IκB phosphorylation. After cells were infected with Ad-ZBP-89, they were treated with CAY10576, MG132 and SN50. After the treatment, total protein was isolated and subjected to Western blot analysis for pIκB and HDAC3. Either CAY10576 or MG132 inhibited pIκB as well as HDAC3 in MIHA, PLC/PRF/5 and Pin1+/+ and Pin1−/− cells (a and b). p65/p50 inhibitory peptide SN50 suppressed NF-κB activity (e) but had no effect on pIκB (c). The level of ZBP-89 mediated HDAC3 reduction was also not affected by SN50 (c). CAY10576 did not affect the level of total IκB (d). Co-IP and Western blot were employed to test if IκB and pIκB could bind to HDAC3. IκB and pIκB were both detected in the immunoprecipitated HDAC3 complex, indicating that HDAC3 can form a complex with IκB, as well as pIκB (f).