p73 competes with co-activators and recruits histone deacetylase to NF-Y in the repression of PDGF beta-receptor.

We investigated mechanisms of the p73alpha-mediated repression of the platelet-derived growth factor beta-receptor (PDGFRB) promoter caused by its interaction with NF-Y. Treatment of cells with the histone deacetylase (HDAC) inhibitor, Trichostatin A, increases PDGFRB promoter activity through the CCAAT motif and counteracts the repression caused by p73alpha. Activation of the PDGFRB promoter by the co-activator p300 also occurs through the CCAAT motif.

pRb, Myc and p53 are critically involved in SV40 large T antigen repression of PDGF beta-receptor transcription.

The expression of the PDGF beta-receptor is tightly regulated during a normal cell cycle. c-Myc and p73alpha repress transcription of the receptor through interaction with NF-Y. In ST15A cells which stably express the temperature-sensitive SV40 large T antigen (LT) the receptor expression and ligand binding decreased under the permissive condition.

p73 independent of c-Myc represses transcription of platelet-derived growth factor beta-receptor through interaction with NF-Y.

We recently reported that c-Myc represses the transcription of platelet-derived growth factor (PDGF) beta-receptor (Izumi, H., Molander, C., Penn, L.