Functional interaction of CREB binding protein (CBP) with nuclear transport proteins and modulation by HDAC inhibitors.

摘要: Nuclear transport proteins such as CSE1, NUP93 and Importin-alpha have recently been shown to be chromatin-associated in yeast, which unexpected functions gene regulation. Here we report interactions between the mammalian histone acetyltransferase CBP with nuclear CAS (a CSE1 homologue) (Impalpha) NUP93. was found bind SRC1 interaction domain (SID) of via a leucine-rich motif N-terminus protein, that is conserved other SID-binding proteins. Coimmunoprecipitation experiments also revealed Impalpha form complex. As known acetylation target CBP/p300, recycled cytoplasm exportin CAS, investigated whether HDAC inhibitors would alter subcellular localization these Treatment COS-1 cells trichostatin A or sodium butyrate resulted sequestration envelope, accumulation aggregates, an increased number CBP-containing PML bodies per cell. In addition, HDACi treatment appeared enhance association coimmunoprecipitation experiments. Our results provide evidence for novel functional chromatin modification enzyme cells.