ABSTRACT
Perez et al. (188) showed that cytoplasmic PMLRAR can also heterodimerize with RXR (by dimerization with the RARa moiety of PMLRAR), thereby sequestering RXR in the cytoplasm of transfected Cos-1 cells. Thus, PMLRAR also has the potential to act as a dominant inhibitor of RXR which may result in the inactivation of other nuclear receptors (such as RARs, TRs, and the vitamin D3 receptor) which require RXR for efficient DNA binding (see above, Section II.B). These types of dominant inhibition may be particularly effective in APL cells in which PMLRAR levels appear to be higher than those ofRAR.
