An overview of recent studies from this and other laboratories on the structures and intracellular dynamics of androgen receptors is presented. Human and rat androgen receptors are unique in that, aside from their DNA and androgen binding domains, they have amino terminal regions rich in oligo- and poly(amino acids) motifs as in some regulatory and homeotic genes. Point mutations that cause sequence changes or deletion of regions of androgen receptors appear to be responsible for some cases of androgen-insensitivity. Monoclonal antibodies produced against specific regions of the androgen receptor bind to androgen receptors but not other major steroid receptors. Androgen receptors in the human and rat prostate, and monkey seminal vesicle were localized to the nucleus of target cells in these tissues with these antibodies; androgen receptors also were found in the cytoplasm of some target cells. Actinomycin D and 3'-deoxyadenosine, inhibitors of transcription, RNA processing and nucleo-cytoplasmic transport of RNA, interfere with the intracellular dynamics of androgen receptors, suggesting as we have proposed previously that androgen receptors may function not only at the site of transcription but also are involved in posttranscriptional regulation of mRNA stability and utilization.