Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

The human androgen receptor (hAR) is a ligand-dependent transcription factor responsible for the development of the male phenotype. The mechanism whereby nuclear translocation of the hAR is induced by its natural ligand 5alpha-dihydrotestosterone is a phenomenon not fully understood. The two-hybrid interaction trap assay has been used to isolate proteins that interact with the hAR in an attempt to identify molecules involved in hAR transactivation and movement. We have identified the actin-binding protein filamin, a 280-kDa component of the cytoskeleton, as an hAR interacting protein. This interaction is ligand independent but is enhanced in its presence. The functional significance of this interaction was analyzed using a cell line deficient in filamin via transient expression of a green fluorescent protein-hAR chimera. In filamin-deficient cells this revealed that hAR remained cytoplasmic even after prolonged exposure to synthetic ligand. Nuclear shuttling was restored when this cell line regained wild-type expression of filamin. These data suggest a novel role for filamin, implicating it as an important molecule in AR movement from the cytoplasm to the nucleus.

Original publication




Journal article


Mol Endocrinol

Publication Date





1618 - 1626


Actins, Animals, Antibodies, Monoclonal, Binding Sites, Biological Transport, Cell Nucleus, Contractile Proteins, Cross-Linking Reagents, DNA, Dihydrotestosterone, Enhancer Elements, Genetic, Filamins, Green Fluorescent Proteins, Humans, Immunosorbent Techniques, Luminescent Proteins, Mice, Microfilament Proteins, Peptide Fragments, Receptors, Androgen, Recombinant Fusion Proteins, Response Elements, Steroids, Transcription, Genetic, Transcriptional Activation, Transfection