Pin1 is a unique enzyme that can isomerize specific phospho-Ser/Thr-Pro peptide bonds, inducing a conformational change in the target protein. Such activity represents a novel and tightly controlled signaling mechanism regulating a spectrum of protein functions during the normal physiology of the cell and in pathological conditions. Our last study demonstrated that Pin1 interacts with the androgen receptor protein and that this interaction is important for its transcriptional activity. Here, we consider the activity that Pin1 plays on the N-terminal domain of different nuclear receptors and provide an interpretation of this phenomenon.
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