title: Pin1 and nuclear receptors: a new language?
abstract: 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.
authors.affiliation: Sbarro Institute for Cancer Research and Molecular Medicine, Center for Biotechnology, College of Science and Technology, Temple University, Philadelphia, Pennsylvania, USA.
authors.forename: Raffaele
authors.initials: R
authors.lastname: La Montagna
authors.forename: Isabella
authors.initials: I
authors.lastname: Caligiuri
authors.forename: Antonio
authors.initials: A
authors.lastname: Giordano
authors.forename: Flavio
authors.initials: F
authors.lastname: Rizzolio
mesh_terms: D001665:Binding Sites; D006801:Humans; D000072340:NIMA-Interacting Peptidylprolyl Isomerase; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D019696:Peptidylprolyl Isomerase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D018160:Receptors, Cytoplasmic and Nuclear / Q000737:chemistry* / Q000378:metabolism
chemical_list: D000072340:NIMA-Interacting Peptidylprolyl Isomerase; D010455:Peptides; D018160:Receptors, Cytoplasmic and Nuclear; C000606846:PIN1 protein, human; D019696:Peptidylprolyl Isomerase