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Pin1 and Nuclear Receptors: A New Language?
Author(s) -
La Montagna Raffaele,
Caligiuri Isabella,
Giordano Antonio,
Rizzolio Flavio
Publication year - 2013
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.24316
Subject(s) - pin1 , receptor , microbiology and biotechnology , transcriptional activity , androgen receptor , nuclear receptor , mechanism (biology) , signal transduction , biology , cell , domain (mathematical analysis) , chemistry , enzyme , biochemistry , isomerase , genetics , gene , physics , gene expression , transcription factor , mathematical analysis , mathematics , prostate cancer , cancer , quantum mechanics
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. J. Cell. Physiol. 228: 1799–1801, 2013. © 2012 Wiley Periodicals, Inc.