Pin1 and Nuclear Receptors: A New Language?

被引：10

作者：

La Montagna, Raffaele ^{[1
,2
,3
]}

Caligiuri, Isabella ^{[1
,2
,3
,4
]}

Giordano, Antonio ^{[1
,2
,3
,4
,5
]}

Rizzolio, Flavio ^{[1
,6
,7
]}

机构：

[1] Temple Univ, Sbarro Inst Canc Res & Mol Med, Ctr Biotechnol, Coll Sci & Technol, Philadelphia, PA 19122 USA

[2] Human Hlth Fdn, Terni, PG, Italy

[3] Human Hlth Fdn, Spoleto, PG, Italy

[4] Univ Siena, Dept Human Pathol & Oncol, I-53100 Siena, Italy

[5] Pascale Fdn, Natl Canc Inst, Canc Res Ctr, INT CROM, Mercogliano, Italy

[6] Natl Canc Inst, Div Expt & Clin Pharmacol, Dept Mol Biol & Translat Res, Aviano, PN, Italy

[7] Ctr Mol Biomed, Aviano, PN, Italy

来源：

JOURNAL OF CELLULAR PHYSIOLOGY | 2013年 / 228卷 / 09期

基金：

欧洲研究理事会;

关键词：

PROLYL-ISOMERASE PIN1; RETINOIC ACID; ALPHA; STABILITY;

D O I：

10.1002/jcp.24316

中图分类号：

Q2 [细胞生物学];

学科分类号：

071013 [干细胞生物学];

摘要：

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: 17991801, 2013. (c) 2012 Wiley Periodicals, Inc.

引用

收藏

页码：1799 / 1801

页数：3

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