Please use this identifier to cite or link to this item: https://doi.org/10.1038/onc.2011.463
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dc.titleProlyl isomerase Pin1 stabilizes and activates orphan nuclear receptor TR3 to promote mitogenesis
dc.contributor.authorChen, H.-Z.
dc.contributor.authorLi, L.
dc.contributor.authorWang, W.-J.
dc.contributor.authorDu, X.-D.
dc.contributor.authorWen, Q.
dc.contributor.authorHe, J.-P.
dc.contributor.authorZhao, B.-X.
dc.contributor.authorLi, G.-D.
dc.contributor.authorZhou, W.
dc.contributor.authorXia, Y.
dc.contributor.authorYang, Q.-Y.
dc.contributor.authorHew, C.-L.
dc.contributor.authorLiou, Y.-C.
dc.contributor.authorWu, Q.
dc.date.accessioned2014-10-27T08:37:31Z
dc.date.available2014-10-27T08:37:31Z
dc.date.issued2012-06-07
dc.identifier.citationChen, H.-Z., Li, L., Wang, W.-J., Du, X.-D., Wen, Q., He, J.-P., Zhao, B.-X., Li, G.-D., Zhou, W., Xia, Y., Yang, Q.-Y., Hew, C.-L., Liou, Y.-C., Wu, Q. (2012-06-07). Prolyl isomerase Pin1 stabilizes and activates orphan nuclear receptor TR3 to promote mitogenesis. Oncogene 31 (23) : 2876-2887. ScholarBank@NUS Repository. https://doi.org/10.1038/onc.2011.463
dc.identifier.issn09509232
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/101468
dc.description.abstractPin1 regulates a subset of phosphoproteins by isomerizing phospho-Ser/Thr-Pro motifs via a post-phosphorylation mechanism. Here, we characterize TR3 as a novel Pin1 substrate, and the mitogenic function of TR3 depends on Pin1-induced isomerization. There are at least three phospho-Ser-Pro motifs on TR3 that bind to Pin1. The Ser95-Pro motif of TR3 is the key site through which Pin1 enhances TR3 stability by retarding its degradation. Pin1 can also catalyze TR3 through phospho-Ser431-Pro motif, which is phosphorylated by extracellular signal-regulated kinase 2 (ERK2), resulting in enhanced TR3 transactivation. Furthermore, Pin1 not only facilitates TR3 targeting to the promoter of cyclin D2, a novel downstream target of TR3, but also promotes TR3 to recruit p300, thereby inducing cell proliferation. Importantly, we found that Pin1 is indispensable for TR3 to promote tumor growth both in vitro and in vivo. Our study thus suggests that Pin1 has an important role in cell proliferation by isomerizing TR3. © 2012 Macmillan Publishers Limited All rights reserved.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1038/onc.2011.463
dc.sourceScopus
dc.subjectcell proliferation
dc.subjectorphan receptor TR3
dc.subjectphosphorylation
dc.subjectprolyl isomerase pin1
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1038/onc.2011.463
dc.description.sourcetitleOncogene
dc.description.volume31
dc.description.issue23
dc.description.page2876-2887
dc.description.codenONCNE
dc.identifier.isiut000305277900007
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