Abstract：
:Pin1 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.
journal_name
Oncogenejournal_title
Oncogeneauthors
Chen HZ,Li L,Wang WJ,Du XD,Wen Q,He JP,Zhao BX,Li GD,Zhou W,Xia Y,Yang QY,Hew CL,Liou YC,Wu Qdoi
10.1038/onc.2011.463subject
Has Abstractpub_date
2012-06-07 00:00:00pages
2876-87issue
23eissn
0950-9232issn
1476-5594pii
onc2011463journal_volume
31pub_type
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