Pin1 acts as a negative regulator of the G2/M transition by interacting with the Aurora-A-Bora complex

Yu Cheng Lee, Jenny Que, Yu Chia Chen, Jen Tai Lin, Yih Cherng Liou, Po Chi Liao, Yu Peng Liu, Kuen Haur Lee, Li Ching Lin, Michael Hsiao, Liang Yi Hung, Chi Ying Huang, Pei Jung Lu

Research output: Contribution to journalArticlepeer-review

33 Citations (Scopus)


Pin1 was the first prolyl isomerase identified that is involved in cell division. The mechanism by which Pin1 acts as a negative regulator of mitotic activity in G2 phase remains unclear. Here, we found that Aurora A can interact with and phosphorylate Pin1 at Ser16, which suppresses the G2/M function of Pin1 by disrupting its binding ability and mitotic entry. Our results also show that phosphorylation of Bora at Ser274 and Ser278 is crucial for binding of Pin1. Through the interaction, Pin1 can alter the cytoplasmic translocation of Bora and promote premature degradation by β-TrCP, which results in a delay in mitotic entry. Together with the results that Pin1 protein levels do not significantly fluctuate during cell-cycle progression and Aurora A suppresses Pin1 G2/M function, our data demonstrate that a gain of Pin1 function can override the Aurora-A-mediated functional suppression of Pin1. Collectively, these results highlight the physiological significance of Aurora-A-mediated Pin1 Ser16 phosphorylation for mitotic entry and the suppression of Pin1 is functionally linked to the regulation of mitotic entry through the Aurora-A-Bora complex.

Original languageEnglish
Pages (from-to)4862-4872
Number of pages11
JournalJournal of Cell Science
Issue number21
Publication statusPublished - Nov 1 2013


  • Aurora a
  • Bora
  • G2/M negative regulator
  • Pin1

ASJC Scopus subject areas

  • Cell Biology


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