Fluorescent resonance energy transfer -based biosensor for detecting conformational changes of Pin1

Masafumi Hidaka, Emiko Okabe, Kodai Hatakeyama, Heather Zook, Chiyoko Uchida, Takafumi Uchida

    Research output: Contribution to journalArticlepeer-review

    2 Citations (Scopus)


    Pin1, a peptidyl prolyl cis/trans isomerase (PPIase), regulates the activity and stability of various phosphorylated proteins. Pin1 consists of a PPIase domain and WW domain, both of which are required for the function of Pin1. However, how the behavior of these domains changes upon binding to phosphorylated proteins has not been analyzed. We created a Fluorescent Resonance Energy Transfer (FRET)-based biosensor “CPinY” which is composed of Pin1 flanked by CFP and YFP, and analyzed the interaction between Pin1 and c-Myc. Our results indicated that the dual phosphorylation of c-Myc at Thr58 and Ser62 is essential for tight interaction with Pin1. Additionally, this interaction caused a significant conformational change in Pin1. Our CPinY biosensor also detected a novel type of inhibitor of Pin1 function. We believe that his biosensor will be a novel drug screening technology targeting Pin1.

    Original languageEnglish
    Pages (from-to)399-404
    Number of pages6
    JournalBiochemical and biophysical research communications
    Issue number2
    Publication statusPublished - 2018 Oct 28


    • Biosensor
    • Conformation
    • FRET
    • PPIase
    • Phosphorylation
    • c-Myc

    ASJC Scopus subject areas

    • Biophysics
    • Biochemistry
    • Molecular Biology
    • Cell Biology


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