Development of a high-throughput screening system targeting the protein-protein interactions between PRL and CNNM

• Published in: Scientific reports Vol. 14; no. 1; pp. 25432 - 13
• Main Authors: Funato, Yosuke, Mimura, Mai, Nunomura, Kazuto, Lin, Bangzhong, Fujii, Shintarou, Haruta, Junichi, Miki, Hiroaki
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 25.10.2024; Nature Publishing Group; Nature Portfolio
• Subjects: 631/154; 631/45; Animals; Antineoplastic drugs; Compound screening; Cyclin M (CNNM); Drug development; Drug interaction; Drug metabolism; Drug screening; Energy transfer; Fluorescence resonance energy transfer; Fluorescence Resonance Energy Transfer - methods; HEK293 Cells; High-throughput screening; High-Throughput Screening Assays - methods; Homogenous time-resolved fluorescence resonance energy transfer (HTR-FRET; HTRF; Humanities and Social Sciences; Humans; Magnesium; Magnesium - metabolism; Membrane proteins; multidisciplinary; Neoplasm Proteins - antagonists & inhibitors; Neoplasm Proteins - metabolism; Pharmacokinetics; Phosphatase of regenerating liver (PRL); Protein Binding; Protein interaction; Protein Tyrosine Phosphatases - antagonists & inhibitors; Protein Tyrosine Phosphatases - metabolism; Protein-protein interaction (PPI); Proteins; Science; Science (multidisciplinary); Protein-protein interaction (PPI); Homogenous time-resolved fluorescence resonance energy transfer (HTR-FRET; Compound screening; HTRF; Cyclin M (CNNM); Phosphatase of regenerating liver (PRL)

Phosphatase of regenerating liver (PRL) is an oncogenic protein that promotes tumor progression by directly binding to cyclin M (CNNM) membrane proteins and inhibiting their Mg 2+ efflux activity. In this study, we have developed a high-throughput screening system to detect the interactions between...