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- W4366088915 abstract "Clustered protocadherin (Pcdh) functions as a cell recognition molecule through the homophilic interaction in CNS. However, its interactions have yet not been visualized in neurons. We previously reported PcdhγB2-FRET probes to be applicable only for cell lines. Herein, we newly designed PcdhγB2-FRET probes by fusing FRET donor and acceptor fluorescent proteins to a single PcdhγB2 molecule and succeeded in visualizing PcdhγB2 homophilic interaction in cultured hippocampal neurons. The γB2-FRET probe localized in the soma and neurites, and FRET signals were observed at contact sites between neurites and eliminated by EGTA addition. Live imaging revealed that the FRET-negative γB2 signals were rapidly moving along neurites and soma, whereas the FRET-positive signals remained in place. We observed that the γB2 proteins at synapses rarely interact homophilically. The γB2-FRET probe would allow us to elucidate the function of the homophilic interaction and the cell recognition mechanism." @default.
- W4366088915 created "2023-04-19" @default.
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- W4366088915 date "2023-04-15" @default.
- W4366088915 modified "2023-10-16" @default.
- W4366088915 title "Visualization of<i>trans</i>homophilic interaction of clustered protocadherin in neurons" @default.
- W4366088915 doi "https://doi.org/10.1101/2023.04.14.536980" @default.
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