| First Author | Hoshino N | Year | 2023 |
| Journal | Proc Natl Acad Sci U S A | Volume | 120 |
| Issue | 38 | Pages | e2301003120 |
| PubMed ID | 37695902 | Mgi Jnum | J:347059 |
| Mgi Id | MGI:7548918 | Doi | 10.1073/pnas.2301003120 |
| Citation | Hoshino N, et al. (2023) Visualization of trans homophilic interaction of clustered protocadherin in neurons. Proc Natl Acad Sci U S A 120(38):e2301003120 |
| abstractText | Clustered protocadherin (Pcdh) functions as a cell recognition molecule through the homophilic interaction in the central nervous system. However, its interactions have not yet been visualized in neurons. We previously reported PcdhgammaB2-Forster resonance energy transfer (FRET) probes to be applicable only to cell lines. Herein, we designed gammaB2-FRET probes by fusing FRET donor and acceptor fluorescent proteins to a single gammaB2 molecule and succeeded in visualizing gammaB2 homophilic interaction in cultured hippocampal neurons. The gammaB2-FRET probe localized in the soma and neurites, and FRET signals, which were observed at contact sites between neurites, eliminated by ethylene glycol tetraacetic acid (EGTA) addition. Live imaging revealed that the FRET-negative gammaB2 signals rapidly moved along neurites and soma, whereas the FRET-positive signals remained in place. We observed that the gammaB2 proteins at synapses rarely interact homophilically. The gammaB2-FRET probe might allow us to elucidate the function of the homophilic interaction and the cell recognition mechanism. |
