| Autor: |
Natsumi Hoshino, Takashi Kanadome, Tomomi Takasugi, Mizuho Itoh, Ryosuke Kaneko, Inoue, Yukiko U., Takayoshi Inoue, Takahiro Hirabayashi, Masahiko Watanabe, Tomoki Matsuda, Takeharu Nagai, Etsuko Tarusawa, Takeshi Yagi |
| Předmět: |
|
| Zdroj: |
Proceedings of the National Academy of Sciences of the United States of America; 9/19/2023, Vol. 120 Issue 38, p1-17, 29p |
| Abstrakt: |
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 Pcdh-B2-Förster resonance energy transfer (FRET) probes to be applicable only to cell lines. Herein, we -B2 designed-FRET probes by fusing FRET donor and acceptor fluorescent proteins to a single γB2 molecule and succeeded in visualizing γB2 homophilic interaction in cultured hippocampal neurons. The γB2-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 γB2 signals rapidly moved 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 might allow us to elucidate the function of the homophilic interaction and the cell recognition mechanism. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
|
