Hirabayashi Lab - UTokyo

Thanks!!

19.04.2025 04:26 — 👍 1    🔁 0    💬 0    📌 0

早速ありがとうございます！

18.04.2025 11:43 — 👍 1    🔁 0    💬 0    📌 0

Using a tool we’ve been developing for analyzing volume EM data (dx.plos.org/10.1371/jour...), we discovered that PDZD8 promotes more complex mitochondrial structures by inhibiting FKBP8.

18.04.2025 11:42 — 👍 0    🔁 0    💬 1    📌 0

That protein? FKBP8. By combining immunoprecipitation and proximity labeling, we identified FKBP8 as a mitochondrial partner of PDZD8.

18.04.2025 11:36 — 👍 0    🔁 0    💬 1    📌 0

In collaboration with Christopher Obara (UCSD), single-particle tracking PALM showed that PDZD8 moves rapidly on the ER but slows down near mitochondria, suggesting it’s captured by a mitochondrial protein.

18.04.2025 11:34 — 👍 0    🔁 0    💬 1    📌 0

Mitochondrial complexity is regulated at ER-mitochondria contact sites via PDZD8-FKBP8 tethering Nature Communications - How PDZD8 acted in Mitochondria-ER contact formation was unclear. Here, the authors show that binding to mitochondrial FKBP8 slows PDZD8’s rapid motion, enhancing...

After 6 years of careful experiments, we’re excited to share our latest manuscript on the identification and function of the PDZD8–FKBP8 protein complex! We now have convincing evidence that structural regulation of mitochondria via ER–mitochondria tethering proteins is real.
rdcu.be/eihrF

18.04.2025 11:31 — 👍 4    🔁 1    💬 1    📌 0