Date: 7 May 2026 (Thursday)
Time: 4:00 pm – 5:00 pm
Venue: Mrs Chen Yang Foo Oi Telemedicine Centre, 2/F, William MW Mong Block, 21 Sassoon Road, Pokfulam, Hong Kong
Host: Professor Michael Hӓusser

Uhtaek Oh is a leading neuroscientist specializing in ion channels and sensory mechanisms. Currently Principal Researcher at KIST's Brain Science Institute (Director 2017–2021), he was previously Professor at Seoul National University College of Pharmacy (1988–2016) and led key Korean scientific societies.

Dr. Oh earned his B.S. from Seoul National University, Ph.D. from University of Oklahoma, and trained at University of Texas. His discoveries include cloning Anoctamin/TMEM16A as a calcium-activated chloride channel essential for heat sensing, itch, and olfaction (Nature 2008, Nat Neurosci 2012), and Tentonin/TMEM150C for mechanosensation and insulin secretion (Neuron 2016–2017). Recent work covers conopeptide blockade (Brit J Pharmacol 2025).

Honors: Korea National Academy of Science Award (2006), Presidential Best Scientist Award (2010), Ho-Am Prize for Medicine (2019).

Numerous physiological functions including touch, hearing, blood pressure control, proprioception, and pain require mechanotransduction processes. Mechanosensitive (MS) channels in many mechanosensory cells mediate these transduction processes. Previously, we identified that Tentonin 3 (TTN3) elicits rapid activation followed by slowed inactivation MS currents, distinct from Piezo channels. TTN3 is known to mediate baroreceptor reflex, proprioception, and insulin-release from pancreatic beta cells. 

Protein stoichiometric analysis revealed that TTN3 is a tetramer. TTN3 is a pore-forming channel subunit as it shows spontaneous and stretch-evoked currents in the lipid bilayer. TTN3 structure was predicted using AlphaFold2 and other deep-learning protein structure prediction programs. The predicted TTN3 structure reveals a rectangular shape with a pore in the center. Four transmembrane a-helices (S1,2,5, and 6) face the lipid membrane, whereas, S3 and S4 of each subunit, comprise ion conducting pore. More importantly, a mutant of a conotoxin, NMB-1, once known as a blocker of the SA-type MS currents in dorsal-root ganglion neurons, inhibited TTN3, but not Piezo1. Therefore, we conclude that TTN3 is a bona-fide MS channel, not a regulator of Piezo1. 

Along with these biophysical properties, physiological functions of TTN3 and its homologs will be discussed.

All are welcome.