Mammalian TMC Family Proteins are Mechanically Gated Ion Channels
Fu, S.; Dong, J.; Luo, X.; Xie, T.; Li, W.; Luo, Y.; Yan, Z.
Show abstract
Every known life form senses and reacts to mechanical forces. These mechanical stimuli can be converted into electrical signals by mechanically gated ion channels, a transduction cascade pivotal to numerous physiological functions including touch, hearing, mechanical pain, circulation, gastrointestinal function, and mechanical loading in various tissues. Despite continuous efforts, numerous mechanically gated ion channels with the mechanotransduction process underlying these physiological functions remain unidentified. Here, we focused on the transmembrane channel-like (TMC) protein family expressed in the cultured cells to identify those with potential mechanosensitive activity. Remarkably, in contrast to human TMC1/2 (HsTMC1/2), human TMC3-8 (HsTMC3-8) proteins are localized to the plasma membrane when heterologously expressed in the cultured cells. Further experiments revealed that mechanical poking stimuli can effectively activate HsTMC3-8. In addition, HsTMC3-8 induced stretch-activated currents and elicited well-resolved single-channel activities in response to negative pressure stimulation. The mutants near the putative pore region altered reversal potentials (Erev) of HsTMC3-8, suggesting that TMC3-8 are likely pore-forming subunits of ion channels. In summary, we proposed that TMC proteins are the largest mammalian mechanically gated ion channel family.
Matching journals
The top 6 journals account for 50% of the predicted probability mass.
Similar papers in this journal
- Thermosensitivity of the voltage-dependent activation of calcium homeostasis modulator 1 (calhm1) ion channel 94%
- FRMPD2: a novel GluN2A-interacting scaffold protein in synaptic excitatory transmission 93%
- Topological analysis of TMEM180, a newly identified membrane protein that is highly expressed in colorectal cancer cells 92%
Similar papers in this journal
- Calcium-driven regulation of voltage-sensing domains in BK channels 93%
- Voltage-clamp fluorometry analysis of structural rearrangements of ATP-gated channel P2X2 upon hyperpolarization 92%
- Identification and classification of ion-channels across the tree of life: Insights into understudied CALHM channels 92%
Similar papers in this journal
Similar papers in this journal
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.