Transmembrane protein 150C (TMEM150C), also known as Tentonin 3 (TTN3), is a transmembrane protein encoded by the TMEM150C/TTN3 gene. TMEM150C/Tentonin 3 consists of 249 amino acids and is predicted to have six transmembrane domains. Mechanosensation, which is mediated by mechanotransduction channels, is a fundamental function required for the survival of vertebrates. The study found that TMEM150C/Tentonin 3 is a new class of mechanotransduction channel. Surprisingly, TMEM150C is expressed in muscle spindle afferents. Since genetic ablation of TMEM150C reduces motor coordination, TMEM150C appears to contribute to proprioception. Therefore, the cloning and expression of TMEM150C can be used to understand various other mechanotransduction mechanisms.
|Basic Information of TMEM150C|
|Protein Name||Transmembrane protein 150C|
|Organism||Homo sapiens (Human)|
The somatosensory ganglia of vertebrates contain various types of mechano-sensitive neurons and neuronal mechano-sensitivity relies on mechano-gated ion channels. Due to the presence of mechano-gated ion channels, these neurons can convert mechanical stimuli into ionic currents, including non-selective excitation channels such as Piezo2 and potassium selective inhibition channels such as TREK-1. Numerous studies have demonstrated that TMEM150C is proposed to mediate mechano-activated current in proprioceptive neurons. TMEM150C can interact with mechano-gated ion channels from different classes (Piezo2, Piezo1, and the potassium channel TREK-1). TMEM150C significantly prolongs the duration of the mechano-current produced by three channels (Piezo2, Piezo1, and the potassium channel TREK-1), reduces apparent activation threshold in Piezo2 and induces the persistent current in Piezo1. Therefore, the TMEM150C is a general regulator of mechano-gated ion channels from different classes. Moreover, TMEM150C is co-expressed with Piezo2 in trigeminal neurons, expanding its role beyond proprioceptors.
Fig.1 A putative topology of TMEM150C predicted by the TMHMM program. Each dot represents an amino acid in mouse TMEM150C. (Hong, 2016)
This article reveals that TMEM150C is a general regulator of mechano-gated ion channels from different classes.
This study supports that TTN3 is a pore-forming unit rather than an amplification aptamer for Piezo1 activity.
This article shows that TTN3/TMEM150C is a component of mechanically sensitive channels with a slow rate of inactivation and contributes to motor coordination.
This study demonstrates that the effect of the DRAM family member TMEM150B on the autophagy process is not related to its ability to regulate survival in glucose-starved cells.
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