TRPM3, also known as MLSN2 and GON-2, belongs to transient receptor potential cation channel subfamily M. It is encoded by the TRPM3 gene, which is located at chromosome 9q21.13. TRPM3 is shown to be widely expressed in kidney, brain, ovary, and testis. In the nervous system, TRPM3 expression has been reported in both CNS and PNS, including DRG neurons and various nonneuronal tissues. The structure of TRPM3 is characterized by a homo-tetrameric channel with a distinct ~700 amino acid long TRPM-specific domain in the cytoplasmic N-terminus.
|Basic Information of TRPM3|
|Protein Name||Transient receptor potential cation channel subfamily M member 3|
|Aliases||GON-2, LTRPC3, MLSN2|
|Organism||Homo sapiens (Human)|
TRPM3 is a nonselective cation channel with relatively high Ca²⁺ permeability and has a strong outwardly rectifying current-voltage relationship, playing crucial roles in cellular calcium ion signaling and homeostasis. The TRPM3 protein can regulate calcium entry, and the activity of this channel will be enhanced under the condition of calcium store depletion. On the other hand, neurosteroid pregnenolone sulfate is reported to activate TRPM3 in the pancreatic beta cell. And the activation may result in calcium influx and subsequent release of insulin, therefore, it is suggested that TRPM3 plays a role in the regulation of glucose homeostasis. Additionally, TRPM3 is involved in multiple other biological processes, such as sensory perception of temperature stimulus, detection of temperature stimulus, etc.
Fig.1 Schematic representation of the molecular mechanisms of TRPM3 modulation. (Joris, 2018)
This article shows that TRPM3 cation channels are modulated by intracellular calcium ion and provides the basis for a mechanism of the calmodulin regulating TRPM3.
This article suggests that agonists of the Gi-coupled µ opioid, GABA-B and NPY receptors, can inhibit the activity of TRPM3 expressed in mouse dorsal root ganglion neurons.
This article demonstrates that TRPM3 is involved in the maximal osmotic response in renal epithelial cells and that the response requires the primary cilia and can be regulated by TRPV4 independent of cilia.
This article demonstrates that diclofenac inhibits human TRPM3 without interacting with the channel pore.
This article confirms that CIM0216 is less capable in activating TRPM3-mediated gene transcription, suggesting that pregnenolone sulfate is still the potent ligand of choice for affecting the gene expression pattern via TRPM3.
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