Transient receptor potential cation channel subfamily M member 5 (TRPM5), also known as long transient receptor potential channel 5 (LTRPC5) or MTR1, is a protein that in humans is encoded by the TRPM5 gene. Similar to the majority of TRPM channels, TRPM5 also includes 6 transmembrane segments (a pore region between segments 5 and 6), and an intracellular N and C termini. The C-terminal domain contains a TRP motif and a zinc finger domain containing alpha-kinase domain. TRPM5 has a biased expression in the duodenum, small intestine, colon, pancreas, and testis.
|Basic Information of TRPM5|
|Protein Name||Transient receptor potential cation channel subfamily M member 5|
|Organism||Homo sapiens (Human)|
TRPM5 is a monovalent-specific, nonselective cation channel that carries Na⁺, K⁺, and Cs⁺ ions equally well, but not Ca²⁺ ions. But TRPM5 may couple intracellular Ca²⁺ release to electrical activity and subsequent cellular responses. Its channel activity is activated by a concentration rise of the intracellular calcium, and consequently, monovalent cations, such as K⁺ and Na⁺, permeate through the membrane, leading to depolarization of the membrane. In the gustatory system, TRPM5 plays a crucial role in taste transduction, including bitter, sweet and umami tastes. Besides, TRPM5 has also been considered as a likely contributor to fat taste signaling. TRPM5 is presented in pancreatic beta-cells where it is an indispensable regulator of insulin secretion. The enhanced expression of TRPM5 in the pancreatic beta-cells results in increased secretion of insulin and shows improvement of mice with type II diabetes.
Fig.1 Schematic overview of intracellular pathways in type II taste receptor cells and pancreatic β-cells. (Philippaert, 2017)
This article shows that TRPM5 can speed up membrane depolarization to influence other ion channel activities and increase the firing rate and amplitude of action potentials by possibly affecting the γ-Aminobutyric acid and Na⁺ related currents.
This article suggests that TRPM5-MCs may regulate the multicellular network activity of the main olfactory epithelium via cholinergic paracrine signaling for functional maintenance and adaptive plasticity.
This article demonstrates that in taste receptor cells both TRPM4 and TRPM5 are essential for normal transduction of taste stimuli.
This article concludes that nicotinic acetylcholine receptors subunits are presented in Trpm5-positive taste receptor cells and their expression levels are differentially affected by chronic oral exposure to ethanol and nicotine.
This article demonstrates that TRPM5 plays a role in chickens' taste transduction and that an inhibitor of TRPM5 can reduce chickens' bitter taste perception of feed ingredients.
In order to provide high-quality membrane protein preparation service, we have developed a versatile Magic™ membrane protein production platform. Our experienced scientists will do their best to help you find a perfect match in your required formats. Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-TRPM5 antibody development services.
As a leading service provider, Creative Biolabs is proud to present our professional service in membrane protein preparation using a variety of strategies. We combine our advanced proteomic technologies and our long-term scientific expertise in the fields of membrane biochemistry to produce, purify, stabilize and characterize many challenging membrane protein targets for global customers. If you are interested in the service we can provide, please feel free to contact us for more information.