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TRPM5 Membrane Protein Introduction

Introduction of TRPM5

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
Gene Name TRPM5
Aliases LTRPC5, MTR1
Organism Homo sapiens (Human)
UniProt ID Q9NZQ8
Transmembrane Times 6
Length (aa) 1165
Sequence MQDVQGPRPGSPGDAEDRRELGLHRGEVNFGGSGKKRGKFVRVPSGVAPSVLFDLLLAEWHLPAPNLVVSLVGEEQPFAMKSWLRDVLRKGLVKAAQSTGAWILTSALRVGLARHVGQAVRDHSLASTSTKVRVVAVGMASLGRVLHRRILEEAQEDFPVHYPEDDGGSQGPLCSLDSNLSHFILVEPGPPGKGDGLTELRLRLEKHISEQRAGYGGTGSIEIPVLCLLVNGDPNTLERISRAVEQAAPWLILVGSGGIADVLAALVNQPHLLVPKVAEKQFKEKFPSKHFSWEDIVRWTKLLQNITSHQHLLTVYDFEQEGSEELDTVILKALVKACKSHSQEPQDYLDELKLAVAWDRVDIAKSEIFNGDVEWKSCDLEEVMVDALVSNKPEFVRLFVDNGADVADFLTYGRLQELYRSVSRKSLLFDLLQRKQEEARLTLAGLGTQQAREPPAGPPAFSLHEVSRVLKDFLQDACRGFYQDGRPGDRRRAEKGPAKRPTGQKWLLDLNQKSENPWRDLFLWAVLQNRHEMATYFWAMGQEGVAAALAACKILKEMSHLETEAEAARATREAKYERLALDLFSECYSNSEARAFALLVRRNRCWSKTTCLHLATEADAKAFFAHDGVQAFLTRIWWGDMAAGTPILRLLGAFLCPALVYTNLITFSEEAPLRTGLEDLQDLDSLDTEKSPLYGLQSRVEELVEAPRAQGDRGPRAVFLLTRWRKFWGAPVTVFLGNVVMYFAFLFLFTYVLLVDFRPPPQGPSGPEVTLYFWVFTLVLEEIRQGFFTDEDTHLVKKFTLYVGDNWNKCDMVAIFLFIVGVTCRMLPSAFEAGRTVLAMDFMVFTLRLIHIFAIHKQLGPKIIVVERMMKDVFFFLFFLSVWLVAYGVTTQALLHPHDGRLEWIFRRVLYRPYLQIFGQIPLDEIDEARVNCSTHPLLLEDSPSCPSLYANWLVILLLVTFLLVTNVLLMNLLIAMFSYTFQVVQGNADMFWKFQRYNLIVEYHERPALAPPFILLSHLSLTLRRVFKKEAEHKREHLERDLPDPLDQKVVTWETVQKENFLSKMEKRRRDSEGEVLRKTAHRVDFIAKYLGGLREQEKRIKCLESQINYCSVLVSSVADVLAQGGGPRSSQHCGEGSQLVAADHRGGLDGWEQPGAGQPPSDT

Function of TRPM5 Membrane Protein

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.

Schematic overview of intracellular pathways in type II taste receptor cells and pancreatic β-cells. Fig.1 Schematic overview of intracellular pathways in type II taste receptor cells and pancreatic β-cells. (Philippaert, 2017)

Application of TRPM5 Membrane Protein in Literature

  1. Farashi S., et al. The role of the transient receptor potential melastatin5 (TRPM5) channels in the pancreatic β-cell electrical activity: A computational modeling study. Comput Biol Chem. 2018, 76:101-108. PubMed ID: 29982164

    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.

  2. Fu Z., et al. ATP and Odor Mixture Activate TRPM5-Expressing Microvillous Cells and Potentially Induce Acetylcholine Release to Enhance Supporting Cell Endocytosis in Mouse Main Olfactory Epithelium. Front Cell Neurosci. 2018, 12:71. PubMed ID: 29615870

    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.

  3. Dutta Banik D., et al. TRPM4 and TRPM5 are both required for normal signaling in taste receptor cells. Proc Natl Acad Sci U S A. 2018, 115(4):E772-E781. PubMed ID: 29311301

    This article demonstrates that in taste receptor cells both TRPM4 and TRPM5 are essential for normal transduction of taste stimuli.

  4. Qian J., et al. Nicotinic acetylcholine receptors (nAChRs) are expressed in Trpm5 positive taste receptor cells (TRCs). PLoS One. 2018, 13(1):e0190465. PubMed ID: 29293602

    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.

  5. Yoshida Y., et al. Expression levels of taste-related genes in palate and tongue tip, and involvement of transient receptor potential subfamily M member 5 (TRPM5) in taste sense in chickens. Anim Sci J. 2018, 89(2):441-447. PubMed ID: 29178505

    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.

TRPM5 Preparation Options

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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.

Reference

  1. Philippaert K, et al. (2017). Steviol glycosides enhance pancreatic beta-cell function and taste sensation by potentiation of TRPM5 channel activity. Nat Commun. 8:14733.

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