Editing Transient receptor potential channel (section)

{{Short description|Class of transport proteins}}
{{Infobox protein family
 | Symbol = TRP 
 | Name = Transient receptor potential (TRP) ion channel 
 | image = 
 | width = 
 | caption = 
 | Pfam= PF06011
 | InterPro= IPR013555
 | SMART= 
 | Prosite =          
 | SCOP =     
 | TCDB = 
 | OPM family= 8
 | OPM protein= 3j5p
 | PDB= 
 | Membranome superfamily = 605
}} 
'''Transient receptor potential channels''' ('''TRP channels''') are a group of [[ion channel]]s located mostly on the [[plasma membrane]] of numerous animal cell types. Most of these are grouped into two broad groups: Group 1 includes [[TRPC]] ( "C" for canonical), [[TRPV]] ("V" for [[vanilloid]]), [[TRPVL]] ("VL" for vanilloid-like), [[TRPM]] ("M" for melastatin), [[TRPS]] ("S" for soromelastatin), [[TRPN]] ("N" for mechanoreceptor potential C), and [[TRPA (channel)|TRPA]] ("A" for ankyrin). Group 2 consists of [[TRPP]] ("P" for polycystic) and [[TRPML]] ("ML" for mucolipin).<ref name = "Islam_2011">{{cite book | veditors = Islam MS | title = Transient Receptor Potential Channels |date=January 2011 | volume = 704 | publisher = Springer |  location = Berlin | pages = 700  | series = Advances in Experimental Medicine and Biology | isbn = 978-94-007-0264-6 }}</ref><ref name="TRP_review" /> Other less-well categorized TRP channels exist, including yeast channels and a number of Group 1 and Group 2 channels present in non-animals.<ref name="TRP_review" /><ref>{{cite journal | vauthors = Arias-Darraz L, Cabezas D, Colenso CK, Alegría-Arcos M, Bravo-Moraga F, Varas-Concha I, Almonacid DE, Madrid R, Brauchi S | display-authors = 6 | title = A transient receptor potential ion channel in Chlamydomonas shares key features with sensory transduction-associated TRP channels in mammals | journal = The Plant Cell | volume = 27 | issue = 1 | pages = 177–88 | date = January 2015 | pmid = 25595824 | pmc = 4330573 | doi = 10.1105/tpc.114.131862 | doi-access = free | bibcode = 2015PlanC..27..177A }}</ref><ref>{{cite journal | vauthors = Lindström JB, Pierce NT, Latz MI | title = Role of TRP Channels in Dinoflagellate Mechanotransduction | journal = The Biological Bulletin | volume = 233 | issue = 2 | pages = 151–167 | date = October 2017 | pmid = 29373067 | doi = 10.1086/695421 | s2cid = 3388001 }}</ref> Many of these channels mediate a variety of sensations such as pain, temperature, different kinds of taste, pressure, and vision. In the body, some TRP channels are thought to behave like microscopic thermometers and used in animals to sense hot or cold.<ref name="pmid25053448">
{{cite journal | vauthors = Vriens J, Nilius B, Voets T | title = Peripheral thermosensation in mammals | journal = Nature Reviews. Neuroscience | volume = 15 | issue = 9 | pages = 573–89 | date = September 2014 | pmid = 25053448 | doi = 10.1038/nrn3784 | s2cid = 27149948 | doi-access = free }}</ref> Some TRP channels are activated by molecules found in spices like garlic ([[allicin]]), chili pepper ([[capsaicin]]), wasabi ([[allyl isothiocyanate]]); others are activated by [[menthol]], [[camphor]], peppermint, and cooling agents; yet others are activated by molecules found in [[cannabis]] (i.e., [[THC]], [[cannabidiol|CBD]] and [[Cannabinol|CBN]]) or [[Stevia rebaudiana|stevia]]. Some act as sensors of osmotic pressure, volume, stretch, and vibration. Most of the channels are activated or inhibited by signaling lipids and contribute to a family of [[lipid-gated ion channels]].<ref>{{cite journal | vauthors = Robinson CV, Rohacs T, Hansen SB | title = Tools for Understanding Nanoscale Lipid Regulation of Ion Channels | journal = Trends in Biochemical Sciences | volume = 44 | issue = 9 | pages = 795–806 | date = September 2019 | pmid = 31060927 | pmc = 6729126 | doi = 10.1016/j.tibs.2019.04.001 }}</ref><ref>{{cite journal | vauthors = Hansen SB | title = Lipid agonism: The PIP2 paradigm of ligand-gated ion channels | journal = Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids | volume = 1851 | issue = 5 | pages = 620–8 | date = May 2015 | pmid = 25633344 | pmc = 4540326 | doi = 10.1016/j.bbalip.2015.01.011 }}</ref>

These [[ion channel]]s have a relatively non-selective permeability to [[cation]]s, including [[sodium]], [[calcium]] and [[magnesium]].

TRP channels were initially discovered in the so-called "transient receptor potential" mutant (''trp''-mutant) strain of the fruit fly ''[[Drosophila]]'', hence their name (see [[Transient receptor potential channel#History of Drosophila TRP channels|History of ''Drosophila'' TRP channels]] below). Later, TRP channels were found in vertebrates where they are ubiquitously expressed in many cell types and tissues. TRP channels are tetrameric, with each protomer composed of 6 [[Alpha helix#Membrane spanning|membrane-spanning helices]] with intracellular N- and [[C terminus|C-termini]]. Mammalian TRP channels are activated and regulated by a wide variety of stimuli and are expressed throughout the body.