Transient receptor potential channel

Transient receptor potential (TRP) ion channel
Identifiers
SymbolTRP
PfamPF06011
InterProIPR013555
OPM superfamily8
OPM protein3j5p
Membranome605
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Transient receptor potential channels (TRP channels) are a group of ion channels 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 ("A" for ankyrin). Group 2 consists of TRPP ("P" for polycystic) and TRPML ("ML" for mucolipin).[1][2] Other less-well categorized TRP channels exist, including yeast channels and a number of Group 1 and Group 2 channels present in non-animals.[2][3][4] 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.[5] 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, CBD and CBN) or 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.[6][7]

These ion channels have a relatively non-selective permeability to cations, 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 History of Drosophila TRP channels below). Later, TRP channels were found in vertebrates where they are ubiquitously expressed in many cell types and tissues. Most TRP channels are composed of 6 membrane-spanning helices with intracellular N- and C-termini. Mammalian TRP channels are activated and regulated by a wide variety of stimuli and are expressed throughout the body.

  1. ^ Islam MS, ed. (January 2011). Transient Receptor Potential Channels. Advances in Experimental Medicine and Biology. Vol. 704. Berlin: Springer. p. 700. ISBN 978-94-007-0264-6.
  2. ^ a b Cite error: The named reference TRP_review was invoked but never defined (see the help page).
  3. ^ Arias-Darraz L, Cabezas D, Colenso CK, Alegría-Arcos M, Bravo-Moraga F, Varas-Concha I, et al. (January 2015). "A transient receptor potential ion channel in Chlamydomonas shares key features with sensory transduction-associated TRP channels in mammals". The Plant Cell. 27 (1): 177–88. doi:10.1105/tpc.114.131862. PMC 4330573. PMID 25595824.
  4. ^ Lindström JB, Pierce NT, Latz MI (October 2017). "Role of TRP Channels in Dinoflagellate Mechanotransduction". The Biological Bulletin. 233 (2): 151–167. doi:10.1086/695421. PMID 29373067. S2CID 3388001.
  5. ^ Vriens J, Nilius B, Voets T (September 2014). "Peripheral thermosensation in mammals". Nature Reviews. Neuroscience. 15 (9): 573–89. doi:10.1038/nrn3784. PMID 25053448. S2CID 27149948.
  6. ^ Robinson CV, Rohacs T, Hansen SB (September 2019). "Tools for Understanding Nanoscale Lipid Regulation of Ion Channels". Trends in Biochemical Sciences. 44 (9): 795–806. doi:10.1016/j.tibs.2019.04.001. PMC 6729126. PMID 31060927.
  7. ^ Hansen SB (May 2015). "Lipid agonism: The PIP2 paradigm of ligand-gated ion channels". Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 1851 (5): 620–8. doi:10.1016/j.bbalip.2015.01.011. PMC 4540326. PMID 25633344.