TRP channels

Stable Identifier
Homo sapiens
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Transient receptor potential (TRP) channel proteins were first discovered in Drosophila melanogaster and have many homologues in other species including humans. TRPs form cationic channels that can detect sensory stimuli such as temperature, pH or oxidative stress and transduce that into either electrical (change in membrane potential) or chemical signals (change in intracellular Ca2+ concentration). In humans, there are 28 TRP genes arranged into 6 subfamilies; TRPA, TRPC, TRPM, TRPML, TRPP, and TRPV (Wu et al. 2010). Each TRP channel subunit consists of six putative transmembrane-spanning segments (S1-S6) with a pore-forming loop between S5 and S6. These subunits assemble into tetramers to form functional channels. All functionally characterized TRP channels are permeable to Ca2+ except TRMP4 and 5 which are only permeable to monovalent cations such as Na+ (Latorre et al. 2009). Most TRPs can cause channelopathies which are risk factors for many disease states (Nilius & Owsianik 2010).
Literature References
PubMed ID Title Journal Year
20025796 Structure-functional intimacies of transient receptor potential channels

Zaelzer, C, Brauchi, S, Latorre, R

Q. Rev. Biophys. 2009
20347603 Transient receptor proteins illuminated: current views on TRPs and disease

Beck, A, Cheng, H, Nelson, PL

Vet. J. 2011
20716668 International Union of Basic and Clinical Pharmacology. LXXVI. Current progress in the mammalian TRP ion channel family

Clapham, DE, Wu, LJ, Sweet, TB

Pharmacol. Rev. 2010
20127491 Transient receptor potential channelopathies

Owsianik, G, Nilius, B

Pflugers Arch. 2010
Event Information
Orthologous Events
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