The TRP superfamily of channels (nomenclature as agreed by NC-IUPHAR [67,397]), whose founder member is the Drosophila Trp channel, exists in mammals as six families; TRPC, TRPM, TRPV, TRPA, TRPP and TRPML based on amino acid homologies. TRP subunits contain six putative TM domains and assemble as homo- or hetero-tetramers to form cation selective channels with diverse modes of activation and varied permeation properties (reviewed by [270]). Established, or potential, physiological functions of the individual members of the TRP families are discussed in detail in the recommended reviews and in a number of books [91,146,252,433]. The established, or potential, involvement of TRP channels in disease [421] is reviewed in [167,251], [254] and [173], together with a special edition of Biochemica et Biophysica Acta on the subject [251]. Additional disease related reviews, for pain [234], stroke [423], sensation and inflammation [363], itch [53], and airway disease [109,391], are available. The pharmacology of most TRP channels has been advanced in recent years. Broad spectrum agents are listed in the tables along with more selective, or recently recognised, ligands that are flagged by the inclusion of a primary reference. See Rubaiy (2019) for a review of pharmacological tools for TRPC1/C4/C5 channels [300]. Most TRP channels are regulated by phosphoinostides such as PtIns(4,5)P₂ although the effects reported are often complex, occasionally contradictory, and likely to be dependent upon experimental conditions, such as intracellular ATP levels (reviewed by [255,299,369]). Such regulation is generally not included in the tables.When thermosensitivity is mentioned, it refers specifically to a high Q10 of gating, often in the range of 10-30, but does not necessarily imply that the channel's function is to act as a 'hot' or 'cold' sensor. In general, the search for TRP activators has led to many claims for temperature sensing, mechanosensation, and lipid sensing. All proteins are of course sensitive to energies of binding, mechanical force, and temperature, but the issue is whether the proposed input is within a physiologically relevant range resulting in a response.

TRPA (ankyrin) family

TRPA1 is the sole mammalian member of this group (reviewed by [104]). TRPA1 activation of sensory neurons contribute to nociception [152,223,331]. Pungent chemicals such as mustard oil (AITC), allicin, and cinnamaldehyde activate TRPA1 by modification of free thiol groups of cysteine side chains, especially those located in its amino terminus [28,134,213,215]. Alkenals with α, β-unsaturated bonds, such as propenal (acrolein), butenal (crotylaldehyde), and 2-pentenal can react with free thiols via Michael addition and can activate TRPA1. However, potency appears to weaken as carbon chain length increases [13,28]. Covalent modification leads to sustained activation of TRPA1. Chemicals including carvacrol, menthol, and local anesthetics reversibly activate TRPA1 by non-covalent binding [157,190,401-402]. TRPA1 is not mechanosensitive under physiological conditions, but can be activated by cold temperatures [76,158]. The electron cryo-EM structure of TRPA1 [276] indicates that it is a 6-TM homotetramer. Each subunit of the channel contains two short ‘pore helices’ pointing into the ion selectivity filter, which is big enough to allow permeation of partially hydrated Ca²⁺ ions.

TRPC (canonical) family

Members of the TRPC subfamily (reviewed by [2,8,35,41,101,165,275,287]) fall into the subgroups outlined below. TRPC2 is a pseudogene in humans. It is generally accepted that all TRPC channels are activated downstream of G_q/11-coupled receptors, or receptor tyrosine kinases (reviewed by [283,354,397]). A comprehensive listing of G-protein coupled receptors that activate TRPC channels is given in [2]. Hetero-oligomeric complexes of TRPC channels and their association with proteins to form signalling complexes are detailed in [8] and [166]. TRPC channels have frequently been proposed to act as store-operated channels (SOCs) (or compenents of mulimeric complexes that form SOCs), activated by depletion of intracellular calcium stores (reviewed by [8,31,61-62,269,277,285,308,420]). However, the weight of the evidence is that they are not directly gated by conventional store-operated mechanisms, as established for Stim-gated Orai channels. TRPC channels are not mechanically gated in physiologically relevant ranges of force. All members of the TRPC family are blocked by 2-APB and SKF96365 [127-128]. Activation of TRPC channels by lipids is discussed by [35]. Important progress has been recently made in TRPC pharmacology [44,70,103,162,231,300,317]. TRPC channels regulate a variety of physiological functions and are implicated in many human diseases [36,45,59,105,149,208,329,339,380,384].

TRPC1/C4/C5 subgroup
TRPC1 alone may not form a functional ion channel [83]. TRPC4/C5 may be distinguished from other TRP channels by their potentiation by micromolar concentrations of La³⁺. TRPC2 is a pseudogene in humans, but in other mammals appears to be an ion channel localized to microvilli of the vomeronasal organ. It is required for normal sexual behavior in response to pheromones in mice. It may also function in the main olfactory epithelia in mice [200,267-268,412,414-415,440].

TRPC3/C6/C7 subgroup
All members are activated by diacylglycerol independent of protein kinase C stimulation [128].

TRPM (melastatin) family

Members of the TRPM subfamily (reviewed by [98,127,277,429]) fall into the five subgroups outlined below.

TRPM1/M3 subgroup
In darkness, glutamate released by the photoreceptors and ON-bipolar cells binds to the metabotropic glutamate receptor 6 , leading to activation of Go . This results in the closure of TRPM1. When the photoreceptors are stimulated by light, glutamate release is reduced, and TRPM1 channels are more active, resulting in cell membrane depolarization. Human TRPM1 mutations are associated with congenital stationary night blindness (CSNB), whose patients lack rod function. TRPM1 is also found melanocytes. Isoforms of TRPM1 may present in melanocytes, melanoma, brain, and retina. In melanoma cells, TRPM1 is prevalent in highly dynamic intracellular vesicular structures [145,262]. TRPM3 (reviewed by [265]) exists as multiple splice variants which differ significantly in their biophysical properties. TRPM3 is expressed in somatosensory neurons and may be important in development of heat hyperalgesia during inflammation (see review [349]). TRPM3 is frequently coexpressed with TRPA1 and TRPV1 in these neurons. TRPM3 is expressed in pancreatic beta cells as well as brain, pituitary gland, eye, kidney, and adipose tissue [264,348]. TRPM3 may contribute to the detection of noxious heat [374].

TRPM2
TRPM2 is activated under conditions of oxidative stress (respiratory burst of phagocytic cells). The direct activators are calcium, adenosine diphosphate ribose (ADPR) [357] and cyclic ADPR (cADPR) [418]. As for many ion channels, PI(4,5)P2 must also be present [412]. Numerous splice variants of TRPM2 exist which differ in their activation mechanisms [88]. Recent studies have reported structures of human (hs) TRPM2, which demonstrate two ADPR binding sites in hsTRPM2, one in the N-terminal MHR1/2 domain and the other in the C-terminal NUDT9-H domain. In addition, one Ca²⁺ binding site in the intracellular S2-S3 loop is revealed and proposed to mediate Ca²⁺ binding that induces conformational changes leading the ADPR-bound closed channel to open [141,382]. Meanwhile, a quadruple-residue motif (979FGQI982) was identified as the ion selectivity filter and a gate to control ion permeation in hsTRPM2 [419]. TRPM2 is involved in warmth sensation [315], and contributes to several diseases [38]. TRPM2 interacts with extra synaptic NMDA receptors (NMDAR) and enhances NMDAR activity in ischemic stroke [438]. Activation of TRPM2 in macrophages promotes atherosclerosis [428,439]. Moreover, silica nanoparticles induce lung inflammation in mice via ROS/PARP/TRPM2 signaling-mediated lysosome impairment and autophagy dysfunction [383]. Recent studies have designed various compounds for their potential to selectively inhibit the TRPM2 channel, including ACA derivatives A23, and 2,3-dihydroquinazolin-4(1H)-one derivatives [425,427].

TRPM4/5 subgroup
TRPM4 and TRPM5 have the distinction within all TRP channels of being impermeable to Ca²⁺ [397]. A splice variant of TRPM4 (i.e.TRPM4b) and TRPM5 are molecular candidates for endogenous calcium-activated cation (CAN) channels [116]. TRPM4 is active in the late phase of repolarization of the cardiac ventricular action potential. TRPM4 deletion or knockout enhances beta adrenergic-mediated inotropy [221]. Mutations are associated with conduction defects [147,221,327]. TRPM4 has been shown to be an important regulator of Ca²⁺ entry in to mast cells [364] and dendritic cell migration [27]. TRPM5 in taste receptor cells of the tongue appears essential for the transduction of sweet, amino acid and bitter stimuli [199] TRPM5 contributes to the slow afterdepolarization of layer 5 neurons in mouse prefrontal cortex [192]. Both TRPM4 and TRPM5 are required transduction of taste stimuli [89].

TRPM6/7 subgroup
TRPM6 and 7 combine channel and enzymatic activities (‘chanzymes’) [66]. These channels have the unusual property of permeation by divalent (Ca²⁺, Mg²⁺, Zn²⁺) and monovalent cations, high single channel conductances, but overall extremely small inward conductance when expressed to the plasma membrane. They are inhibited by internal Mg²⁺ at ~0.6 mM, around the free level of Mg²⁺ in cells. Whether they contribute to Mg²⁺ homeostasis is a contentious issue. PIP2 is required for TRPM6 and TRPM7 activation [304,399]. When either gene is deleted in mice, the result is embryonic lethality [151,396]. The C-terminal kinase region of TRPM6 and TRPM7 is cleaved under unknown stimuli, and the kinase phosphorylates nuclear histones [182-183]. TRPM7 is responsible for oxidant- induced Zn²⁺ release from intracellular vesicles [1] and contributes to intestinal mineral absorption essential for postnatal survival [232]. The putative metal transporter proteins CNNM1-4 interact with TRPM7 and regulate TRPM7 channel activity [22,176].

TRPM8
Is a channel activated by cooling and pharmacological agents evoking a ‘cool’ sensation and participates in the thermosensation of cold temperatures [30,68,82] reviewed by [172,209,239,370]. Direct chemical agonists include menthol and icilin[406]. Besides, linalool can promote ERK phosphorylation in human dermal microvascular endothelial cells, down-regulate intracellular ATP levels, and activate TRPM8 [33]. Recent studies have found that TRPM8 has typical S4-S5 connectomes with clear selective filters and exowell rings [191], and have identified cryo-electron microscopy structures of mouse TRPM8 in closed, intermediate, and open states along the ligand- and PIP₂-dependent gated pathways [413]. Moreover, the last 36 amino acids at the carboxyl terminal of TRPM8 are key protein sequences for TRPM8's temperature-sensitive function [71]. TRPM8 deficiency reduced the expression of S100A9 and increased the expression of HNF4α in the liver of mice, which reduced inflammation and fibrosis progression in mice with liver fibrosis, and helped to alleviate the symptoms of bile duct disease [206]. Channel deficiency also shortens the time of hypersensitivity reactions in migraine mouse models by promoting the recovery of normal sensitivity [7]. A cyclic peptide DeC‐1.2 was designed to inhibit ligand activation of TRPM8 but not cold activation, which can eliminate the side effects of cold dysalgesia in oxaliplatin-treated mice without changing body temperature [5]. Analysis of clinical data shows that TRPM8-specific blockers WS12 can reduce tumor growth in colorectal cancer xenografted mice by reducing transcription and activation of Wnt signaling regulators and β-catenin and its target oncogenes, such as C-Myc and Cyclin D1 [272].

TRPML (mucolipin) family

The TRPML family [69,286,289,405,422] consists of three mammalian members (TRPML1-3). TRPML channels are probably restricted to intracellular vesicles and mutations in the gene (MCOLN1) encoding TRPML1 (mucolipin-1) cause the neurodegenerative disorder mucolipidosis type IV (MLIV) in man. TRPML1 is a cation selective ion channel that is important for sorting/transport of endosomes in the late endocytotic pathway and specifically, fission from late endosome-lysosome hybrid vesicles and lysosomal exocytosis [309]. TRPML2 and TRPML3 show increased channel activity in low luminal sodium and/or increased luminal pH, and are activated by similar small molecules [56,112,326]. A naturally occurring gain of function mutation in TRPML3 (i.e. A419P) results in the varitint waddler (Va) mouse phenotype (reviewed by [256,289]).

TRPP (polycystin) family

The TRPP family (reviewed by [77,79,107,136,394]) or PKD2 family is comprised of PKD2 (PC2), PKD2L1 (PC2L1), PKD2L2 (PC2L2), which have been renamed TRPP1, TRPP2 and TRPP3, respectively [397]. It should also be noted that the nomenclature of PC2 was TRPP2 in old literature. However, PC2 has been uniformed to be called TRPP2 [126]. PKD2 family channels are clearly distinct from the PKD1 family, whose function is unknown. PKD1 and PKD2 form a hetero-oligomeric complex with a 1:3 ratio. [336]. Although still being sorted out, TRPP family members appear to be 6TM spanning nonselective cation channels.

TRPV (vanilloid) family

Members of the TRPV family (reviewed by [365]) can broadly be divided into the non-selective cation channels, TRPV1-4 and the more calcium selective channels TRPV5 and TRPV6.

TRPV1-V4 subfamily
TRPV1 is involved in the development of thermal hyperalgesia following inflammation and may contribute to the detection of noxius heat (reviewed by [282,328,343]). Numerous splice variants of TRPV1 have been described, some of which modulate the activity of TRPV1, or act in a dominant negative manner when co-expressed with TRPV1 [314]. The pharmacology of TRPV1 channels is discussed in detail in [118] and [372]. TRPV2 is probably not a thermosensor in man [273], but has recently been implicated in innate immunity [203]. Functional TRPV2 expression is described in placental trophoblast cells of mouse [73]. TRPV3 and TRPV4 are both thermosensitive. There are claims that TRPV4 is also mechanosensitive, but this has not been established to be within a physiological range in a native environment [52,196].

TRPV5/V6 subfamily
TRPV5 and TRPV6 are highly expressed in placenta, bone, and kidney. Under physiological conditions, TRPV5 and TRPV6 are calcium selective channels involved in the absorption and reabsorption of calcium across intestinal and kidney tubule epithelia (reviewed by [74,96,240,393]).TRPV6 is reported to play a key role in calcium transport in the mouse placenta [392].

TRPA (ankyrin) family

Agents activating TRPA1 in a covalent manner are thiol reactive electrophiles that bind to cysteine and lysine residues within the cytoplasmic domain of the channel [134,212]. TRPA1 is activated by a wide range of endogenous and exogenous compounds and only a few representative examples are mentioned in the table: an exhaustive listing can be found in [26]. In addition, TRPA1 is potently activated by intracellular zinc (EC₅₀ = 8 nM) [11,139]. A gain-of-function mutation in TRPA1 was found to cause familial episodic pain syndrome [184].

TRPM (melastatin) family

Ca²⁺ activates all splice variants of TRPM2, but other activators listed are effective only at the full length isoform [88]. Inhibition of TRPM2 by clotrimazole, miconazole, econazole, flufenamic acid is largely irreversible. Co-application of pregnenolone sulphate and clotrimazole caused TRPM3 currents to acquire an inwardly rectifying component at negative voltages, resulting in a biphasic conductance-voltage relationship. Evidence was presented that the inward current might reflect the permeation of cations through the opening of a non-canonical pore [373]. TRPM3 activity is impaired in chronic fatigue syndrome/myalgic encephalomyelitis patients suggesting changes in intracellular Ca²⁺ concentration, which may impact natural killer cellular functions [51]. TRPM4 exists as multiple spice variants: data listed are for TRPM4b. The sensitivity of TRPM4b and TRPM5 to activation by [Ca²⁺]_i demonstrates a pronounced and time-dependent reduction following excision of inside-out membrane patches [357]. The V_½ for activation of TRPM4 and TRPM5 demonstrates a pronounced negative shift with increasing temperature. Activation of TRPM8 by depolarization is strongly temperature-dependent via a channel-closing rate that decreases with decreasing temperature. The V_½ is shifted in the hyperpolarizing direction both by decreasing temperature and by exogenous agonists, such as (-)-menthol [368] whereas antagonists produce depolarizing shifts in V_½ [238]. The V_½ for the native channel is far more positive than that of heterologously expressed TRPM8 [238]. It should be noted that (-)-menthol and structurally related compounds can elicit release of Ca²⁺ from the endoplasmic reticulum independent of activation of TRPM8 [216]. Intracellular pH modulates activation of TRPM8 by cold and icilin, but not (-)-menthol [9].

TRPML (mucolipin) family

Data in the table are for TRPML proteins mutated (i.e TRPML1^Va, TRPML2^Va and TRPML3^Va) at loci equivalent to TRPML3 A419P to allow plasma membrane expression when expressed in HEK-293 cells and subsequent characterisation by patch-clamp recording [86,111,163,243,403]. Data for wild type TRPML3 are also tabulated [163-164,243,403]. It should be noted that alternative methodologies, particularly in the case of TRPML1, have resulted in channels with differing biophysical characteristics (reviewed by [286]). Initial functional characteristics of TRPML channels are performed on their Va mutations of TRPMLs at loci equivalent to TRPML3 A419P. Current pharmacological characterization of channel activators and blockers are conducted on wild-type channel proteins using endolysosomal patch-clamp [57,87,284,318].

TRPP (polycystin) family

Data in the table are extracted from [72,79] and [320]. Broadly similar single channel conductance, mono- and di-valent cation selectivity and sensitivity to blockers are observed for TRPP2 co-expressed with TRPP1 [78]. Ca²⁺, Ba²⁺ and Sr²⁺ permeate TRPP3, but reduce inward currents carried by Na⁺. Mg²⁺ is largely impermeant and exerts a voltage dependent inhibition that increases with hyperpolarization.

TRPV (vanilloid) family

Activation of TRPV1 by depolarisation is strongly temperature-dependent via a channel opening rate that increases with increasing temperature. The V_½ is shifted in the hyperpolarizing direction both by increasing temperature and by exogenous agonists [368]. TRPV3 channel dysfunction caused by genetic gain-of-function mutations is implicated in the pathogenesis of skin inflammation, dermatitis, and chronic itch. In rodents, a sponateous gain-of-function matation of the TRPV3 gene causes the development of skin lesions with pruritus and dermatitis [17,202]. In contrast to other thermoTRP channels, TRPV3 sensitizes rather than desensitizes, upon repeated stimulation with either heat or agonists [64,204,404]. The sensitivity of TRPV4 to heat, but not 4α-PDD is lost upon patch excision. TRPV4 is activated by anandamide and arachidonic acid following P450 epoxygenase-dependent metabolism to 5,6-epoxyeicosatrienoic acid (reviewed by [260]). Activation of TRPV4 by cell swelling, but not heat, or phorbol esters, is mediated via the formation of epoxyeicosatrieonic acids. Phorbol esters bind directly to TRPV4. Different TRPV4 mutations load to a broad spectrum of dominant skeletal dysplasias [181,298] and spinal muscular atrophies and hereditary motor and sensory neuropathies [19,81]. Similar mutations were also found in patients with Charcot-Marie-Tooth disease type 2C [187]. TRPV5 preferentially conducts Ca²⁺ under physiological conditions, but in the absence of extracellular Ca²⁺, conducts monovalent cations. Single channel conductances listed for TRPV5 and TRPV6 were determined in divalent cation-free extracellular solution. Ca²⁺-induced inactivation occurs at hyperpolarized potentials when Ca²⁺ is present extracellularly. Single channel events cannot be resolved (probably due to greatly reduced conductance) in the presence of extracellular divalent cations. Measurements of P_Ca/P_Na for TRPV5 and TRPV6 are dependent upon ionic conditions due to anomalous mole fraction behaviour. Blockade of TRPV5 and TRPV6 by extracellular Mg²⁺ is voltage-dependent. Intracellular Mg²⁺ also exerts a voltage dependent block that is alleviated by hyperpolarization and contributes to the time-dependent activation and deactivation of TRPV6 mediated monovalent cation currents. TRPV5 and TRPV6 differ in their kinetics of Ca²⁺-dependent inactivation and recovery from inactivation. TRPV5 and TRPV6 function as homo- and hetero-tetramers.

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Subcommittee members: Haoxing Xu (Chairperson) Qiushi Chair Professor, Liangzhu Laboratory & Zhejiang University Medical Center 1369 Wenyi West Rd Yuhang, Hangzhou China, 310000 Markus Delling UCSF School of Medicine 1550 4th Street Room 284E San Francisco, CA 94158 USA Kotdaji Ha UCSF School of Medicine 1550 4th Street Room 284E San Francisco, CA 94158 USA Jinbin Tian Department of Integrative Biology and Pharmacology McGovern Medical School The University of Texas Health Science Center at Houston Houston, TX 77030 USA Charlotte Van den Eynde Laboratory of Endometrium, Endometriosis & Reproductive Medicine Department Development & Regeneration KU Leuven G-PURE Leuven, Belgium Joris Vriens Laboratory of Endometrium, Endometriosis & Reproductive Medicine Department Development & Regeneration Katholieke Universiteit Leuven G-PURE Leuven, Belgium Lixia Yue University of Connecticut School of Medicine Farmington, CT USA Xiaoli Zhang Department of Molecular, Cellular and Developmental Biology University of Michigan 3089 Natural Science Building (Kraus) 830 North University Avenue Ann Arbor, MI 48109-1048 USA Michael X. Zhu Department of Integrative Biology and Pharmacology McGovern Medical School The University of Texas Health Science Center at Houston Houston, TX 77030 USA Christian M. Grimm, Prof. Walther-Straub-Institut für Pharmakologie und Toxikologie Medizinische Fakultät Ludwig-Maximilians-Universität (LMU) München Nussbaumstr. 26 (Raum A.062) 80336 München Germany

Other contributors: Ana I. Caceres Duke University School of Medicine Durham, NC 27710 United States Katrien De Clercq Katholieke Universiteit Leuven Leuven Flanders Belgium Meiqin Hu Liangzhu Laboratory & Zhejiang University 1369 Wenyi West Rd Yuhang, Hangzhou China, 310000 Sairam V. Jabba Duke University School of Medicine Durham, NC 27710 United States Sven E. Jordt Duke University School of Medicine Durham, NC 27710 United States Qiang Liu Liangzhu Laboratory & Zhejiang University 1369 Wenyi West Rd Yuhang, Hangzhou China, 310000 Fan Yang Liangzhu Laboratory & Zhejiang University 1369 Wenyi West Rd Yuhang, Hangzhou China, 310000 Wei Yang Liangzhu Laboratory & Zhejiang University 1369 Wenyi West Rd Yuhang, Hangzhou China, 310000