Unlocking the therapeutic potential of TRPV3: Insights into thermosensation, channel modulation, and skin homeostasis involving TRPV3.
TRPV3
temperature
Journal
BioEssays : news and reviews in molecular, cellular and developmental biology
ISSN: 1521-1878
Titre abrégé: Bioessays
Pays: United States
ID NLM: 8510851
Informations de publication
Date de publication:
20 May 2024
20 May 2024
Historique:
revised:
02
05
2024
received:
29
02
2024
accepted:
06
05
2024
medline:
21
5
2024
pubmed:
21
5
2024
entrez:
21
5
2024
Statut:
aheadofprint
Résumé
Recent insights reveal the significant role of TRPV3 in warmth sensation. A novel finding elucidated how thermosensation is affected by TRPV3 membrane abundance that is modulated by the transmembrane protein TMEM79. TRPV3 is a warmth-sensitive ion channel predominantly expressed in epithelial cells, particularly skin keratinocytes. Multiple studies investigated the roles of TRPV3 in cutaneous physiology and pathophysiology. TRPV3 activation by innocuous warm temperatures in keratinocytes highlights its significance in temperature sensation, but whether TRPV3 directly contributes to warmth sensations in vivo remains controversial. This review explores the electrophysiological and structural properties of TRPV3 and how modulators affect its intricate regulatory mechanisms. Moreover, we discuss the multifaceted involvement of TRPV3 in skin physiology and pathology, including barrier formation, hair growth, inflammation, and itching. Finally, we examine the potential of TRPV3 as a therapeutic target for skin diseases and highlight its diverse role in maintaining skin homeostasis.
Identifiants
pubmed: 38769699
doi: 10.1002/bies.202400047
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2400047Subventions
Organisme : Japan Society for the Promotion of Science
ID : 21H02667
Organisme : Japan Society for the Promotion of Science
ID : 23H04943
Informations de copyright
© 2024 The Authors. BioEssays published by Wiley Periodicals LLC.
Références
Peier, A. M., Reeve, A. J., Andersson, D. A., Moqrich, A., Earley, T. J., Hergarden, A. C., Story, G. M., Colley, S., Hogenesch, J. B., Mcintyre, P., Bevan, S., & Patapoutian, A. (2002). A heat‐sensitive TRP channel expressed in keratinocytes. Science, 296, 2046–2049. https://doi.org/10.1126/science.1073140
Smith, G. D., Gunthorpe, M. J., Kelsell, R. E., Hayes, P. D., Reilly, P., Facer, P., Wright, J. E., Jerman, J. C., Walhin, J.‐P., Ooi, L., Egerton, J., Charles, K. J., Smart, D., Randall, A. D., Anand, P., & Davis, J. B. (2002). TRPV3 is a temperature‐sensitive vanilloid receptor‐like protein. Nature, 418, 186–190. https://doi.org/10.1038/nature00894
Xu, H., Ramsey, I. S, Kotecha, S. A., Moran, M. M., Chong, J. A., Lawson, D., Ge, P., Lilly, J., Silos‐Santiago, I., Xie, Y., Distefano, P. S., Curtis, R., & Clapham, D. E. (2002). TRPV3 is a calcium‐permeable temperature‐sensitive cation channel. Nature, 418, 181–186. https://doi.org/10.1038/nature00882
Liedtke, W., Choe, Y., Martí‐Renom, M. A., Bell, A. M., Denis, C. S., Andrejšali, Hudspeth, A. J., Friedman, J. M., & Heller, S. (2000). Vanilloid receptor–related osmotically activated channel (VR‐OAC), a candidate vertebrate osmoreceptor. Cell, 103, 525–535. https://doi.org/10.1016/S0092‐8674(00)00143‐4
Lei, J., Yoshimoto, R. U., Matsui, T., Amagai, M., Kido, M. A., & Tominaga, M. (2023). Involvement of skin TRPV3 in temperature detection regulated by TMEM79 in mice. Nature Communications, 14, 4104. https://doi.org/10.1038/s41467‐023‐39712‐x
Borbíró, I., Lisztes, E., Tóth, B. I., Czifra, G., Oláh, A., Szöllősi, A. G., Szentandrássy, N., Nánási, P. P., Péter, Z., Paus, R., Kovács, L., & Bíró, T. (2011). Activation of transient receptor potential vanilloid‐3 inhibits human hair growth. Journal of Investigative Dermatology, 131, 1605–1614. https://doi.org/10.1038/jid.2011.122
Mergler, S., Garreis, F., Sahlmüller, M., Reinach, P. S., Paulsen, F., & Pleyer, U. (2011). Thermosensitive transient receptor potential channels (thermo‐TRPs) in human corneal epithelial cells. Journal of Cellular Physiology, 226, 1828–1842. https://doi.org/10.1002/jcp.22514
Ueda, T., Yamada, T., Ugawa, S., Ishida, Y., & Shimada, S. (2009). TRPV3, a thermosensitive channel is expressed in mouse distal colon epithelium. Biochemical and Biophysical Research Communications, 383, 130–134. https://doi.org/10.1016/j.bbrc.2009.03.143
Aijima, R., Wang, B., Takao, T., Mihara, H., Kashio, M., Ohsaki, Y., Zhang, J.‐Q., Mizuno, A., Suzuki, M., Yamashita, Y., Masuko, S., Goto, M., Tominaga, M., & Kido, M. A. (2015). The thermosensitive TRPV3 channel contributes to rapid wound healing in oral epithelia. The FASEB Journal, 29, 182–192. https://doi.org/10.1096/fj.14‐251314
Xu, H., Delling, M., Jun, J. C., & Clapham, D. E. (2006). Oregano, thyme and clove‐derived flavors and skin sensitizers activate specific TRP channels. Nature Neuroscience, 9, 628–635. https://doi.org/10.1038/nn1692
Facer, P., Casula, M. A., Smith, G. D., Benham, C. D., Chessell, I. P., Bountra, C., Sinisi, M., Birch, R., & Anand, P. (2007). Differential expression of the capsaicin receptor TRPV1 and related novel receptors TRPV3, TRPV4 and TRPM8 in normal human tissues and changes in traumatic and diabetic neuropathy. BMC Neurology, 7, 11. https://doi.org/10.1186/1471‐2377‐7‐11
Inada, H., Iida, T., & Tominaga, M. (2006). Different expression patterns of TRP genes in murine B and T lymphocytes. Biochemical and Biophysical Research Communications, 350, 762–767. https://doi.org/10.1016/j.bbrc.2006.09.111
Gees, M., Colsoul, B., & Nilius, B. (2010). The role of transient receptor potential cation channels in Ca2+ signaling. Cold Spring Harbor Perspectives in Biology, 2, a003962. https://doi.org/10.1101/cshperspect.a003962
Xiao, R., Tang, J., Wang, C., Colton, C. K., Tian, J., & Zhu, M. X. (2008). Calcium plays a central role in the sensitization of TRPV3 channel to repetitive stimulations *. Journal of Biological Chemistry, 283, 6162–6174. https://doi.org/10.1074/jbc.M706535200
Liu, Q., Wang, J., Wei, X., Hu, J., Ping, C., Gao, Y., Xie, C., Wang, P., Cao, P., Cao, Z., Yu, Y., Li, D., & Yao, J. (2021). Therapeutic inhibition of keratinocyte TRPV3 sensory channel by local anesthetic dyclonine. eLife, 10, e68128. https://doi.org/10.7554/eLife.68128
Neuberger, A., Nadezhdin, K. D., Zakharian, E., & Sobolevsky, A. I. (2021). Structural mechanism of TRPV3 channel inhibition by the plant‐derived coumarin osthole. EMBO Reports, 22, e53233. https://doi.org/10.15252/embr.202153233
Qi, H., Shi, Y., Wu, H., Niu, C., Sun, X., & Wang, K. (2022). Inhibition of temperature‐sensitive TRPV3 channel by two natural isochlorogenic acid isomers for alleviation of dermatitis and chronic pruritus. Acta Pharmaceutica Sinica B, 12, 723–734. https://doi.org/10.1016/j.apsb.2021.08.002
Singh, A. K., McGoldrick, L. L., Demirkhanyan, L., Leslie, M., Zakharian, E., & Sobolevsky, A. I. (2019). Structural basis of temperature sensation by the TRP channel TRPV3. Nature Structural & Molecular Biology, 26, 994–998. https://doi.org/10.1038/s41594‐019‐0318‐7
Chung, M.‐K., Güler, A. D., & Caterina, M. J. (2005). Biphasic currents evoked by chemical or thermal activation of the heat‐gated ion channel, TRPV3*. Journal of Biological Chemistry, 280, 15928–15941. https://doi.org/10.1074/jbc.M500596200
Li, M., Toombes, G. E. S., Silberberg, S. D., & Swartz, K. J. (2015). Physical basis of apparent pore dilation of ATP‐activated P2X receptor channels. Nature Neuroscience, 18, 1577–1583. https://doi.org/10.1038/nn.4120
Deering‐Rice, C. E., Mitchell, V. K., Romero, E. G., Abdel Aziz, M. H., Ryskamp, D. A., Križaj, D., Venkat, R. G., & Reilly, C. A. (2014). Drofenine: A 2‐APB analog with improved selectivity for human TRPV3. Pharmacology Research & Perspectives, 2, e00062. https://doi.org/10.1002/prp2.62
Su, W., Qiao, X., Wang, W., He, S., Liang, K., & Hong, X. (2023). TRPV3: Structure, diseases and modulators. Molecules, 28, 774. https://doi.org/10.3390/molecules28020774
Kalinovskii, A. P., Utkina, L. L., Korolkova, Y. V., & Andreev, Y. A. (2023). TRPV3 ion channel: From gene to pharmacology. International Journal of Molecular Sciences, 24, 8601. https://doi.org/10.3390/ijms24108601
Singh, A. K., McGoldrick, L. L., & Sobolevsky, A. I. (2018). Structure and gating mechanism of the transient receptor potential channel TRPV3. Nature Structural & Molecular Biology, 25, 805. https://doi.org/10.1038/s41594‐018‐0108‐7
Zubcevic, L., Borschel, W. F., Hsu, A. L., Borgnia, M. J., & Lee, S.‐Y. (2019). Regulatory switch at the cytoplasmic interface controls TRPV channel gating. eLife, 8, e47746. https://doi.org/10.7554/eLife.47746
Hu, H.‐Z., Gu, Q., Wang, C., Colton, C. K., Tang, J., Kinoshita‐Kawada, M., Lee, L.‐Y., Wood, J. D., & Zhu, M. X. (2004). 2‐Aminoethoxydiphenyl borate is a common activator of TRPV1, TRPV2, and TRPV3*. Journal of Biological Chemistry, 279, 35741–35748. https://doi.org/10.1074/jbc.M404164200
Singh, A. K., Saotome, K., Mcgoldrick, L. L., & Sobolevsky, A. I. (2018). Structural bases of TRP channel TRPV6 allosteric modulation by 2‐APB. Nature Communications, 9, 2465. https://doi.org/10.1038/s41467‐018‐04828‐y
Lievremont, J.‐P., Bird, G. S., & Putney, J. W. (2005). Mechanism of inhibition of TRPC cation channels by 2‐aminoethoxydiphenylborane. Molecular Pharmacology, 68, 758–762. https://doi.org/10.1124/mol.105.012856
Xu, S.‐Z., Zeng, F., Boulay, G., Grimm, C., Harteneck, C., & Beech, D. J. (2005). Block of TRPC5 channels by 2‐aminoethoxydiphenyl borate: A differential, extracellular and voltage‐dependent effect. British Journal of Pharmacology, 145, 405–414. https://doi.org/10.1038/sj.bjp.0706197
Togashi, K., Inada, H., & Tominaga, M. (2008). Inhibition of the transient receptor potential cation channel TRPM2 by 2‐aminoethoxydiphenyl borate (2‐APB). British Journal of Pharmacology, 153, 1324–1330. https://doi.org/10.1038/sj.bjp.0707675
Chokshi, R., Fruasaha, P., & Kozak, J. A. (2012). 2‐Aminoethyl diphenyl borinate (2‐APB) inhibits TRPM7 channels through an intracellular acidification mechanism. Channels (Austin), 6, 362–369. https://doi.org/10.4161/chan.21628
Colton, C. K., & Zhu, M. X. (2007). 2‐Aminoethoxydiphenyl borate as a common activator of TRPV1, TRPV2, and TRPV3 channels. Handbook of Experimental Pharmacology, 179, 173–187. https://doi.org/10.1007/978‐3‐540‐34891‐7_10
Moqrich, A., Hwang, S. W., Earley, T. J., Petrus, M. J., Murray, A. N., Spencer, K. S. R., Andahazy, M., Story, G. M., & Patapoutian, A. (2005). Impaired thermosensation in mice lacking TRPV3, a heat and camphor sensor in the skin. Science, 307, 1468–1472. https://doi.org/10.1126/science.1108609
Vogt‐Eisele, A. K., Weber, K., Sherkheli, M. A., Vielhaber, G., Panten, J., Gisselmann, G., & Hatt, H. (2007). Monoterpenoid agonists of TRPV3. British Journal of Pharmacology, 151, 530–540. https://doi.org/10.1038/sj.bjp.0707245
Xu, H., Blair, N. T., & Clapham, D. E. (2005). Camphor activates and strongly desensitizes the transient receptor potential vanilloid subtype 1 channel in a vanilloid‐independent mechanism. The Journal of Neuroscience, 25, 8924–8937. https://doi.org/10.1523/JNEUROSCI.2574‐05.2005
Selescu, T., Ciobanu, A. C., Dobre, C., Reid, G., & Babes, A. (2013). Camphor activates and sensitizes transient receptor potential melastatin 8 (TRPM8) to cooling and icilin. Chemical Senses, 38, 563–575. https://doi.org/10.1093/chemse/bjt027
Cheng, X., Jin, J., Hu, L., Shen, D., Dong, X.‐P., Samie, M. A., Knoff, J., Eisinger, B., Liu, M.‐L., Huang, S. M., Caterina, M. J., Dempsey, P., Michael, L. E., Dlugosz, A. A., Andrews, N. C., Clapham, D. E., & Xu, H. (2010). TRP channel regulates EGFR signaling in hair morphogenesis and skin barrier formation. Cell, 141, 331–343. https://doi.org/10.1016/j.cell.2010.03.013
Seo, S. H., Kim, S., Kim, S.‐E., Chung, S., & Lee, S. E. (2020). Enhanced thermal sensitivity of TRPV3 in keratinocytes underlies heat‐induced pruritogen release and pruritus in atopic dermatitis. Journal of Investigative Dermatology, 140, 2199–2209.e6. https://doi.org/10.1016/j.jid.2020.02.028
Zhang, F., Lin, Y., Min, W., Hou, Y., Yuan, K., Wang, J., & Yang, P. (2021). Computational discovery, structural optimization and biological evaluation of novel inhibitors targeting transient receptor potential vanilloid type 3 (TRPV3). Bioorganic Chemistry, 114, 105093. https://doi.org/10.1016/j.bioorg.2021.105093
Fan, J., Hu, L., Yue, Z., Liao, D., Guo, F., Ke, H., Jiang, D., Yang, Y., & Lei, X. (2023). Structural basis of TRPV3 inhibition by an antagonist. Nature Chemical Biology, 19, 81–90. https://doi.org/10.1038/s41589‐022‐01166‐5
Han, Y., Luo, A., Kamau, P. M., Takomthong, P., Hu, J., Boonyarat, C., Luo, L., & Lai, R. (2021). A plant‐derived TRPV3 inhibitor suppresses pain and itch. British Journal of Pharmacology, 178, 1669–1683. https://doi.org/10.1111/bph.15390
Sun, X.‐Y., Sun, L.‐L., Qi, H., Gao, Q., Wang, G.‐X., Wei, N.‐N., & Wang, K. (2018). Antipruritic effect of natural coumarin osthole through selective inhibition of thermosensitive TRPV3 channel in the skin. Molecular Pharmacology, 94, 1164–1173. https://doi.org/10.1124/mol.118.112466
Zhang, H., Sun, X., Qi, H., Ma, Q., Zhou, Q., Wang, W., & Wang, K. (2019). Pharmacological inhibition of the temperature‐sensitive and Ca2+‐permeable transient receptor potential vanilloid TRPV3 channel by natural forsythoside B attenuates pruritus and cytotoxicity of keratinocytes. Journal of Pharmacology and Experimental Therapeutics, 368, 21–31. https://doi.org/10.1124/jpet.118.254045
Neuberger, A., Nadezhdin, K. D., & Sobolevsky, A. I. (2022). Structural mechanism of TRPV3 channel inhibition by the anesthetic dyclonine. Nature Communications, 13, 2795. https://doi.org/10.1038/s41467‐022‐30537‐8
Zubcevic, L., Herzik, M. A., Wu, M., Borschel, W. F., Hirschi, M., Song, A. S., Lander, G. C., & Lee, S.‐Y. (2018). Conformational ensemble of the human TRPV3 ion channel. Nature Communications, 9, 4773. https://doi.org/10.1038/s41467‐018‐07117‐w
Shimada, H., Kusakizako, T., Dung Nguyen, T. H., Nishizawa, T., Hino, T., Tominaga, M., & Nureki, O. (2020). The structure of lipid nanodisc‐reconstituted TRPV3 reveals the gating mechanism. Nature Structural & Molecular Biology, 27, 645–652. https://doi.org/10.1038/s41594‐020‐0439‐z
Deng, Z., Maksaev, G., Rau, M., Xie, Z., Hu, H., Fitzpatrick, J. A. J., & Yuan, P. (2020). Gating of human TRPV3 in a lipid bilayer. Nature Structural & Molecular Biology, 27, 635–644. https://doi.org/10.1038/s41594‐020‐0428‐2
Nadezhdin, K. D., Neuberger, A., Trofimov, Y. A., Krylov, N. A., Sinica, V., Kupko, N., Vlachova, V., Zakharian, E., Efremov, R. G., & Sobolevsky, A. I. (2021). Structural mechanism of heat‐induced opening of a temperature‐sensitive TRP channel. Nature Structural & Molecular Biology, 28, 564–572. https://doi.org/10.1038/s41594‐021‐00615‐4
Lansky, S., Betancourt, J. M., Zhang, J., Jiang, Y., Kim, E. D., Paknejad, N., Nimigean, C. M., Yuan, P., & Scheuring, S. (2023). A pentameric TRPV3 channel with a dilated pore. Nature, 621, 206–214. https://doi.org/10.1038/s41586‐023‐06470‐1
Cao, E., Liao, M., Cheng, Y., & Julius, D. (2013). TRPV1 structures in distinct conformations reveal activation mechanisms. Nature, 504, 113–118. https://doi.org/10.1038/nature12823
Zubcevic, L., Herzik, M. A., Chung, B. C., Liu, Z., Lander, G. C., & Lee, S.‐Y. (2016). Cryo‐electron microscopy structure of the TRPV2 ion channel. Nature Structural & Molecular Biology, 23, 180–186. https://doi.org/10.1038/nsmb.3159
Saotome, K., Singh, A. K., Yelshanskaya, M. V., & Sobolevsky, A. I. (2016). Crystal structure of the epithelial calcium channel TRPV6. Nature, 534, 506–511. https://doi.org/10.1038/nature17975
Chowdhury, S., Jarecki, B. W., & Chanda, B. (2014). A molecular framework for temperature‐dependent gating of ion channels. Cell, 158, 1148–1158. https://doi.org/10.1016/j.cell.2014.07.026
Neuberger, A., & Sobolevsky, A. I. (2023). Pentameric TRPV3: An artifact or a clue to channel function? Cell Calcium, 116, 102812. https://doi.org/10.1016/j.ceca.2023.102812
Phelps, C. B., Wang, R. R., Choo, S. S., & Gaudet, R. (2010). Differential regulation of TRPV1, TRPV3, and TRPV4 sensitivity through a conserved binding site on the ankyrin repeat domain *. Journal of Biological Chemistry, 285, 731–740. https://doi.org/10.1074/jbc.M109.052548
Liu, B., Yao, J., Zhu, M. X., & Qin, F. (2011). Hysteresis of gating underlines sensitization of TRPV3 channels. Journal of General Physiology, 138, 509–520. https://doi.org/10.1085/jgp.201110689
Bollag, W. B. (2021). Down‐regulated calcium‐sensing receptor in keratinocytes and skin from aged mice and humans impairs function. Journal of Investigative Dermatology, 141, 2558–2561. https://doi.org/10.1016/j.jid.2021.04.005
Ciardo, M. G., & Ferrer‐Montiel, A. (2017). Lipids as central modulators of sensory TRP channels. Biochimica et Biophysica Acta (BBA)—Biomembranes, 1859, 1615–1628. https://doi.org/10.1016/j.bbamem.2017.04.012
Hu, H.‐Z., Xiao, R., Wang, C., Gao, N., Colton, C. K., Wood, J. D., & Zhu, M. X. (2006). Potentiation of TRPV3 channel function by unsaturated fatty acids. Journal of Cellular Physiology, 208, 201–212. https://doi.org/10.1002/jcp.20648
Klein, A. S., Tannert, A., & Schaefer, M. (2014). Cholesterol sensitises the transient receptor potential channel TRPV3 to lower temperatures and activator concentrations. Cell Calcium, 55, 59–68. https://doi.org/10.1016/j.ceca.2013.12.001
Doerner, J. F., Hatt, H., & Ramsey, I. S (2011). Voltage‐ and temperature‐dependent activation of TRPV3 channels is potentiated by receptor‐mediated PI(4,5)P2 hydrolysis. Journal of General Physiology, 137, 271–288. https://doi.org/10.1085/jgp.200910388
Cao, X., Yang, F., Zheng, J., & Wang, K. (2012). Intracellular proton‐mediated activation of TRPV3 channels accounts for the exfoliation effect of α‐hydroxyl acids on keratinocytes. Journal of Biological Chemistry, 287, 25905–25916. https://doi.org/10.1074/jbc.M112.364869
Gao, L., Yang, P., Qin, P., Lu, Y., Li, X., Tian, Q., Li, Y., Xie, C., Tian, J.‐B., Zhang, C., Tian, C., Zhu, M. X., & Yao, J. (2016). Selective potentiation of 2‐APB‐induced activation of TRPV1–3 channels by acid. Scientific Reports, 6, 20791. https://doi.org/10.1038/srep20791
Wang, H., Yang, P., Lu, Y., Wang, J., Jeon, J., Wang, Q., Tian, J.‐B., Zang, B., Yu, Y., & Zhu, M. X. (2021). Mechanisms of proton inhibition and sensitization of the cation channel TRPV3. Journal of General Physiology, 153, e202012663. https://doi.org/10.1085/jgp.202012663
Murata, T., Honda, T., Mostafa, A., & Kabashima, K. (2022). Stratum corneum as polymer sheet: Concept and cornification processes. Trends in Molecular Medicine, 28, 350–359. https://doi.org/10.1016/j.molmed.2022.02.008
Matsui, T., Kadono‐Maekubo, N., Suzuki, Y., Furuichi, Y., Shiraga, K., Sasaki, H., Ishida, A., Takahashi, S., Okada, T., Toyooka, K., Sharif, J., Abe, T., Kiyonari, H., Tominaga, M., Miyawaki, A., & Amagai, M. (2021). A unique mode of keratinocyte death requires intracellular acidification. Proceedings of the National Academy of Sciences, 118, e2020722118. https://doi.org/10.1073/pnas.2020722118
Liebe, H., Liebe, F., Sponder, G., Hedtrich, S., & Stumpff, F. (2021). Beyond Ca2+ signalling: The role of TRPV3 in the transport of NH4+. Pflügers Archiv ‐ European Journal of Physiology, 473, 1859–1884. https://doi.org/10.1007/s00424‐021‐02616‐0
Szöllősi, A. G., Vasas, N., Angyal, Á., Kistamás, K., Nánási, P. P., Mihály, J., Béke, G., Herczeg‐Lisztes, E., Szegedi, A., Kawada, N., Yanagida, T., Mori, T., Kemény, L., & Bíró, T. (2018). Activation of TRPV3 regulates inflammatory actions of human epidermal keratinocytes. Journal of Investigative Dermatology, 138, 365–374. https://doi.org/10.1016/j.jid.2017.07.852
Hoffstaetter, L. J., Bagriantsev, S. N., & Gracheva, E. O. (2018). TRPs et al.: A molecular toolkit for thermosensory adaptations. Pflügers Archiv ‐ European Journal of Physiology, 470, 745–759. https://doi.org/10.1007/s00424‐018‐2120‐5
Cheng, W., Yang, F., Liu, S., Colton, C. K., Wang, C., Cui, Y., Cao, X., Zhu, M. X., Sun, C., Wang, K., & Zheng, J. (2012). Heteromeric heat‐sensitive transient receptor potential channels exhibit distinct temperature and chemical response*. Journal of Biological Chemistry, 287, 7279–7288. https://doi.org/10.1074/jbc.M111.305045
Liu, B., & Qin, F. (2017). Single‐residue molecular switch for high‐temperature dependence of vanilloid receptor TRPV3. Proceedings of the National Academy of Sciences, 114, 1589–1594. https://doi.org/10.1073/pnas.1615304114
Lynch, V. J., Bedoya‐Reina, O. C., Ratan, A., Sulak, M., Drautz‐Moses, D. I., Perry, G. H., Miller, W., & Schuster, S. C. (2015). Elephantid genomes reveal the molecular bases of Woolly Mammoth adaptations to the arctic. Cell Reports, 12, 217–228. https://doi.org/10.1016/j.celrep.2015.06.027
Saito, S., Fukuta, N., Shingai, R., & Tominaga, M. (2011). Evolution of vertebrate transient receptor potential vanilloid 3 channels: Opposite temperature sensitivity between mammals and western clawed frogs. PLOS Genetics, 7, e1002041. https://doi.org/10.1371/journal.pgen.1002041
Huang, S. M., Li, X., Yu, Y., Wang, J., & Caterina, M. J. (2011). TRPV3 and TRPV4 ion channels are not major contributors to mouse heat sensation. Molecular Pain, 7, 1744‐8069‐7–37. https://doi.org/10.1186/1744‐8069‐7‐37
Miyamoto, T., Petrus, M. J., Dubin, A. E., & Patapoutian, A. (2011). TRPV3 regulates nitric oxide synthase‐independent nitric oxide synthesis in the skin. Nature Communications, 2, 369. https://doi.org/10.1038/ncomms1371
Schaefer, M. (2024). TRPV3 returns with a pleasant feeling of warmth. Cell Calcium, 118, 102853. https://doi.org/10.1016/j.ceca.2024.102853
Dhaka, A., Murray, A. N., Mathur, J., Earley, T. J., Petrus, M. J., & Patapoutian, A. (2007). TRPM8 is required for cold sensation in mice. Neuron, 54, 371–378. https://doi.org/10.1016/j.neuron.2007.02.024
Caterina, M. J., Leffler, A., Malmberg, A. B., Martin, W. J., Trafton, J., Petersen‐Zeitz, K. R., Koltzenburg, M., Basbaum, A. I., & Julius, D. (2000). Impaired nociception and pain sensation in mice lacking the capsaicin receptor. Science, 288, 306–313. https://doi.org/10.1126/science.288.5464.306
Chung, M.‐K., Lee, H., Mizuno, A., Suzuki, M., & Caterina, M. J. (2004). TRPV3 and TRPV4 mediate warmth‐evoked currents in primary mouse keratinocytes *. Journal of Biological Chemistry, 279, 21569–21575. https://doi.org/10.1074/jbc.M401872200
Hu, F., Cao, X., Niu, C., & Wang, K. (2022). Coassembly of warm temperature–Sensitive transient receptor potential vanilloid (TRPV) 3 and TRPV4 channel complexes with distinct functional properties. Molecular Pharmacology, 101, 390–399. https://doi.org/10.1124/molpharm.121.000370
Sadler, K. E., Moehring, F., & Stucky, C. L. (2020). Keratinocytes contribute to normal cold and heat sensation. eLife, 9, e58625. https://doi.org/10.7554/eLife.58625
Mandadi, S., Sokabe, T., Shibasaki, K., Katanosaka, K., Mizuno, A., Moqrich, A., Patapoutian, A., Fukumi‐Tominaga, T., Mizumura, K., & Tominaga, M. (2009). TRPV3 in keratinocytes transmits temperature information to sensory neurons via ATP. Pflügers Archiv ‐ European Journal of Physiology, 458, 1093–1102. https://doi.org/10.1007/s00424‐009‐0703‐x
Souslova, V., Cesare, P., Ding, Y., Akopian, A. N., Stanfa, L., Suzuki, R., Carpenter, K., Dickenson, A., Boyce, S., Hill, R., Nebenius‐Oosthuizen, D., Smith, A. J. H., Kidd, E. J., & Wood, J. N. (2000). Warm‐coding deficits and aberrant inflammatory pain in mice lacking P2×3 receptors. Nature, 407, 1015–1017. https://doi.org/10.1038/35039526
Shimizu, I., Iida, T., Guan, Y., Zhao, C., Raja, S. N., Jarvis, M. F., Cockayne, D. A., & Caterina, M. J. (2005). Enhanced thermal avoidance in mice lacking the ATP receptor P2×3. Pain, 116, 96–108. https://doi.org/10.1016/j.pain.2005.03.030
Huang, S. M., Lee, H., Chung, M.‐K., Park, U., Yu, Y. Y., Bradshaw, H. B., Coulombe, P. A., Walker, J. M, & Caterina, M. J. (2008). Overexpressed transient receptor potential vanilloid 3 ion channels in skin keratinocytes modulate pain sensitivity via prostaglandin E2. The Journal of Neuroscience, 28, 13727–13737. https://doi.org/10.1523/JNEUROSCI.5741‐07.2008
Wang, Y., Li, H., Xue, C., Chen, H., Xue, Y., Zhao, F., Zhu, M. X., & Cao, Z. (2021). TRPV3 enhances skin keratinocyte proliferation through EGFR‐dependent signaling pathways. Cell Biology and Toxicology, 37, 313–330. https://doi.org/10.1007/s10565‐020‐09536‐2
Yamanoi, Y., Lei, J., Takayama, Y., Hosogi, S., Marunaka, Y., & Tominaga, M. (2023). TRPV3‐ANO1 interaction positively regulates wound healing in keratinocytes. Communications Biology, 6, 1–13. https://doi.org/10.1038/s42003‐023‐04482‐1
Song, Z., Chen, X., Zhao, Q., Stanic, V., Lin, Z., Yang, S., Chen, T., Chen, J., & Yang, Y. (2021). Hair loss caused by gain‐of‐function mutant TRPV3 is associated with premature differentiation of follicular keratinocytes. Journal of Investigative Dermatology, 141, 1964–1974. https://doi.org/10.1016/j.jid.2020.11.036
Zhong, W., Hu, L., Cao, X., Zhao, J., Zhang, X., Lee, M., Wang, H., Zhang, J., Chen, Q., Feng, C., Duo, L., Wang, X., Tang, L., Lin, Z., & Yang, Y. (2021). Genotype‒Phenotype correlation of TRPV3‐related Olmsted syndrome. Journal of Investigative Dermatology, 141, 545–554. https://doi.org/10.1016/j.jid.2020.06.035
Lin, Z., Chen, Q., Lee, M., Cao, X., Zhang, J., Ma, D., Chen, L., Hu, X., Wang, H., Wang, X., Zhang, P., Liu, X., Guan, L., Tang, Y., Yang, H., Tu, P., Bu, D., Zhu, X., Wang, K., … Yang, Y. (2012). Exome sequencing reveals mutations in TRPV3 as a cause of Olmsted syndrome. The American Journal of Human Genetics, 90, 558–564. https://doi.org/10.1016/j.ajhg.2012.02.006
Guo, Y., Song, Y., Liu, W., Wang, T., Ma, X., & Yu, Z. (2023). Novel insights into the role of keratinocytes‐expressed TRPV3 in the skin. Biomolecules, 13, 513. https://doi.org/10.3390/biom13030513
Xiao, R., Tian, J., Tang, J., & Zhu, M. X. (2008). The TRPV3 mutation associated with the hairless phenotype in rodents is constitutively active. Cell Calcium, 43, 334–343. https://doi.org/10.1016/j.ceca.2007.06.004
Yoshioka, T., Imura, K., Asakawa, M., Suzuki, M., Oshima, I., Hirasawa, T., Sakata, T., Horikawa, T., & Arimura, A. (2009). Impact of the Gly573Ser substitution in TRPV3 on the development of allergic and pruritic dermatitis in mice. Journal of Investigative Dermatology, 129, 714–722. https://doi.org/10.1038/jid.2008.245
Sulk, M., Seeliger, S., Aubert, J., Schwab, V. D., Cevikbas, F., Rivier, M., Nowak, P., Voegel, J. J., Buddenkotte, J., & Steinhoff, M. (2012). Distribution and expression of non‐neuronal transient receptor potential (TRPV) ion channels in Rosacea. Journal of Investigative Dermatology, 132, 1253–1262. https://doi.org/10.1038/jid.2011.424
Nattkemper, L. A., Tey, H. L., Valdes‐Rodriguez, R., Lee, H., Mollanazar, N. K., Albornoz, C., Sanders, K. M., & Yosipovitch, G. (2018). The genetics of chronic itch: Gene expression in the skin of patients with atopic dermatitis and psoriasis with severe itch. Journal of Investigative Dermatology, 138, 1311–1317. https://doi.org/10.1016/j.jid.2017.12.029
Larkin, C., Chen, W., Szabó, I. L., Shan, C., Dajnoki, Z., Szegedi, A., Buhl, T., Fan, Y., O'neill, S., Walls, D., Cheng, W., Xiao, S., Wang, J., & Meng, J. (2021). Novel insights into the TRPV3‐mediated itch in atopic dermatitis. Journal of Allergy and Clinical Immunology, 147, 1110–1114.e5. https://doi.org/10.1016/j.jaci.2020.09.028
Vasas, N., Pénzes, Z., Kistamás, K., Nánási, P. P., Molnár, S., Szegedi, A., Szöllősi, A. G., & Bíró, T. (2022). Transient receptor potential vanilloid 3 expression is increased in non‐lesional skin of atopic dermatitis patients. Experimental Dermatology, 31, 807–813. https://doi.org/10.1111/exd.14530
Cui, T.‐T., Wang, G.‐X., Wei, N.‐N., & Wang, K. (2018). A pivotal role for the activation of TRPV3 channel in itch sensations induced by the natural skin sensitizer carvacrol. Acta Pharmacologica Sinica, 39, 331–335. https://doi.org/10.1038/aps.2017.152
Dang, T. H., Kim, J. Y., Kim, H. J., Kim, B. J., Kim, W. K., & Nam, J. H. (2023). Alpha‐Mangostin: A potent inhibitor of TRPV3 and pro‐inflammatory cytokine secretion in keratinocytes. International Journal of Molecular Sciences, 24, 12930. https://doi.org/10.3390/ijms241612930
Zhao, J., Munanairi, A., Liu, X.‐Y., Zhang, J., Hu, L., Hu, M., Bu, D., Liu, L., Xie, Z., Kim, B. S., Yang, Y., & Chen, Z.‐F. (2020). PAR2 mediates itch via TRPV3 signaling in keratinocytes. Journal of Investigative Dermatology, 140, 1524–1532. https://doi.org/10.1016/j.jid.2020.01.012
Sasaki, T., Shiohama, A., Kubo, A., Kawasaki, H., Ishida‐Yamamoto, A., Yamada, T., Hachiya, T., Shimizu, A., Okano, H., Kudoh, J., & Amagai, M. (2013). A homozygous nonsense mutation in the gene for Tmem79, a component for the lamellar granule secretory system, produces spontaneous eczema in an experimental model of atopic dermatitis. Journal of Allergy and Clinical Immunology, 132, 1111–1120.e4. https://doi.org/10.1016/j.jaci.2013.08.027
Saunders, S. P., Goh, C. S. M., Brown, S. J., Palmer, C. N. A., Porter, R. M., Cole, C., Campbell, L. E., Gierlinski, M., Barton, G. J., Schneider, G., Balmain, A., Prescott, A. R., Weidinger, S., Baurecht, H., Kabesch, M., Gieger, C., Lee, Y.‐A., Tavendale, R., Mukhopadhyay, S., … Fallon, P. G. (2013). Tmem79/Matt is the matted mouse gene and is a predisposing gene for atopic dermatitis in human subjects. Journal of Allergy and Clinical Immunology, 132, 1121–1129. https://doi.org/10.1016/j.jaci.2013.08.046
Saunders, S. P., Floudas, A., Moran, T., Byrne, C M., Rooney, M. D., Fahy, C. M. R., Geoghegan, J. A., Iwakura, Y., Fallon, P. G., & Schwartz, C. (2020). Dysregulated skin barrier function in Tmem79 mutant mice promotes IL‐17A‐dependent spontaneous skin and lung inflammation. Allergy, 75, 3216–3227. https://doi.org/10.1111/all.14488
Emrick, J. J., Mathur, A., Wei, J., Gracheva, E. O., Gronert, K., Rosenblum, M. D., & Julius, D. (2018). Tissue‐specific contributions of Tmem79 to atopic dermatitis and mast cell‐mediated histaminergic itch. Proceedings of the National Academy of Sciences, 115, E12091–E12100. https://doi.org/10.1073/pnas.1814132115
Asakawa, M., Yoshioka, T., Matsutani, T., Hikita, I., Suzuki, M., Oshima, I., Tsukahara, K., Arimura, A., Horikawa, T., Hirasawa, T., & Sakata, T. (2006). Association of a mutation in TRPV3 with defective hair growth in rodents. Journal of Investigative Dermatology, 126, 2664–2672. https://doi.org/10.1038/sj.jid.5700468
Sugaya, M. (2020). The role of Th17‐related cytokines in atopic dermatitis. International Journal of Molecular Sciences, 21, 1314. https://doi.org/10.3390/ijms21041314
Morimoto, A., Fukuda, K., Ito, Y., Tahara, U., Sasaki, T., Shiohama, A., Kawasaki, H., Kawakami, E., Naganuma, T., Arita, M., Sasaki, H., Koseki, H., Matsui, T., & Amagai, M. (2022). Microbiota‐independent spontaneous dermatitis associated with increased sebaceous lipid production in Tmem79‐deficient mice. Journal of Investigative Dermatology, 142, 2864–2872.e6. https://doi.org/10.1016/j.jid.2022.06.003