Transient Receptor Potential Channels TRPM4 and TRPC3 Critically Contribute to Respiratory Motor Pattern Formation but Not Rhythmogenesis in Rodent Brainstem Circuits
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The Structural Basis for an On–Off Switch Controlling Gβγ-Mediated Inhibition of TRPM3 Channels
The structural basis for an on–off switch controlling Gβγ-mediated inhibition of TRPM3 channels Marc Behrendta,b,1,2, Fabian Grussc,1,3, Raissa Enzerotha,b, Sandeep Demblaa,b, Siyuan Zhaod, Pierre-Antoine Crassousd, Florian Mohra, Mieke Nysc, Nikolaos Lourose, Rodrigo Gallardoe,4, Valentina Zorzinif,5, Doris Wagnera, Anastassios Economou (Αναστάσιoς Οικoνόμoυ)f, Frederic Rousseaue, Joost Schymkowitze, Stephan E. Philippg, Tibor Rohacsd, Chris Ulensc,6, and Johannes Oberwinklera,b,6 aInstitut für Physiologie und Pathophysiologie, Philipps-Universität Marburg, 35037 Marburg, Germany;bCenter for Mind, Brain and Behavior (CMBB), Philipps-Universität Marburg and Justus-Liebig-Universität Giessen, 35032 Marburg, Germany; cLaboratory of Structural Neurobiology, Department of Cellular and Molecular Medicine, KU Leuven, 3000 Leuven, Belgium; dDepartment of Pharmacology, Physiology and Neuroscience, Rutgers New Jersey Medical School, Newark, NJ 07103; eSwitch Laboratory, VIB Center for Brain and Disease Research, Department of Cellular and Molecular Medicine, KU Leuven, 3000 Leuven, Belgium; fLaboratory of Molecular Bacteriology, Department of Microbiology and Immunology, Rega Institute for Medical Research, KU Leuven, 3000 Leuven, Belgium; and gExperimentelle und Klinische Pharmakologie und Toxikologie, Universität des Saarlandes, 66421 Homburg, Germany Edited by László Csanády, Semmelweis University, Budapest, Hungary, and accepted by Editorial Board Member David E. Clapham August 27, 2020 (received for review February 13, 2020) TRPM3 channels play important roles in the detection of noxious also subject to inhibition by activated μORsorotherGPCRs(6, heat and in inflammatory thermal hyperalgesia. The activity of 24–28), a process that has been shown to take place in peripheral these ion channels in somatosensory neurons is tightly regulated by endings of nociceptive neurons since locally applied μOR or μ βγ -opioid receptors through the signaling of G proteins, thereby GABA receptor agonists inhibit TRPM3-dependent pain (24–26). -
The TRPP2-Dependent Channel of Renal Primary Cilia Also Requires TRPM3
The TRPP2-dependent channel of renal primary cilia also requires TRPM3 Steven J. Kleene1, Brian J. Siroky2, Julio A. Landero-Figueroa3, Bradley P. Dixon4, Nolan W. Pachciarz2, Lu Lu2, and Nancy K. Kleene1 1Department of Pharmacology and Systems Physiology, University of Cincinnati, Cincinnati, Ohio; 2Division of Nephrology and Hypertension, Cincinnati Children's Hospital Medical Center, Cincinnati, Ohio; 3Department of Chemistry, University of Cincinnati, Cincinnati, Ohio; 4Renal Section, Department of Pediatrics, University of Colorado School of Medicine, Aurora, Colorado IntroductIon Primary cilia of renal epithelial cells express several members of the transient receptor potential (TRP) class of cation-conducting channel, including TRPC1, TRPM3, TRPM4, TRPP2, and TRPV4. Some cases of autosomal dominant polycystic kidney disease (ADPKD) are caused by defects in TRPP2 (also called polycystin-2, PC2, or PKD2). A large-conductance, TRPP2- dependent channel in renal cilia has been well described, but it is not known whether this channel includes any other protein subunits. Methods To study this question, we investigated the pharmacology of the TRPP2-dependent channel through electrical recordings from the cilia of mIMCD-3 cells, a murine cell line of renal epithelial origin, results The pharmacology was found to match that of TRPM3 channels. The ciliary TRPP2-dependent channel is known to be activated by depolarization and/or increasing cytoplasmic Ca2+. This activation was greatly enhanced by external pregnenolone sulfate, an agonist of TRPM3 channels. Pregnenolone sulfate did not change the current-voltage relation of the channel. CIM0216, another TRPM3 agonist, modestly increased the activity of the ciliary channels. The channels were effectively blocked by isosakuranetin, a specific inhibitor of TRPM3 channels. -
The TRPM4 Channel Inhibitor 9-Phenanthrol
W&M ScholarWorks Arts & Sciences Articles Arts and Sciences 2014 The TRPM4 channel inhibitor 9-phenanthrol R. Guinamard T. Hof C. A. Del Negro College of William and Mary Follow this and additional works at: https://scholarworks.wm.edu/aspubs Recommended Citation Guinamard, R., Hof, T., & Del Negro, C. A. (2014). The TRPM4 channel inhibitor 9‐phenanthrol. British Journal of Pharmacology, 171(7), 1600-1613. This Article is brought to you for free and open access by the Arts and Sciences at W&M ScholarWorks. It has been accepted for inclusion in Arts & Sciences Articles by an authorized administrator of W&M ScholarWorks. For more information, please contact [email protected]. British Journal of DOI:10.1111/bph.12582 www.brjpharmacol.org BJP Pharmacology REVIEW Correspondence Romain Guinamard, Groupe Signalisation, Electrophysiologie et Imagerie des Lésions The TRPM4 channel d’Ischémie/Reperfusion Myocardique, EA4650, Université de Caen Basse Normandie, inhibitor 9-phenanthrol Sciences D, Esplande de la Paix, CS 14032, 14032 Caen Cedex 5, R Guinamard1,2, T Hof1 and C A Del Negro2 France. E-mail: [email protected] ---------------------------------------------------------------- 1EA 4650, Groupe Signalisation, Electrophysiologie et Imagerie des Lésions d’Ischémie-Reperfusion Myocardique, UCBN, Normandie Université, Caen, France, 2Department Keywords 9-phenanthrol; TRPM4; of Applied Science, The College of William and Mary, Williamsburg, VA, USA calcium-activated non-selective cation channel; cardioprotection; NSCCa ---------------------------------------------------------------- Received 1 November 2013 Revised 17 December 2013 Accepted 8 January 2014 The phenanthrene-derivative 9-phenanthrol is a recently identified inhibitor of the transient receptor potential melastatin (TRPM) 4 channel, a Ca2+-activated non-selective cation channel whose mechanism of action remains to be determined. -
Involvement of TRPC4 and 5 Channels in Persistent Firing in Hippocampal CA1 Pyramidal Cells
cells Article Involvement of TRPC4 and 5 Channels in Persistent Firing in Hippocampal CA1 Pyramidal Cells Alberto Arboit 1,2,3, Antonio Reboreda 1,4 and Motoharu Yoshida 1,3,4,5,* 1 German Center for Neurodegenerative Diseases (DZNE), 39120 Magdeburg, Germany; [email protected] (A.A.); [email protected] (A.R.) 2 Otto-von-Guericke University, 39120 Magdeburg, Germany 3 Faculty of Psychology, Ruhr University Bochum (RUB), Universitätsstraße 150, 44801 Bochum, Germany 4 Leibniz Institute for Neurobiology (LIN), 39118 Magdeburg, Germany 5 Center for Behavioral Brain Sciences (CBBS), 39106 Magdeburg, Germany * Correspondence: [email protected] Received: 1 December 2019; Accepted: 1 February 2020; Published: 5 February 2020 Abstract: Persistent neural activity has been observed in vivo during working memory tasks, and supports short-term (up to tens of seconds) retention of information. While synaptic and intrinsic cellular mechanisms of persistent firing have been proposed, underlying cellular mechanisms are not yet fully understood. In vitro experiments have shown that individual neurons in the hippocampus and other working memory related areas support persistent firing through intrinsic cellular mechanisms that involve the transient receptor potential canonical (TRPC) channels. Recent behavioral studies demonstrating the involvement of TRPC channels on working memory make the hypothesis that TRPC driven persistent firing supports working memory a very attractive one. However, this view has been challenged by recent findings that persistent firing in vitro is unchanged in TRPC knock out (KO) mice. To assess the involvement of TRPC channels further, we tested novel and highly specific TRPC channel blockers in cholinergically induced persistent firing in mice CA1 pyramidal cells for the first time. -
Heteromeric TRP Channels in Lung Inflammation
cells Review Heteromeric TRP Channels in Lung Inflammation Meryam Zergane 1, Wolfgang M. Kuebler 1,2,3,4,5,* and Laura Michalick 1,2 1 Institute of Physiology, Charité—Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin, Humboldt-Universität zu Berlin, and Berlin Institute of Health, 10117 Berlin, Germany; [email protected] (M.Z.); [email protected] (L.M.) 2 German Centre for Cardiovascular Research (DZHK), 10785 Berlin, Germany 3 German Center for Lung Research (DZL), 35392 Gießen, Germany 4 The Keenan Research Centre for Biomedical Science, St. Michael’s Hospital, Toronto, ON M5B 1W8, Canada 5 Department of Surgery and Physiology, University of Toronto, Toronto, ON M5S 1A8, Canada * Correspondence: [email protected] Abstract: Activation of Transient Receptor Potential (TRP) channels can disrupt endothelial bar- rier function, as their mediated Ca2+ influx activates the CaM (calmodulin)/MLCK (myosin light chain kinase)-signaling pathway, and thereby rearranges the cytoskeleton, increases endothelial permeability and thus can facilitate activation of inflammatory cells and formation of pulmonary edema. Interestingly, TRP channel subunits can build heterotetramers, whereas heteromeric TRPC1/4, TRPC3/6 and TRPV1/4 are expressed in the lung endothelium and could be targeted as a protec- tive strategy to reduce endothelial permeability in pulmonary inflammation. An update on TRP heteromers and their role in lung inflammation will be provided with this review. Keywords: heteromeric TRP assemblies; pulmonary inflammation; endothelial permeability; TRPC3/6; TRPV1/4; TRPC1/4 Citation: Zergane, M.; Kuebler, W.M.; Michalick, L. Heteromeric TRP Channels in Lung Inflammation. Cells 1. Introduction 2021, 10, 1654. https://doi.org Pulmonary microvascular endothelial cells are a key constituent of the blood air bar- /10.3390/cells10071654 rier that has to be extremely thin (<1 µm) to allow for rapid and efficient alveolo-capillary gas exchange. -
FKBP52 Regulates TRPC3-Dependent Ca<Sup>
© 2019. Published by The Company of Biologists Ltd | Journal of Cell Science (2019) 132, jcs231506. doi:10.1242/jcs.231506 RESEARCH ARTICLE FKBP52 regulates TRPC3-dependent Ca2+ signals and the hypertrophic growth of cardiomyocyte cultures Sandra Bandleon1, Patrick P. Strunz1, Simone Pickel2, Oleksandra Tiapko3, Antonella Cellini1, Erick Miranda-Laferte2 and Petra Eder-Negrin1,* ABSTRACT A single TRPC subunit is composed of six transmembrane The transient receptor potential (TRP; C-classical, TRPC) channel domains with a pore-forming loop connecting the transmembrane ‘ ’ TRPC3 allows a cation (Na+/Ca2+) influx that is favored by the domains 5 and 6, a preserved 25 amino acid sequence called a TRP domain and two cytosolic domains, an N-terminal ankyrin repeat stimulation of Gq protein-coupled receptors (GPCRs). An enhanced TRPC3 activity is related to adverse effects, including pathological domain and a C-terminal coiled-coil domain (Eder et al., 2007; Fan hypertrophy in chronic cardiac disease states. In the present study, et al., 2018). The cytosolic domains mediate ion channel formation we identified FK506-binding protein 52 (FKBP52, also known as and are implicated in ion channel regulation and plasma membrane FKBP4) as a novel interaction partner of TRPC3 in the heart. FKBP52 targeting (Eder et al., 2007). Among several protein interaction sites, was recovered from a cardiac cDNA library by a C-terminal TRPC3 the C-terminus of all TRPC subunits harbors a highly conserved fragment (amino acids 742–848) in a yeast two-hybrid screen. proline-rich sequence that corresponds to the binding domain in the Drosophila Downregulation of FKBP52 promoted a TRPC3-dependent photoreceptor channel TRPL for the FK506-binding hypertrophic response in neonatal rat cardiomyocytes (NRCs). -
Ion Channels 3 1
r r r Cell Signalling Biology Michael J. Berridge Module 3 Ion Channels 3 1 Module 3 Ion Channels Synopsis Ion channels have two main signalling functions: either they can generate second messengers or they can function as effectors by responding to such messengers. Their role in signal generation is mainly centred on the Ca2 + signalling pathway, which has a large number of Ca2+ entry channels and internal Ca2+ release channels, both of which contribute to the generation of Ca2 + signals. Ion channels are also important effectors in that they mediate the action of different intracellular signalling pathways. There are a large number of K+ channels and many of these function in different + aspects of cell signalling. The voltage-dependent K (KV) channels regulate membrane potential and + excitability. The inward rectifier K (Kir) channel family has a number of important groups of channels + + such as the G protein-gated inward rectifier K (GIRK) channels and the ATP-sensitive K (KATP) + + channels. The two-pore domain K (K2P) channels are responsible for the large background K current. Some of the actions of Ca2 + are carried out by Ca2+-sensitive K+ channels and Ca2+-sensitive Cl − channels. The latter are members of a large group of chloride channels and transporters with multiple functions. There is a large family of ATP-binding cassette (ABC) transporters some of which have a signalling role in that they extrude signalling components from the cell. One of the ABC transporters is the cystic − − fibrosis transmembrane conductance regulator (CFTR) that conducts anions (Cl and HCO3 )and contributes to the osmotic gradient for the parallel flow of water in various transporting epithelia. -
Structure of Full-Length Human TRPM4
Structure of full-length human TRPM4 Jingjing Duana,1, Zongli Lib,c,1, Jian Lid,e,1, Ana Santa-Cruza, Silvia Sanchez-Martineza, Jin Zhangd,2, and David E. Claphama,f,g,2 aHoward Hughes Medical Institute, Ashburn, VA 20147; bHoward Hughes Medical Institute, Harvard Medical School, Boston, MA 02115; cDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115; dSchool of Basic Medical Sciences, Nanchang University, Nanchang, 330031 Jiangxi, China; eDepartment of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, KY 40536; fDepartment of Neurobiology, Harvard Medical School, Boston, MA 02115; and gDepartment of Cardiology, Boston Children’s Hospital, Boston, MA 02115 Contributed by David E. Clapham, January 25, 2018 (sent for review December 19, 2017; reviewed by Mark T. Nelson, Dejian Ren, and Thomas Voets) Transient receptor potential melastatin subfamily member 4 Structure of Human TRPM4 (TRPM4) is a widely distributed, calcium-activated, monovalent- Full-length human TRPM4 (1,214 residues) was expressed using selective cation channel. Mutations in human TRPM4 (hTRPM4) the BacMam expression system (Materials and Methods). The result in progressive familial heart block. Here, we report the + TRPM4 construct used for expression retained the key func- electron cryomicroscopy structure of hTRPM4 in a closed, Na - tional properties of the wild-type channel, such as permeability + + bound, apo state at pH 7.5 to an overall resolution of 3.7 Å. Five to Na and K and activation by intracellular calcium (Fig. S1A). partially hydrated sodium ions are proposed to occupy the center The protein, obtained in the absence of exogenous calcium ions, of the conduction pore and the entrance to the coiled-coil domain. -
TRPC3 Channels Confer Cellular Memory of Recent Neuromuscular Activity
TRPC3 channels confer cellular memory of recent neuromuscular activity Paul Rosenberg*, April Hawkins*, Jonathan Stiber*, John M. Shelton†, Kelley Hutcheson*, Rhonda Bassel-Duby†, Dong Min Shin‡, Zhen Yan*, and R. Sanders Williams*§ *Departments of Internal Medicine and Pharmacology, Duke University Medical School, Durham, NC 27710; †Department of Molecular Biology and Medicine, University of Texas Southwestern Medical Center, Dallas, TX 75390; and ‡Department of Oral Biology, Yonsei University, Seoul 120-749, South Korea Edited by Charles F. Stevens, The Salk Institute for Biological Studies, La Jolla, CA, and approved May 11, 2004 (received for review December 9, 2003) Skeletal muscle adapts to different patterns of motor nerve activity a role for non-voltage-dependent calcium influx from the by alterations in gene expression that match specialized properties extracellular space in controlling the subcellular compartmen- of contraction, metabolism, and muscle mass to changing work talization and transactivator function of NFAT. In particular, demands (muscle plasticity). Calcineurin, a calcium͞calmodulin- expression of TRPC3, a nonselective calcium influx channel, is dependent, serine–threonine protein phosphatase, has been increased in response to neurostimulation and activated cal- shown to control programs of gene expression in skeletal muscles, cineurin and is limiting to NFAT-dependent transactivation. as in other cell types, through the transcription factor nuclear We propose that TRPC3 channels participate in a positive factor of activated T cells (NFAT). This study provides evidence that feedback circuit, thereby conferring a form of cellular memory the function of NFAT as a transcriptional activator is regulated by that is a prominent feature of adaptive plasticity of skeletal neuromuscular stimulation in muscles of intact animals and that muscles in response to neurostimulation. -
Ca Influx and Protein Scaffolding Via TRPC3 Sustain PKC and ERK
Research Article 927 Ca2+ influx and protein scaffolding via TRPC3 sustain PKC and ERK activation in B cells Takuro Numaga1,2, Motohiro Nishida3, Shigeki Kiyonaka1,4, Kenta Kato1, Masahiro Katano1, Emiko Mori1, Tomohiro Kurosaki5, Ryuji Inoue6, Masaki Hikida7, James W. Putney, Jr2 and Yasuo Mori1,4,* 1Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Kyoto 615-8510, Japan 2Laboratory of Signal Transduction, National Institute of Environmental Health Sciences, National Institutes of Health, Department of Health and Human Services, Research Triangle Park, NC 27709, USA 3Department of Pharmacology and Toxicology, Graduate School of Pharmaceutical Sciences, Kyushu University, Higashi-ku, Fukuoka 812-8582, Japan 4CREST, JST, Chiyoda-ku, Tokyo 102-0075, Japan 5Laboratory for Lymphocyte Differentiation, RIKEN Research Center for Allergy and Immunology, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan 6Department of Physiology, School of Medicine, Fukuoka University, Jonan-ku, Fukuoka 814-0180, Japan 7Center for Innovation in Immunoregulative Technology and Therapeutics, Graduate School of Medicine, Kyoto University, Kyoto 606-8501, Japan *Author for correspondence ([email protected]) Accepted 18 December 2009 Journal of Cell Science 123, 927-938 © 2010. Published by The Company of Biologists Ltd doi:10.1242/jcs.061051 Summary 2+ Ca signaling mediated by phospholipase C that produces inositol 1,4,5-trisphosphate [Ins(1,4,5)P3] and diacylglycerol (DAG) controls 2+ 2+ lymphocyte activation. In contrast to store-operated Ca entry activated by Ins(1,4,5)P3-induced Ca release from endoplasmic reticulum, the importance of DAG-activated Ca2+ entry remains elusive. Here, we describe the physiological role of DAG-activated Ca2+ entry channels in B-cell receptor (BCR) signaling. -
Distribution Profiles of Transient Receptor Potential Melastatin-Related and Vanilloid-Related Channels in Prostatic Tissue in Rat
TRPM and TRPV in rat prostate DOI: 10.1111/j.1745-7262.2007.00291.x www.asiaandro.com .Original Article . Distribution profiles of transient receptor potential melastatin-related and vanilloid-related channels in prostatic tissue in rat Huai-Peng Wang*, Xiao-Yong Pu*, Xing-Huan Wang Department of Urology, Guangdong Provnicial People’s Hospital, Guangzhou 510080, China Abstract Aim: To investigate the expression and distribution of the members of the transient receptor potential (TRP) channel members of TRP melastatin (TRPM) and TRP vanilloid (TRPV) subfamilies in rat prostatic tissue. Methods: Pros- tate tissue was obtained from male Sprague-Dawley rats. Reverse transcription polymerase chain reaction (RT-PCR) and quantitative real-time polymerase chain reaction (PCR) were used to check the expression of all TRPM and TRPV channel members with specific primers. Immunohistochemistry staining for TRPM8 and TRPV1 were also per- formed in rat tissues. Results: TRPM2, TRPM3, TRPM4, TRPM6, TRPM7, TRPM8, TRPV2 and TRPV4 mRNA were detected in all rat prostatic tissues. Very weak signals for TRPM1, TRPV1 and TRPV3 were also detected. The mRNA of TRPM5, TRPV5 and TRPV6 were not detected in all RT-PCR experiments. Quantitative real-time RT-PCR showed that TRPM2, TRPM3, TRPM4, TRPM8, TRPV2 and TRPV4 were the most abundantly expressed TRPM and TRPV subtypes, respectively. Fluorescence immunohistochemistry indicated that TRPM8 and TRPV1 are highly expressed in both epithelial and smooth muscle cells. Conclusion: Our results demonstrate that mRNA or protein for TRPM1, TRPM2, TRPM3, TRPM4, TRPM6, TRPM7, TRPM8, TRPV1, TRPV2, TRPV3 and TRPV4 exist in rat prostatic tissue. The data presented here assists in elucidating the physiological function of TRPM and TRPV channels. -
Transient Receptor Potential Canonical (TRPC) Channels As Modulators of Migration and Invasion
International Journal of Molecular Sciences Review Transient Receptor Potential Canonical (TRPC) Channels as Modulators of Migration and Invasion Muhammad Yasir Asghar 1,2 and Kid Törnquist 1,2,* 1 Minerva Foundation Institute for Medical Research, Biomedicum Helsinki 2U, Tukholmankatu 8, 00290 Helsinki, Finland; yasir.asghar@helsinki.fi 2 Faculty of Science and Engineering, Cell Biology, Åbo Akademi University, Tykistökatu 6A, 20520 Turku, Finland * Correspondence: ktornqvi@abo.fi Received: 11 February 2020; Accepted: 26 February 2020; Published: 3 March 2020 Abstract: Calcium (Ca2+) is perhaps the most versatile signaling molecule in cells. Ca2+ regulates a large number of key events in cells, ranging from gene transcription, motility, and contraction, to energy production and channel gating. To accomplish all these different functions, a multitude of channels, pumps, and transporters are necessary. A group of channels participating in these processes is the transient receptor potential (TRP) family of cation channels. These channels are divided into 29 subfamilies, and are differentially expressed in man, rodents, worms, and flies. One of these subfamilies is the transient receptor potential canonical (TRPC) family of channels. This ion channel family comprises of seven isoforms, labeled TRPC1–7. In man, six functional forms are expressed (TRPC1, TRPC3–7), whereas TRPC2 is a pseudogene; thus, not functionally expressed. In this review, we will describe the importance of the TRPC channels and their interacting molecular partners in the etiology of cancer, particularly in regard to regulating migration and invasion. Keywords: TRPC; ion channels; cancer; thyroid; calcium; migration; invasion; angiogenesis 1. Introduction Increasing evidence during the past decade indicates that different ion channels are expressed in several cancers in humans, and regulate a multitude of cellular processes, including migration, invasion and proliferation [1–3].