Phylogenetics Identifies Two Eumetazoan TRPM Clades and an Eighth TRP Family, TRP Soromelastatin (TRPS)

Abstract Transient receptor potential melastatins (TRPMs) are most well known as cold and menthol sensors, but are in fact broadly critical for life, from ion homeostasis to reproduction. Yet, the evolutionary relationship between TRPM channels remains largely unresolved, particularly with respect to the placement of several highly divergent members. To characterize the evolution of TRPM and like channels, we performed a large-scale phylogenetic analysis of >1,300 TRPM-like sequences from 14 phyla (Annelida, Arthropoda, Brachiopoda, Chordata, Cnidaria, Echinodermata, Hemichordata, Mollusca, Nematoda, Nemertea, Phoronida, Priapulida, Tardigrada, and Xenacoelomorpha), including sequences from a variety of recently sequenced genomes that fill what would otherwise be substantial taxonomic gaps. These findings suggest: 1) the previously recognized TRPM family is in fact two distinct families, including canonical TRPM channels and an eighth major previously undescribed family of animal TRP channel, TRP soromelastatin; 2) two TRPM clades predate the last bilaterian–cnidarian ancestor; and 3) the vertebrate–centric trend of categorizing TRPM channels as 1–8 is inappropriate for most phyla, including other chordates.

Download Full-text

Phylogenetic inference identifies two eumetazoan TRPM clades and an 8th family of TRP channel, TRP soromelastatin (TRPS)

10.1101/860445 ◽

2019 ◽

Author(s):

Nathaniel J. Himmel ◽

Thomas R. Gray ◽

Daniel N. Cox

Keyword(s):

Phylogenetic Analysis ◽

Large Scale ◽

Ion Homeostasis ◽

Evolutionary Relationship ◽

Phylogenetic Inference ◽

Trp Channel ◽

Trpm Channels

AbstractTRP melastatins (TRPMs) are most well-known as cold and menthol sensors, but are in fact broadly critical for life, from ion homeostasis to reproduction. Yet the evolutionary relationship between TRPM channels remains largely unresolved, particularly with respect to the placement of several highly divergent members. To characterize the evolution of TRPM and like channels, we performed a large-scale phylogenetic analysis of >1,300 TRPM-like sequences from 14 phyla (Annelida, Arthropoda, Brachiopoda, Chordata, Cnidaria, Echinodermata, Hemichordata, Mollusca, Nematoda, Nemertea, Phoronida, Priapulida, Tardigrada, and Xenacoelomorpha), including sequences from a variety of recently sequenced genomes that fill what would otherwise be substantial taxonomic gaps. These findings suggest: (1) The previously recognized TRPM family is in fact two distinct families, including canonical TRPM channels, and an 8th major, previously undescribed family of animal TRP channel, TRP soromelastatin (TRPS); (2) two TRPM clades predate the last bilaterian-cnidarian ancestor; and (3) the vertebrate-centric trend of categorizing TRPM channels as 1-8 is inappropriate for most phyla, including other chordates.

Download Full-text

Role of TRP Channels in the Regulation of the Endosomal Pathway

Physiology ◽

10.1152/physiol.00048.2010 ◽

2011 ◽

Vol 26 (1) ◽

pp. 14-22 ◽

Cited By ~ 43

Author(s):

Ken Abe ◽

Rosa Puertollano

Keyword(s):

Membrane Trafficking ◽

Transient Receptor Potential ◽

Trp Channels ◽

Ion Homeostasis ◽

Receptor Potential ◽

Trp Channel ◽

Endosomal Pathway ◽

Transient Receptor

Some members of the transient receptor potential (TRP) channel superfamily have proved to be essential in maintaining adequate ion homeostasis, signaling, and membrane trafficking in the endosomal pathway. The unique properties of the TRP channels confer cells the ability to integrate cytosolic and intraluminal stimuli and allow maintained and regulated release of Ca2+ from endosomes and lysosomes.

Download Full-text

Expression of transient receptor potential (TRP) channel mRNAs in the mouse olfactory bulb

Neuroscience Letters ◽

10.1016/j.neulet.2012.07.013 ◽

2012 ◽

Vol 524 (1) ◽

pp. 49-54 ◽

Cited By ~ 13

Author(s):

Hong-Wei Dong ◽

James C. Davis ◽

ShengYuan Ding ◽

Qiang Nai ◽

Fu-Ming Zhou ◽

...

Keyword(s):

Olfactory Bulb ◽

Transient Receptor Potential ◽

Receptor Potential ◽

Trp Channel ◽

Transient Receptor

Download Full-text

Molecular Bases of Multimodal Regulation of a Fungal Transient Receptor Potential (TRP) Channel

Journal of Biological Chemistry ◽

10.1074/jbc.m112.434795 ◽

2013 ◽

Vol 288 (21) ◽

pp. 15303-15317 ◽

Cited By ~ 11

Author(s):

Makoto Ihara ◽

Shin Hamamoto ◽

Yohei Miyanoiri ◽

Mitsuhiro Takeda ◽

Masatsune Kainosho ◽

...

Keyword(s):

Transient Receptor Potential ◽

Receptor Potential ◽

Trp Channel ◽

Transient Receptor ◽

Molecular Bases

Download Full-text

TRP Channels as Sensors of Aldehyde and Oxidative Stress

Biomolecules ◽

10.3390/biom11101401 ◽

2021 ◽

Vol 11 (10) ◽

pp. 1401

Author(s):

Katharina E. M. Hellenthal ◽

Laura Brabenec ◽

Eric R. Gross ◽

Nana-Maria Wagner

Keyword(s):

Lipid Peroxidation ◽

Transient Receptor Potential ◽

Trp Channels ◽

Treatment Options ◽

Receptor Potential ◽

The Body ◽

Trp Channel ◽

Alcoholic Beverages ◽

Organ Injury ◽

Transient Receptor

The transient receptor potential (TRP) cation channel superfamily comprises more than 50 channels that play crucial roles in physiological processes. TRP channels are responsive to several exogenous and endogenous biomolecules, with aldehydes emerging as a TRP channel trigger contributing to a cellular cascade that can lead to disease pathophysiology. The body is not only exposed to exogenous aldehydes via tobacco products or alcoholic beverages, but also to endogenous aldehydes triggered by lipid peroxidation. In response to lipid peroxidation from inflammation or organ injury, polyunsaturated fatty acids undergo lipid peroxidation to aldehydes, such as 4-hydroxynonenal. Reactive aldehydes activate TRP channels via aldehyde-induced protein adducts, leading to the release of pro-inflammatory mediators driving the pathophysiology caused by cellular injury, including inflammatory pain and organ reperfusion injury. Recent studies have outlined how aldehyde dehydrogenase 2 protects against aldehyde toxicity through the clearance of toxic aldehydes, indicating that targeting the endogenous aldehyde metabolism may represent a novel treatment strategy. An addition approach can involve targeting specific TRP channel regions to limit the triggering of a cellular cascade induced by aldehydes. In this review, we provide a comprehensive summary of aldehydes, TRP channels, and their interactions, as well as their role in pathological conditions and the different therapeutical treatment options.

Download Full-text

Functional characterization of transient receptor potential channels in mouse urothelial cells

AJP Renal Physiology ◽

10.1152/ajprenal.00599.2009 ◽

2010 ◽

Vol 298 (3) ◽

pp. F692-F701 ◽

Cited By ~ 101

Author(s):

Wouter Everaerts ◽

Joris Vriens ◽

Grzegorz Owsianik ◽

Giovanni Appendino ◽

Thomas Voets ◽

...

Keyword(s):

Plasma Membrane ◽

Patch Clamp ◽

Calcium Imaging ◽

Transient Receptor Potential ◽

Receptor Potential ◽

Functional Expression ◽

Sensory Function ◽

Trp Channel ◽

Urothelial Cells ◽

Transient Receptor

The bladder urothelium is currently believed to be a sensory structure, contributing to mechano- and chemosensation in the bladder. Transient receptor potential (TRP) cation channels act as polymodal sensors and may underlie some of the receptive properties of urothelial cells. However, the exact TRP channel expression profile of urothelial cells is unclear. In this study, we have performed a systematic analysis of the molecular and functional expression of various TRP channels in mouse urothelium. Urothelial cells from control and trpv4−/− mice were isolated, cultured (12–48 h), and used for quantitative real-time PCR, immunocytochemistry, calcium imaging, and whole cell patch-clamp experiments. At the mRNA level, TRPV4, TRPV2, and TRPM7 were the most abundantly expressed TRP genes. Immunohistochemistry showed a clear expression of TRPV4 in the plasma membrane, whereas TRPV2 was more prominent in the cytoplasm. TRPM7 was detected in the plasma membrane as well as cytoplasmic vesicles. Calcium imaging and patch-clamp experiments using TRP channel agonists and antagonists provided evidence for the functional expression of TRPV4, TRPV2, and TRPM7 but not of TRPA1, TRPV1, and TRPM8. In conclusion, we have demonstrated functional expression of TRPV4, TRPV2, and TRPM7 in mouse urothelial cells. These channels may contribute to the (mechano)sensory function of the urothelial layer and represent potential targets for the treatment of bladder dysfunction.

Download Full-text

Activation of TRPV1 channels leads to stimulation of NKCC1 cotransport in the lens

AJP Cell Physiology ◽

10.1152/ajpcell.00252.2018 ◽

2018 ◽

Vol 315 (6) ◽

pp. C793-C802 ◽

Cited By ~ 8

Author(s):

Mohammad Shahidullah ◽

Amritlal Mandal ◽

Nicholas A. Delamere

Keyword(s):

Ion Transport ◽

Transient Receptor Potential ◽

Ion Homeostasis ◽

Receptor Potential ◽

Transient Receptor Potential Vanilloid ◽

Signaling Mechanism ◽

Trpv1 Channels ◽

Trpv1 Antagonist ◽

Transient Receptor ◽

Stimulation Of

Lens ion homeostasis is crucial in maintaining water content and, in turn, refractive index and transparency of the multicellular syncytium-like structure. New information is emerging on the regulation of ion transport in the lens by mechanisms that rely on transient receptor potential vanilloid (TRPV) ion channels. We found recently that TRPV1 activation leads to Ca2+/PKC-dependent ERK1/2 signaling. Here, we show that the TRPV1 agonist capsaicin (100 nM) and hyperosmotic solution (350 vs. 300 mosM) each caused an increase of bumetanide-inhibitable Rb uptake by intact porcine lenses and Na-K-2Cl cotransporter 1 (NKCC1) phosphorylation in the lens epithelium. The TRPV1 antagonist A889425 (1 µM) abolished the increases of Rb uptake and NKCC1 phosphorylation in response to hyperosmotic solution. Exposing lenses to hyperosmotic solution in the presence of MEK/ERK inhibitor U0126 (10 µM) or the with-no-lysine kinase (WNK) inhibitor WNK463 (1 µM) also prevented NKCC1 phosphorylation and the Rb uptake responses to hyperosmotic solution. WNK463 did not prevent the increase in ERK1/2 phosphorylation that occurs in response to capsaicin or hyperosmotic solution, suggesting that ERK1/2 activation occurs before WNK activation in the sequence of signaling events. Taken together, the evidence indicates that activation of TRPV1 is a critical early step in a signaling mechanism that responds to a hyperosmotic stimulus, possibly lens shrinkage. By activating ERK1/2 and WNK, TRPV1 activation leads to NKCC1 phosphorylation and stimulation of NKCC1-mediated ion transport.

Download Full-text