scholarly journals Worms find PEZO-1’s function easy to swallow

2021 ◽  
Vol 154 (1) ◽  
Author(s):  
Ben Short
Keyword(s):  
Ion Channel ◽  
C Elegans ◽  
Mechanosensitive Ion Channel ◽  
Pharyngeal Pumping

JGP study finds that the C. elegans orthologue of the PIEZO family is a mechanosensitive ion channel that regulates pharyngeal pumping and food sensation.

scholarly journals C. elegans PEZO-1 is a Mechanosensitive Channel Involved in Food Sensation

2021 ◽  
Author(s):  
Jonathan R.M. Millet ◽  
Luis O Romero ◽  
Jungsoo Lee ◽  
Valeria Vásquez
Keyword(s):  
Fine Tuning ◽  
Mechanosensitive Channel ◽  
C Elegans ◽  
Physiological Processes ◽  
Embryo Cultures ◽  
Mechanosensitive Ion Channel ◽  
Food Content ◽  
Pharyngeal Pumping ◽  
Contraction And Relaxation ◽  
Pharyngeal Function

PIEZO channels are force sensors essential for physiological processes including baroreception and proprioception. The Caenorhabditis elegans genome encodes an ortholog gene of the Piezo family, pezo-1, expressed in several tissues including the pharynx. This myogenic pump is an essential component of the C. elegans alimentary canal whose contraction and relaxation are modulated by mechanical stimulation elicited by food content. Whether pezo-1 encodes a mechanosensitive channel and contributes to pharyngeal function remains unknown. Here, we leverage genome editing, genetics, microfluidics, and electropharyngeogram recordings to establish that pezo-1 is expressed in the pharynx, including a proprioceptive-like neuron, and regulates pharyngeal function. Knockout (KO) and gain-of-function (GOF) mutants reveal that pezo-1 is involved in fine-tuning pharyngeal pumping frequency, sensing osmolarity, and food quality. Using pressure-clamp experiments in primary C. elegans embryo cultures, we determine that pezo-1 KO cells do not display mechanosensitive currents, whereas cells expressing wild-type or GOF PEZO-1 exhibit mechanosensitivity. Moreover, infecting the Spodoptera frugiperda cell line with a baculovirus containing the pezo-1 isoform G (among the longest isoforms) demonstrates that pezo-1 encodes a mechanosensitive channel. Our findings reveal that pezo-1 is a mechanosensitive ion channel that regulates food sensation in worms.

scholarly journals C. elegans PEZO-1 is a mechanosensitive ion channel involved in food sensation

2021 ◽  
Vol 154 (1) ◽  
Author(s):  
Jonathan R.M. Millet ◽  
Luis O. Romero ◽  
Jungsoo Lee ◽  
Briar Bell ◽  
Valeria Vásquez
Keyword(s):  
Ion Channel ◽  
Fine Tuning ◽  
C Elegans ◽  
Physiological Processes ◽  
Embryo Cultures ◽  
Mechanosensitive Ion Channel ◽  
Food Content ◽  
Food Mechanical Properties ◽  
Contraction And Relaxation ◽  
Pharyngeal Function

PIEZO channels are force sensors essential for physiological processes, including baroreception and proprioception. The Caenorhabditis elegans genome encodes an orthologue gene of the Piezo family, pezo-1, which is expressed in several tissues, including the pharynx. This myogenic pump is an essential component of the C. elegans alimentary canal, whose contraction and relaxation are modulated by mechanical stimulation elicited by food content. Whether pezo-1 encodes a mechanosensitive ion channel and contributes to pharyngeal function remains unknown. Here, we leverage genome editing, genetics, microfluidics, and electropharyngeogram recording to establish that pezo-1 is expressed in the pharynx, including in a proprioceptive-like neuron, and regulates pharyngeal function. Knockout (KO) and gain-of-function (GOF) mutants reveal that pezo-1 is involved in fine-tuning pharyngeal pumping frequency, as well as sensing osmolarity and food mechanical properties. Using pressure-clamp experiments in primary C. elegans embryo cultures, we determine that pezo-1 KO cells do not display mechanosensitive currents, whereas cells expressing wild-type or GOF PEZO-1 exhibit mechanosensitivity. Moreover, infecting the Spodoptera frugiperda cell line with a baculovirus containing the G-isoform of pezo-1 (among the longest isoforms) demonstrates that pezo-1 encodes a mechanosensitive channel. Our findings reveal that pezo-1 is a mechanosensitive ion channel that regulates food sensation in worms.

scholarly journals Chondroprotection by urocortin involves blockade of the mechanosensitive ion channel Piezo1

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
K. M. Lawrence ◽  
R. C. Jones ◽  
T. R. Jackson ◽  
R. L. Baylie ◽  
B. Abbott ◽  
...  
Keyword(s):  
Ion Channel ◽  
Mechanosensitive Ion Channel

scholarly journals Functional Characterization of the Adenylyl Cyclase Genesgs-1by Analysis of a Mutational Spectrum inCaenorhabditis elegans

Genetics ◽  
2002 ◽  
Vol 161 (1) ◽  
pp. 133-142 ◽  
Author(s):  
Celine Moorman ◽  
Ronald H A Plasterk
Keyword(s):  
Life Span ◽  
Adenylyl Cyclase ◽  
Neuronal Degeneration ◽  
Functional Characterization ◽  
Adenylyl Cyclases ◽  
Loss Of Function ◽  
C Elegans ◽  
Larval Stages ◽  
Pharyngeal Pumping

AbstractThe sgs-1 (suppressor of activated Gαs) gene encodes one of the four adenylyl cyclases in the nematode C. elegans and is most similar to mammalian adenylyl cyclase type IX. We isolated a complete loss-of-function mutation in sgs-1 and found it to result in animals with retarded development that arrest in variable larval stages. sgs-1 mutant animals exhibit lethargic movement and pharyngeal pumping and (while not reaching adulthood) have a mean life span that is >50% extended compared to wild type. An extensive set of reduction-of-function mutations in sgs-1 was isolated in a screen for suppressors of a neuronal degeneration phenotype induced by the expression of a constitutively active version of the heterotrimeric Gαs subunit of C. elegans. Although most of these mutations change conserved residues within the catalytic domains of sgs-1, mutations in the less-conserved transmembrane domains are also found. The sgs-1 reduction-of-function mutants are viable and have reduced locomotion rates, but do not show defects in pharyngeal pumping or life span.

scholarly journals Estimation of the pore size of the large-conductance mechanosensitive ion channel of Escherichia coli

1997 ◽  
Vol 73 (4) ◽  
pp. 1925-1931 ◽  
Author(s):  
C.C. Cruickshank ◽  
R.F. Minchin ◽  
A.C. Le Dain ◽  
B. Martinac
Keyword(s):  
Escherichia Coli ◽  
Ion Channel ◽  
Pore Size ◽  
Mechanosensitive Ion Channel

Neuropeptide signalling shapes feeding and reproductive behaviours in male C. elegans

2021 ◽  
Author(s):  
Matthew J Gadenne ◽  
Iris Hardege ◽  
Djordji Suleski ◽  
Paris Jaggers ◽  
Isabel Beets ◽  
...  
Keyword(s):  
Synaptic Connectivity ◽  
Male Mating ◽  
Sexually Dimorphic ◽  
C Elegans ◽  
Mating Efficiency ◽  
Sexually Dimorphic Expression ◽  
Pharyngeal Pumping ◽  
Insight Into ◽  
Feeding Behaviours ◽  
Dimorphic Expression

Sexual dimorphism occurs where different sexes of the same species display differences in characteristics not limited to reproduction. For the nematode Caenorhabditis elegans, in which the complete neuroanatomy has been solved for both hermaphrodites and males, sexually dimorphic features have been observed both in terms of the number of neurons and in synaptic connectivity. In addition, male behaviours, such as food-leaving to prioritise searching for mates, have been attributed to neuropeptides released from sex-shared or sex-specific neurons. In this study, we show that the lury-1 neuropeptide gene shows a sexually dimorphic expression pattern; being expressed in pharyngeal neurons in both sexes but displaying additional expression in tail neurons only in the male. We also show that lury-1 mutant animals show sex differences in feeding behaviours, with pharyngeal pumping elevated in hermaphrodites but reduced in males. LURY-1 also modulates male mating efficiency, influencing motor events during contact with a hermaphrodite. Our findings indicate sex-specific roles of this peptide in feeding and reproduction in C. elegans, providing further insight into neuromodulatory control of sexually dimorphic behaviours.

scholarly journals Simulations of Subunit Interactions in the C. Elegans GluCl Ligand-Gated Ion Channel

2012 ◽  
Vol 102 (3) ◽  
pp. 472a
Author(s):  
Ozge Yoluk ◽  
Samuel Murail ◽  
Erik Lindahl
Keyword(s):  
Ion Channel ◽  
Subunit Interactions ◽  
C Elegans

scholarly journals TACAN is an essential component of the mechanosensitive ion channel responsible for pain sensing

2018 ◽  
Author(s):  
L. Beaulieu-Laroche ◽  
M. Christin ◽  
AM Donoghue ◽  
F. Agosti ◽  
N. Yousefpour ◽  
...  
Keyword(s):  
Ion Channels ◽  
Heterologous Expression ◽  
Ion Channel ◽  
Behavioral Responses ◽  
Mechanical Stimuli ◽  
Thermal Pain ◽  
Fundamental Process ◽  
Mechanosensitive Ion Channel ◽  
Pain Stimuli ◽  
Essential Subunit

SummaryMechanotransduction, the conversion of mechanical stimuli into electrical signals, is a fundamental process underlying several physiological functions such as touch and pain sensing, hearing and proprioception. This process is carried out by specialized mechanosensitive ion channels whose identities have been discovered for most functions except pain sensing. Here we report the identification of TACAN (Tmem120A), an essential subunit of the mechanosensitive ion channel responsible for sensing mechanical pain. TACAN is expressed in a subset of nociceptors, and its heterologous expression increases mechanically-evoked currents in cell lines. Purification and reconstitution of TACAN in synthetic lipids generates a functional ion channel. Finally, knocking down TACAN decreases the mechanosensitivity of nociceptors and reduces behavioral responses to mechanical but not to thermal pain stimuli, without affecting the sensitivity to touch stimuli. We propose that TACAN is a pore-forming subunit of the mechanosensitive ion channel responsible for sensing mechanical pain.

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