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 in vitro and in vivo investigation of modulators of hyperactivated ion channel induced necrosis in C. elegans

2012 ◽  
Vol 26 (S1) ◽  
Author(s):  
Shaunak Kamat ◽  
Laura Bianchi ◽  
Shrutika Yeola ◽  
Monica Driscoll
Keyword(s):  
Ion Channel ◽  
C Elegans

scholarly journals Erratum: Betaine acts on a ligand-gated ion channel in the nervous system of the nematode C. elegans

2014 ◽  
Vol 17 (12) ◽  
pp. 1840-1840
Author(s):  
Aude S Peden ◽  
Patrick Mac ◽  
You-Jun Fei ◽  
Cecilia Castro ◽  
Guoliang Jiang ◽  
...  
Keyword(s):  
Nervous System ◽  
Ion Channel ◽  
C Elegans

scholarly journals Sequence and transmembrane topology of MEC-4, an ion channel subunit required for mechanotransduction in Caenorhabditis elegans.

1996 ◽  
Vol 133 (5) ◽  
pp. 1071-1081 ◽  
Author(s):  
C C Lai ◽  
K Hong ◽  
M Kinnell ◽  
M Chalfie ◽  
M Driscoll
Keyword(s):  
Caenorhabditis Elegans ◽  
Ion Channel ◽  
Critical Role ◽  
Comparative Sequence Analysis ◽  
Mechanical Stimuli ◽  
Transmembrane Topology ◽  
C Elegans ◽  
Carboxy Terminal

The process by which mechanical stimuli are converted into cellular responses is poorly understood, in part because key molecules in this mode of signal transduction, the mechanically gated ion channels, have eluded cloning efforts. The Caenorhabditis elegans mec-4 gene encodes a subunit of a candidate mechanosensitive ion channel that plays a critical role in touch reception. Comparative sequence analysis of C. elegans and Caenorhabditis briggsae mec-4 genes was used to initiate molecular studies that establish MEC-4 as a 768-amino acid protein that includes two hydrophobic domains theoretically capable of spanning a lipid bilayer. Immunoprecipitation of in vitro translated mec-4 protein with domain-specific anti-MEC-4 antibodies and in vivo characterization of a series of mec-4lacZ fusion proteins both support the hypothesis that MEC-4 crosses the membrane twice. The MEC-4 amino- and carboxy-terminal domains are situated in the cytoplasm and a large domain, which includes three Cys-rich regions, is extracellular. Definition of transmembrane topology defines regions that might interact with the extracellular matrix or cytoskeleton to mediate mechanical signaling.

scholarly journals Betaine acts on a ligand-gated ion channel in the nervous system of the nematode C. elegans

2013 ◽  
Vol 16 (12) ◽  
pp. 1794-1801 ◽  
Author(s):  
Aude S Peden ◽  
Patrick Mac ◽  
You-Jun Fei ◽  
Cecilia Castro ◽  
Guoliang Jiang ◽  
...  
Keyword(s):  
Nervous System ◽  
Ion Channel ◽  
C Elegans

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 Neuronally Produced Betaine Acts via a Novel Ligand Gated Ion Channel to Control Behavioural States

2021 ◽  
Author(s):  
Iris Hardege ◽  
Julia Morud ◽  
Jingfang Yu ◽  
Tatiana S Wilson ◽  
Frank Schroeder ◽  
...  
Keyword(s):  
Nervous System ◽  
Ion Channel ◽  
Molecular Mechanisms ◽  
Amino Acid Derivative ◽  
Single Pair ◽  
Complex Behaviour ◽  
Functional Roles ◽  
C Elegans ◽  
Nematode Worm ◽  
Control Complex

Trimethyl glycine, or betaine, is an amino acid derivative found in diverse organisms, from bacteria to plants and animals. It can function as an osmolyte to protect cells against osmotic stress, and building evidence suggests betaine may also play important functional roles in the nervous system. However, despite growing interest in betaine's roles in the nervous system, few molecular mechanisms have been elucidated. Here we identify the expression of betaine synthesis pathway genes in the nervous system of the nematode worm, C. elegans. We show that betaine, produced in a single pair of interneurons, the RIMs, can control complex behavioural states. Moreover, we also identify and characterise a new betaine-gated inhibitory ligand gated ion channel, LGC-41, which is required for betaine related behavioural changes. Intriguingly we observed expression of LGC-41 in punctate structures across several sensory and interneurons, including those synaptically connected to the RIMs. Our data presents a neuronal molecular mechanism for the action of betaine, via a specific receptor, in the control of complex behaviour within the nervous system of C. elegans. This may suggest a much broader role for betaine in the regulation of animal nervous systems than previously recognised.

scholarly journals Insight into DEG/ENaC Channel Gating from Genetics and Structure

Physiology ◽  
2012 ◽  
Vol 27 (5) ◽  
pp. 282-290 ◽  
Author(s):  
Amy L. Eastwood ◽  
Miriam B. Goodman
Keyword(s):  
Ion Channel ◽  
Research Community ◽  
Mechanosensitive Channels ◽  
C Elegans ◽  
Channel Proteins ◽  
New Models ◽  
Ion Channel Proteins ◽  
Pain Receptors ◽  
Insight Into

The founding members of the superfamily of DEG/ENaC ion channel proteins are C. elegans proteins that form mechanosensitive channels in touch and pain receptors. For more than a decade, the research community has used mutagenesis to identify motifs that regulate gating. This review integrates insight derived from unbiased in vivo mutagenesis screens with recent crystal structures to develop new models for activation of mechanically gated DEGs.

scholarly journals IGDB-2, an Ig/FNIII protein, binds the ion channel LGC-34 and controls sensory compartment morphogenesis in C. elegans

2017 ◽  
Vol 430 (1) ◽  
pp. 105-112 ◽  
Author(s):  
Wendy Wang ◽  
Elliot A. Perens ◽  
Grigorios Oikonomou ◽  
Sean W. Wallace ◽  
Yun Lu ◽  
...  
Keyword(s):  
Ion Channel ◽  
C Elegans

Behavioral role of the canonical transient receptor potential (TRP) ion channel, TRP‐1, in C. elegans

2007 ◽  
Vol 21 (5) ◽  
Author(s):  
Ana Y. Estevez ◽  
Brian Aucter ◽  
Charles Dirac ◽  
Thomas Lepesqueur ◽  
Alejandra Marrero ◽  
...  
Keyword(s):  
Ion Channel ◽  
Transient Receptor Potential ◽  
Receptor Potential ◽  
C Elegans ◽  
Canonical Transient Receptor Potential ◽  
Transient Receptor ◽  
Trp Ion Channel

scholarly journals Identification of small-molecule ion channel modulators in C. elegans channelopathy models

2018 ◽  
Vol 9 (1) ◽  
Author(s):  
Qiang Jiang ◽  
Kai Li ◽  
Wen-Jing Lu ◽  
Shuang Li ◽  
Xin Chen ◽  
...  
Keyword(s):  
Ion Channel ◽  
Small Molecule ◽  
C Elegans ◽  
Ion Channel Modulators
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