scholarly journals DMD‐10 and its Potential Effect on Regulation of the Glutamate Receptor GLR‐1 in C. elegans

2018 ◽  
Vol 32 (S1) ◽  
Author(s):  
Lily Renee Johnsky ◽  
Annette McGehee
Keyword(s):  
Glutamate Receptor ◽  
Potential Effect ◽  
C Elegans

scholarly journals Polymodal Functionality of C. elegans OLL Neurons in Mechanosensation and Thermosensation

2021 ◽  
Author(s):  
Yuedan Fan ◽  
Wenjuan Zou ◽  
Jia Liu ◽  
Umar Al-Sheikh ◽  
Hankui Cheng ◽  
...  
Keyword(s):  
Glutamate Receptor ◽  
Sensory Neurons ◽  
Molecular Mechanisms ◽  
Temperature Sensitive ◽  
Cold Sensation ◽  
Cold Response ◽  
C Elegans ◽  
Sensory Modalities ◽  
A Cell ◽  
Bona Fide

AbstractSensory modalities are important for survival but the molecular mechanisms remain challenging due to the polymodal functionality of sensory neurons. Here, we report the C. elegans outer labial lateral (OLL) sensilla sensory neurons respond to touch and cold. Mechanosensation of OLL neurons resulted in cell-autonomous mechanically-evoked Ca2+ transients and rapidly-adapting mechanoreceptor currents with a very short latency. Mechanotransduction of OLL neurons might be carried by a novel Na+ conductance channel, which is insensitive to amiloride. The bona fide mechano-gated Na+-selective degenerin/epithelial Na+ channels, TRP-4, TMC, and Piezo proteins are not involved in this mechanosensation. Interestingly, OLL neurons also mediated cold but not warm responses in a cell-autonomous manner. We further showed that the cold response of OLL neurons is not mediated by the cold receptor TRPA-1 or the temperature-sensitive glutamate receptor GLR-3. Thus, we propose the polymodal functionality of OLL neurons in mechanosensation and cold sensation.

Mechanosensory signalling in C. elegans mediated by the GLR-1 glutamate receptor

Nature ◽  
1995 ◽  
Vol 378 (6552) ◽  
pp. 78-81 ◽  
Author(s):  
Andres V. Maricq ◽  
Erin Peckol ◽  
Monica Driscoll ◽  
Cornelia I. Bargmann
Keyword(s):  
Glutamate Receptor ◽  
C Elegans

scholarly journals Erratum: Mechanosensory signalling in C. elegans mediated by the GLR-1 glutamate receptor

Nature ◽  
1996 ◽  
Vol 379 (6567) ◽  
pp. 749-749 ◽  
Author(s):  
Andres V. Maricq ◽  
Erin Peckol ◽  
Monica Driscoll ◽  
Cornelia I. Bargmann
Keyword(s):  
Glutamate Receptor ◽  
C Elegans

Xenon Acts by Inhibition of Non–N -methyl-d-aspartate Receptor–mediated Glutamatergic Neurotransmission in Caenorhabditis elegans 

2005 ◽  
Vol 103 (3) ◽  
pp. 508-513 ◽  
Author(s):  
Peter Nagele ◽  
Laura B. Metz ◽  
C Michael Crowder
Keyword(s):  
Nitrous Oxide ◽  
Caenorhabditis Elegans ◽  
Nmda Receptor ◽  
Glutamate Receptor ◽  
Glutamatergic Transmission ◽  
Wild Type ◽  
C Elegans ◽  
Aspartate Receptor ◽  
Nmda Glutamate Receptor ◽  
Response Transformation

Background Electrophysiologic experiments in rodents have found that nitrous oxide and xenon inhibit N-methyl-D-aspartate (NMDA)-type glutamate receptors. These findings led to the hypothesis that xenon and nitrous oxide along with ketamine form a class of anesthetics with the identical mechanism, NMDA receptor antagonism. Here, the authors ask in Caenorhabditis elegans whether xenon, like nitrous oxide, acts by a NMDA receptor-mediated mechanism. Methods Xenon:oxygen mixtures were delivered into sealed chambers until the desired concentration was achieved. The effects of xenon on various behaviors were measured on wild-type and mutant C. elegans strains. Results With an EC50 of 15-20 vol% depending on behavioral endpoint, xenon altered C. elegans locomotion in a manner indistinguishable from that of mutants in glutamatergic transmission. Xenon reduced the frequency and duration of backward locomotion without altering its speed or other behaviors tested. Mutation of glr-1, encoding a non-NMDA glutamate receptor subunit, abolished the behavioral effects of xenon; however, mutation of nmr-1, which encodes the pore-forming subunit of an NMDA glutamate receptor previously shown to be required for nitrous oxide action, did not significantly alter xenon response. Transformation of the glr-1 mutant with the wild-type glr-1 gene partially restored xenon sensitivity, confirming that glr-1 was necessary for the full action of xenon. Conclusions Xenon acts in C. elegans to alter locomotion through a mechanism requiring the non-NMDA glutamate receptor encoded by glr-1. Unlike for the action of nitrous oxide in C. elegans, the NMDA receptor encoded by nmr-1 is not essential for sensitivity to xenon.

scholarly journals The C. elegans Glutamate Receptor Subunit NMR-1 Is Required for Slow NMDA-Activated Currents that Regulate Reversal Frequency during Locomotion

Neuron ◽  
2001 ◽  
Vol 31 (4) ◽  
pp. 617-630 ◽  
Author(s):  
Penelope J. Brockie ◽  
Jerry E. Mellem ◽  
Thomas Hills ◽  
David M. Madsen ◽  
Andres V. Maricq
Keyword(s):  
Glutamate Receptor ◽  
Receptor Subunit ◽  
C Elegans ◽  
Glutamate Receptor Subunit ◽  
Reversal Frequency

Synaptic code for sensory modalities revealed by C. elegans GLR-1 glutamate receptor

Nature ◽  
1995 ◽  
Vol 378 (6552) ◽  
pp. 82-85 ◽  
Author(s):  
Anne C. Hart ◽  
Shannon Sims ◽  
Joshua M. Kaplan
Keyword(s):  
Glutamate Receptor ◽  
C Elegans ◽  
Sensory Modalities

scholarly journals Neuronal Control of Locomotion in C. elegans Is Modified by a Dominant Mutation in the GLR-1 Ionotropic Glutamate Receptor

Neuron ◽  
1999 ◽  
Vol 24 (2) ◽  
pp. 347-361 ◽  
Author(s):  
Yi Zheng ◽  
Penelope J Brockie ◽  
Jerry E Mellem ◽  
David M Madsen ◽  
Andres V Maricq
Keyword(s):  
Glutamate Receptor ◽  
Ionotropic Glutamate Receptor ◽  
Dominant Mutation ◽  
C Elegans ◽  
Neuronal Control

scholarly journals UEV-1 Is an Ubiquitin-Conjugating Enzyme Variant That Regulates Glutamate Receptor Trafficking in C. elegans Neurons

PLoS ONE ◽  
2010 ◽  
Vol 5 (12) ◽  
pp. e14291 ◽  
Author(s):  
Lawrence B. Kramer ◽  
Jaegal Shim ◽  
Michelle L. Previtera ◽  
Nora R. Isack ◽  
Ming-Chih Lee ◽  
...  
Keyword(s):  
Glutamate Receptor ◽  
Receptor Trafficking ◽  
C Elegans ◽  
Glutamate Receptor Trafficking ◽  
Ubiquitin Conjugating Enzyme ◽  
Enzyme Variant ◽  
Conjugating Enzyme
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