ArticleMolecular biology of the cell2016
Caenorhabditis elegans paraoxonase-like proteins control the functional expression of DEG/ENaC mechanosensory proteins.
Article in Molecular biology of the cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 30 citations in OpenAlex.
- Evolution of sensory systems underlies the emergence of predatory feeding behaviors in nematodes.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Evolution of sensory systems underlies the emergence of predatory feeding behaviours in nematodes.bioRxiv : the preprint server for biology · 2025Article
- Review
- OSP-1 protects neurons from autophagic cell death induced by acute oxidative stress.Nature communications · 2025Article
- The diverse functions of the DEG/ENaC family: linking genetic and physiological insights.The Journal of physiology · 2023Article
- Complementary biological and computational approaches identify distinct mechanisms of chlorpyrifos versus chlorpyrifos-oxon-induced dopaminergic neurotoxicity.Toxicological sciences : an official journal of the Society of Toxicology · 2023Article
- Paraoxonase 2 is an ER chaperone that regulates the epithelial NaAmerican journal of physiology. Cell physiology · 2022Article
- CPB-3 and CGH-1 localize to motile particles within dendrites in C. elegans PVD sensory neurons.BMC research notes · 2021Article
- Effect of the protease plasmin onmicroPublication biology · 2021Article
- Human Paraoxonase-2 (PON2): Protein Functions and Modulation.Antioxidants (Basel, Switzerland) · 2021Review
- DEG/ENaC Ion Channels in the Function of the Nervous System: From Worm to Man.Advances in experimental medicine and biology · 2021Article
- The WD40-repeat protein WDR-48 promotes the stability of the deubiquitinating enzyme USP-46 by inhibiting its ubiquitination and degradation.The Journal of biological chemistry · 2020Article
- Article
- Paraoxonase 3 functions as a chaperone to decrease functional expression of the epithelial sodium channel.The Journal of biological chemistry · 2020Article
- Molecular Structure of the Hair Cell Mechanoelectrical Transduction Complex.Cold Spring Harbor perspectives in medicine · 2019Review
- Insights into the roles of CMK-1 and OGT-1 in interstimulus interval-dependent habituation inProceedings. Biological sciences · 2018Article
- Functional features of the "finger" domain of the DEG/ENaC channels MEC-4 and UNC-8.American journal of physiology. Cell physiology · 2018Article
- Pore-lining residues of MEC-4 and MEC-10 channel subunits tune theThe Journal of biological chemistry · 2018Article
- Regulation of the epithelial NaThe Journal of biological chemistry · 2017Article
- Ca2+ permeability and Na+ conductance in cellular toxicity caused by hyperactive DEG/ENaC channels.American journal of physiology. Cell physiology · 2016Article
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
Abstract
Caenorhabditis eleganssenses gentle touch via a mechanotransduction channel formed from the DEG/ENaC proteins MEC-4 and MEC-10. An additional protein, the paraoxonase-like protein MEC-6, is essential for transduction, and previous work suggested that MEC-6 was part of the transduction complex. We found that MEC-6 and a similar protein, POML-1, reside primarily in the endoplasmic reticulum and do not colocalize with MEC-4 on the plasma membrane in vivo. As with MEC-6, POML-1 is needed for touch sensitivity, the neurodegeneration caused by themec-4(d)mutation, and the expression and distribution of MEC-4 in vivo. Both proteins are likely needed for the proper folding or assembly of MEC-4 channels in vivo as measured by FRET. MEC-6 detectably increases the rate of MEC-4 accumulation on theXenopusoocyte plasma membrane. These results suggest that MEC-6 and POML-1 interact with MEC-4 to facilitate expression and localization of MEC-4 on the cell surface. Thus MEC-6 and POML-1 act more like chaperones for MEC-4 than channel components.
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