ArticleNature neuroscience2012
Positive modulation of a Cys-loop acetylcholine receptor by an auxiliary transmembrane subunit.
Article in Nature neuroscience, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 57 citations in OpenAlex.
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- Caenorhabditis elegans in anthelmintic research - Old model, new perspectives.International journal for parasitology. Drugs and drug resistance · 2020Review
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- Hair cell α9α10 nicotinic acetylcholine receptor functional expression regulated by ligand binding and deafness gene products.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- EAT-18 is an essential auxiliary protein interacting with the non-alpha nAChR subunit EAT-2 to form a functional receptor.PLoS pathogens · 2020Article
- Molecular constituents and localization of the ionotropic GABA receptor complex in vivo.Current opinion in neurobiology · 2019Review
- Pharming for Genes in Neurotransmission: Combining Chemical and Genetic Approaches in Caenorhabditis elegans.ACS chemical neuroscience · 2018Review
- The Claudin-like Protein HPO-30 Is Required to Maintain LAChRs at theThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2018Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Auxiliary subunits regulate the trafficking, localization or gating kinetics of voltage- and ligand-gated ion channels by associating tightly and specifically with pore-forming subunits. However, no auxiliary subunits have been identified for members of the Cys-loop receptor superfamily. Here we identify MOLO-1, a positive regulator of levamisole-sensitive acetylcholine receptors (L-AChRs) at the Caenorhabditis elegans neuromuscular junction. MOLO-1 is a one-pass transmembrane protein that contains a single extracellular globular domain-the TPM domain, found in bacteria, plants and invertebrates, including nonvertebrate chordates. Loss of MOLO-1 impairs locomotion and renders worms resistant to the anthelmintic drug levamisole. In molo-1 mutants, L-AChR-dependent synaptic transmission is reduced by half, while the number and localization of receptors at synapses remain unchanged. In a heterologous expression system, MOLO-1 physically interacts with L-AChRs and directly enhances channel gating without affecting unitary conductance. The identification of MOLO-1 expands the mechanisms for generating functional and pharmacological diversity in the Cys-loop superfamily.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.