ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2009
Mouse RIC-3, an endoplasmic reticulum chaperone, promotes assembly of the alpha7 acetylcholine receptor through a cytoplasmic coiled-coil domain.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 42 citations in OpenAlex.
- RIC-3 Interacts Directly with the 5-HTbioRxiv : the preprint server for biology · 2026Article
- Effects of Swapping 5HT3 and α7 Residues in Chimeric Receptor Proteins on RIC3 and NACHO Chaperone Actions.Molecules (Basel, Switzerland) · 2025Article
- Nicotine-Induced Endoplasmic Reticulum Stress and Airway Smooth Muscle Cell Proliferation Is Mediated by α7nAChR and Chaperones-RIC-3 and TMEM35.American journal of respiratory cell and molecular biology · 2025Article
- Functional expression and properties of the tick α6 homomeric nicotinic acetylcholine receptor inCurrent research in parasitology & vector-borne diseases · 2025Article
- Unraveling the molecular interactions between α7 nicotinic receptor and a RIC3 variant associated with backward speech.Cellular and molecular life sciences : CMLS · 2024Article
- Two residues determine nicotinic acetylcholine receptor requirement for RIC-3.Protein science : a publication of the Protein Society · 2023Article
- Reconstitution of an N-AChR from Brugia malayi, an evolved change in acetylcholine receptor accessory protein requirements in filarial parasites.PLoS pathogens · 2022Article
- Speculation on How RIC-3 and Other Chaperones Facilitate α7 Nicotinic Receptor Folding and Assembly.Molecules (Basel, Switzerland) · 2022Review
- Multidimensional Intersection of Nicotine, Gene Expression, and Behavior.Frontiers in behavioral neuroscience · 2021Article
- RIC3, the cholinergic anti-inflammatory pathway, and neuroinflammation.International immunopharmacology · 2020Article
- Why Does Knocking Out NACHO, But Not RIC3, Completely Block Expression of α7 Nicotinic Receptors in Mouse Brain?Biomolecules · 2020Article
- FKBP8 Enhances Protein Stability of the CLC-1 Chloride Channel at the Plasma Membrane.International journal of molecular sciences · 2018Article
- Proteomic Investigation of Murine Neuronal α7-Nicotinic Acetylcholine Receptor Interacting Proteins.Journal of proteome research · 2018Article
- RIC-3 expression and splicing regulate nAChR functional expression.Molecular brain · 2016Article
- Looking below the surface of nicotinic acetylcholine receptors.Trends in pharmacological sciences · 2015Review
- Functional Chimeras of GLIC Obtained by Adding the Intracellular Domain of Anion- and Cation-Conducting Cys-Loop Receptors.Biochemistry · 2015Article
- Article
- Lynx1 shifts α4β2 nicotinic receptor subunit stoichiometry by affecting assembly in the endoplasmic reticulum.The Journal of biological chemistry · 2014Article
- The duplicated α7 subunits assemble and form functional nicotinic receptors with the full-length α7.The Journal of biological chemistry · 2014Article
- RIC-3 differentially modulates α4β2 and α7 nicotinic receptor assembly, expression, and nicotine-induced receptor upregulation.BMC neuroscience · 2013Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
RIC-3 (resistant to inhibitor of cholinesterase) is a transmembrane protein, found in invertebrates and vertebrates, that modulates the surface expression of a variety of nicotinic acetylcholine receptors (nAChRs) in neurons and other cells. To understand its mechanism of action, we investigated the cellular location, transmembrane topology and cellular mechanism by which RIC-3 facilitates alpha7 assembly and surface expression in cultured mammalian cells. We show that the mouse protein is targeted to the ER by the first 31 aa which act as a cleavable signal sequence. The mature protein is a single-pass type I transmembrane protein whose N terminus resides in the lumen of the ER with the coiled-coil domain in the cytoplasm. RIC-3, which binds both unfolded and folded alpha7 subunits, facilitates the surface expression of receptor principally by promoting the folding and assembly of the alpha7 subunits in the ER into fully polymerized receptor. Functional analysis shows that facilitation of surface expression of alpha7 in mammalian cells is reduced in RIC-3 mutants lacking the signal peptide, the lumenal segment or the coiled-coil domain, but not in mutants lacking the long C-terminal region downstream of the coiled-coil domain. We show that the coiled-coil domain of mRIC-3 is not required for the interaction of mRIC-3 with alpha7, but does mediate a homotypic interaction between molecules of mRIC-3. We suggest that efficient assembly of the homomeric alpha7 nAChR may thus require mRIC-3 self-association through the cytoplasmic coiled-coil domain and suggest a model by which this may occur.
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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.