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Related Concept Videos

Cholinergic Receptors: Nicotinic01:15

Cholinergic Receptors: Nicotinic

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Nicotinic receptors are ligand-gated ion channels that are activated by acetylcholine and nicotine. Upon activation, they cause a rapid increase in the permeability of cells to K+, Na+, and Ca2+, followed by depolarization and excitation. They are in the autonomic ganglia, skeletal neuromuscular junction, CNS, and adrenal medulla.
There are two types of nicotinic receptors: neuromuscular (NM/NM/N1) and neuronal (NN/NN/N2). The two families differ based on their location and selectivity to...
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Cholinergic Receptors: Muscarinic01:25

Cholinergic Receptors: Muscarinic

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The pharmacological actions of acetylcholine are elicited via its binding to two families of cholinergic receptors or cholinoceptors, namely, muscarinic and nicotinic receptors. Muscarinic receptors are G protein-coupled receptors and have five subtypes, M1–M5. All mAChR subtypes are activated by acetylcholine and blocked by the antagonist, atropine. 
The subtypes M1, M3, and M5 couple with the Gq subunit and activate the phospholipase C (PLC) activity, mobilizing intracellular Ca2+....
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Cholinergic Neurons: Neurotransmission01:23

Cholinergic Neurons: Neurotransmission

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Cholinergic neurotransmission involves the synthesis and the release of acetylcholine (ACh) in order to transmit nerve impulses across the synapse. The process begins with the synthesis of acetyl CoA, a precursor for ACh, from ATP, acetate, and coenzyme A in the mitochondria. Choline, another vital precursor, is transported inside the neuron through choline transporters, including high-affinity choline transporter CHT1, low-affinity choline transporter CTL1, and lower-affinity choline...
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Direct-Acting Cholinergic Agonists: Chemistry and Structure-Activity Relationship01:22

Direct-Acting Cholinergic Agonists: Chemistry and Structure-Activity Relationship

1.1K
Cholinergic agonists or cholinomimetics mimic the action of acetylcholine to stimulate the parasympathetic nervous system. They are categorized into direct-acting and indirect-acting agents. The direct-acting cholinergic drugs induce the parasympathetic response by directly binding to the muscarinic or nicotine receptors. In comparison, the indirect-acting cholinergic drugs prevent acetylcholine hydrolysis, indirectly contributing to the extended parasympathetic response.
The direct-acting...
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Ligand-Gated Ion Channel Receptor: Gating Mechanism01:30

Ligand-Gated Ion Channel Receptor: Gating Mechanism

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Ligand-gated ion channels are transmembrane proteins that play a vital role in intercellular communication and functions of the nervous system. They allow the influx of ions across the membrane once the neurotransmitter binds, allowing the subsequent transmission of electrical excitation across the neurons. Other ligand-gated ion channels, like the γ-aminobutyric acid (GABA) receptor, permit anions like chloride into the cells on the binding of the GABA molecule. Their entry into the cell...
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Structure of Lipids03:38

Structure of Lipids

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Related Experiment Video

Updated: Aug 6, 2025

Construction of Model Lipid Membranes Incorporating G-protein Coupled Receptors GPCRs
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Construction of Model Lipid Membranes Incorporating G-protein Coupled Receptors GPCRs

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Structure and function meet at the nicotinic acetylcholine receptor-lipid interface.

Francisco J Barrantes1

  • 1Laboratory of Molecular Neurobiology, Biomedical Research Institute, Faculty of Medical Sciences, Pontifical Catholic University of Argentina (UCA) - Argentine Scientific & Technol. Research Council (CONICET), Av. Alicia Moreau de Justo 1600, C1107AAZ Buenos Aires, Argentina.

Pharmacological Research
|March 17, 2023
PubMed
Summary

Nicotinic acetylcholine receptors (nAChRs) interact with membrane lipids, influencing their function. New structural data reveals specific lipid binding sites, offering insights into receptor modulation and potential therapeutic targets.

Keywords:
CholesterolCholesterol consensus recognition domainsLipid-receptor interactionsNicotinic receptorProtein-vicinal lipidsTransmembrane domains

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Probing Nicotinic Acetylcholine Receptor Function in Mouse Brain Slices via Laser Flash Photolysis of Photoactivatable Nicotine

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Local Application of Drugs to Study Nicotinic Acetylcholine Receptor Function in Mouse Brain Slices
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Probing Nicotinic Acetylcholine Receptor Function in Mouse Brain Slices via Laser Flash Photolysis of Photoactivatable Nicotine
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Local Application of Drugs to Study Nicotinic Acetylcholine Receptor Function in Mouse Brain Slices
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Local Application of Drugs to Study Nicotinic Acetylcholine Receptor Function in Mouse Brain Slices

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Area of Science:

  • Neuroscience
  • Structural Biology
  • Biochemistry

Background:

  • Nicotinic acetylcholine receptors (nAChRs) are key pentameric ligand-gated ion channels mediating fast synaptic transmission.
  • nAChRs are transmembrane proteins that interact with their lipid membrane environment, a process known as receptor-lipid crosstalk.
  • Lipids modulate nAChR function, including ligand binding, affinity, and ion channel gating.

Purpose of the Study:

  • To elucidate the structural basis of nAChR-lipid interactions.
  • To identify specific binding sites for phospholipids and cholesterol on nAChRs.
  • To provide mechanistic explanations for lipid modulation of nAChR function.

Main Methods:

  • Cryogenic electron microscopy (cryo-EM) studies of neuronal and electroplax nAChRs.
  • Spectroscopic and affinity labeling studies.
  • Site-directed mutagenesis, single-channel electrophysiology, and molecular dynamics simulations.

Main Results:

  • Cryo-EM revealed specific binding sites for phospholipids and cholesterol on lipid-exposed nAChR regions.
  • Structural data confirms the role of the M4 transmembrane domains as a 'lipid sensor' modulating nAChR activity.
  • Integration of structural, functional, and computational data provides a detailed map of lipid-sensitive loci.

Conclusions:

  • nAChR function is significantly modulated by interactions with its lipid microenvironment.
  • Specific lipid binding sites, particularly involving M4 domains, are crucial for this modulation.
  • Understanding these lipid-sensitive sites opens avenues for therapeutic targeting of nAChRs in disease states.