ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2002
Evidence for a centrally located gate in the pore of a serotonin-gated ion channel.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
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The trial behind it
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Who cites it
34 citing papers in PubMed, 75 citations in OpenAlex.
- Targeted Therapy for Orofacial Pain: A Novel Perspective for Precision Medicine.Journal of personalized medicine · 2023Review
- Structure, Function and Physiology of 5-Hydroxytryptamine Receptors Subtype 3.Sub-cellular biochemistry · 2021Review
- International Union of Basic and Clinical Pharmacology. CX. Classification of Receptors for 5-hydroxytryptamine; Pharmacology and Function.Pharmacological reviews · 2021Review
- Cryo-EM structure of 5-HTNature communications · 2018Article
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- Mutagenic analysis of the intracellular portals of the human 5-HT3A receptor.The Journal of biological chemistry · 2013Article
- A single channel mutation alters agonist efficacy at 5-HT3A and 5-HT3AB receptors.British journal of pharmacology · 2013Article
- Approaching the 5-HT₃ receptor heterogeneity by computational studies of the transmembrane and intracellular domains.Journal of computer-aided molecular design · 2013Article
- 5-HT(3) receptors.The Journal of biological chemistry · 2012Review
- Emerging approaches to probing ion channel structure and function.Neuroscience bulletin · 2012Review
- Mutations that stabilize the open state of the Erwinia chrisanthemi ligand-gated ion channel fail to change the conformation of the pore domain in crystals.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Binding sites for bilobalide, diltiazem, ginkgolide, and picrotoxinin at the 5-HT3 receptor.Molecular pharmacology · 2011Article
- Rings of charge within the extracellular vestibule influence ion permeation of the 5-HT3A receptor.The Journal of biological chemistry · 2011Article
- Structure of the M2 transmembrane segment of GLIC, a prokaryotic Cys loop receptor homologue from Gloeobacter violaceus, probed by substituted cysteine accessibility.The Journal of biological chemistry · 2011Article
- One-microsecond molecular dynamics simulation of channel gating in a nicotinic receptor homologue.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Atomic structure and dynamics of pentameric ligand-gated ion channels: new insight from bacterial homologues.The Journal of physiology · 2010Review
- Pore structure of the Cys-loop ligand-gated ion channels.Neurochemical research · 2009Review
- The 5-HT3 receptor--the relationship between structure and function.Neuropharmacology · 2009Review
- Structural determinants of Ca2+ permeability and conduction in the human 5-hydroxytryptamine type 3A receptor.The Journal of biological chemistry · 2008Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Serotonin-gated ion channels (5-HT3) are members of the ligand-gated channel family, which includes channels that are opened directly by the neurotransmitter acetylcholine, GABA, glycine, or glutamate. Although there is general agreement that the second transmembrane domain (M2) lines the pore, the position of the gate in the M2 is less certain. Here, we used substituted cysteine accessibility method (SCAM) to provide new evidence for a centrally located gate that moves during channel activation. In the closed state, three cysteine substitutions, located on the extracellular side of M2, were modified by methanethiosulfonate (MTS) reagents. In contrast, 13 cysteine substitutions were modified in the open state with MTS reagents. The pattern of inhibition (every three to four substitutions) was consistent with an alpha helical structure for the middle and cytoplasmic segments of the M2 transmembrane domain. Unexpectedly, open-state modification of two amino acids in the center of M2 with three different MTS reagents prevented channels from fully closing in the absence of neurotransmitter. Our results are consistent with a model in which the central region of the M2 transmembrane domain is inaccessible in the closed state and moves during channel activation.
Indexed as
Identifiers
11880493PMC6758895W1760036962What OpenQuestion holds
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.