ArticleJournal of neurochemistry2013
Multiple tyrosine residues at the GABA binding pocket influence surface expression and mediate kinetics of the GABAA receptor.
Article in Journal of neurochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 19 citations in OpenAlex.
- Modular Structure and Polymerization Status of GABAInternational journal of molecular sciences · 2024Article
- αACS chemical neuroscience · 2022Article
- GABAJournal, genetic engineering & biotechnology · 2021Review
- αACS chemical neuroscience · 2021Article
- GABAFrontiers in cellular neuroscience · 2020Article
- γ-Aminobutyric acid (GABA) signalling in plants.Cellular and molecular life sciences : CMLS · 2017Review
- Abnormal subcellular localization of GABAA receptor subunits in schizophrenia brain.Translational psychiatry · 2015Article
- A hydrophobic area of the GABA ρ₁ receptor containing phenylalanine 124 influences both receptor activation and deactivation.Journal of molecular neuroscience : MN · 2015Article
- α1F64 Residue at GABA(A) receptor binding site is involved in gating by influencing the receptor flipping transitions.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The prevalence of aromatic residues in the ligand binding site of the GABA(A) receptor, as with other cys-loop ligand-gated ion channels, is undoubtedly important for the ability of neurotransmitters to bind and trigger channel opening. Here, we have examined three conserved tyrosine residues at the GABA binding pocket (β(2) Tyr97, β(2) Tyr157, and β(2) Tyr205), making mutations to alanine and phenylalanine. We fully characterized the effects each mutation had on receptor function using heterologous expression in HEK-293 cells, which included examining surface expression, kinetics of macroscopic currents, microscopic binding and unbinding rates for an antagonist, and microscopic binding rates for an agonist. The assembly or trafficking of GABA(A) receptors was disrupted when tyrosine mutants were expressed as αβ receptors, but interestingly not when expressed as αβγ receptors. Mutation of each tyrosine accelerated deactivation and slowed GABA binding. This provides strong evidence that these residues influence the binding of GABA. Qualitatively, mutation of each tyrosine has a very similar effect on receptor function; however, mutations at β(2) Tyr157 and β(2) Tyr205 are more detrimental than β(2) Tyr97 mutations, particularly to the GABA binding rate. Overall, the results suggest that interactions involving multiple tyrosine residues are likely during the binding process.
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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.