ArticleCellular and molecular life sciences : CMLS2006
Role of the conserved glutamine 291 in the rat gamma-aminobutyric acid transporter rGAT-1.
Article in Cellular and molecular life sciences : CMLS, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Molecular basis of human GABA transporter 3 inhibition.Nature communications · 2025Article
- A comparative review on the well-studied GAT1 and the understudied BGT-1 in the brain.Frontiers in physiology · 2023Review
- The "www" ofMembranes · 2022Review
- The Lepidopteran KAAT1 and CAATCH1: Orthologs to Understand Structure-Function Relationships in Mammalian SLC6 Transporters.Neurochemical research · 2022Article
- Modeling and Simulation ofComputational and structural biotechnology journal · 2019Article
- Chloride binding site of neurotransmitter sodium symporters.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Functional defects in the external and internal thin gates of the γ-aminobutyric acid (GABA) transporter GAT-1 can compensate each other.The Journal of biological chemistry · 2013Article
- Evolutionary history of the GABA transporter (GAT) group revealed by marine invertebrate GAT-1.PloS one · 2013Article
- Functional consequences of sulfhydryl modification of the γ-aminobutyric acid transporter 1 at a single solvent-exposed cysteine residue.The Journal of membrane biology · 2012Article
- An acidic amino acid transmembrane helix 10 residue conserved in the neurotransmitter:sodium:symporters is essential for the formation of the extracellular gate of the γ-aminobutyric acid (GABA) transporter GAT-1.The Journal of biological chemistry · 2012Article
- Reconstructing a chloride-binding site in a bacterial neurotransmitter transporter homologue.The Journal of biological chemistry · 2011Article
- A glutamine residue conserved in the neurotransmitter:sodium:symporters is essential for the interaction of chloride with the GABA transporter GAT-1.The Journal of biological chemistry · 2011Article
- Assessing the ability of sequence-based methods to provide functional insight within membrane integral proteins: a case study analyzing the neurotransmitter/Na+ symporter family.BMC bioinformatics · 2007Article
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8 authors.
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Abstract
We investigated the role of the Q291 glutamine residue in the functioning of the rat gamma-aminobutyric acid (GABA) transporter GAT-1. Q291 mutants cannot transport GABA or give rise to transient, leak and transport-coupled currents even though they are targeted to the plasma membrane. Coexpression experiments of wild-type and Q291 mutants suggest that GAT-1 is a functional monomer though it requires oligomeric assembly for membrane insertion. We determined the accessibility of Q291 by investigating the impact of impermeant sulfhydryl reagents on cysteine residues engineered in close proximity to Q291. The effect of these reagents indicates that Q291 faces the external aqueous milieu. The introduction of a steric hindrance close to Q291 by means of [2-(trimethylammonium)ethyl] methanethiosulfonate bromide modification of C74A/T290C altered the affinity of the mutant for cations. Taken together, these results suggest that this irreplaceable residue is involved in the interaction with sodium or in maintaining the cation accessibility to the transporter.
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