ArticleThe Journal of physiology2002
The relation between charge movement and transport-associated currents in the rat GABA cotransporter rGAT1.
Article in The Journal of physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 36 citations in OpenAlex.
- Unveiling the crucial role of betaine: modulation of GABA homeostasis via SLC6A1 transporter (GAT1).Cellular and molecular life sciences : CMLS · 2024Article
- A comparative review on the well-studied GAT1 and the understudied BGT-1 in the brain.Frontiers in physiology · 2023Review
- The "www" ofMembranes · 2022Review
- Functional characterization of Atlantic salmon (Salmo salar L.) PepT2 transporters.The Journal of physiology · 2022Article
- Conformational changes represent the rate-limiting step in the transport cycle of maize sucrose transporter1.The Plant cell · 2013Article
- An inverse relationship links temperature and substrate apparent affinity in the ion-coupled cotransporters rGAT1 and KAAT1.International journal of molecular sciences · 2012Article
- Functional and structural determinants of reverse operation in the pH-dependent oligopeptide transporter PepT1.Cellular and molecular life sciences : CMLS · 2011Article
- Residues R282 and D341 act as electrostatic gates in the proton-dependent oligopeptide transporter PepT1.The Journal of physiology · 2011Article
- Sucrose- and H-dependent charge movements associated with the gating of sucrose transporter ZmSUT1.PloS one · 2010Article
- Transient currents in the glycine cotransporter GlyT1 reveal different steps in transport mechanism.Journal of molecular neuroscience : MN · 2010Article
- GABA transporter lysine 448: a key residue for tricyclic antidepressants interaction.Cellular and molecular life sciences : CMLS · 2009Article
- Functional expression of the oligopeptide transporter PepT1 from the sea bass (Dicentrarchus labrax).Pflugers Archiv : European journal of physiology · 2009Article
- Turnover rate of the gamma-aminobutyric acid transporter GAT1.The Journal of membrane biology · 2007Article
- Effect of substrate on the pre-steady-state kinetics of the Na(+)/glucose cotransporter.Biophysical journal · 2007Article
- Role of the conserved glutamine 291 in the rat gamma-aminobutyric acid transporter rGAT-1.Cellular and molecular life sciences : CMLS · 2006Article
- Rapid substrate-induced charge movements of the GABA transporter GAT1.Biophysical journal · 2005Article
- Relations between substrate affinities and charge equilibration rates in the rat GABA cotransporter GAT1.The Journal of physiology · 2005Article
- Novel properties of a mouse gamma-aminobutyric acid transporter (GAT4).The Journal of membrane biology · 2005Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Most cotransporters characteristically display two main kinds of electrical activity: in the absence of organic substrate, transient presteady-state currents (I(pre)) are generated by charge relocation during voltage steps; in the presence of substrate, sustained, transport-associated currents (I(tr)) are recorded. Quantitative comparison of these two currents, in Xenopus oocytes expressing the neural GABA cotransporter rGAT1, revealed several unforeseen consistencies between I(pre) and I(tr), in terms of magnitude and kinetic parameters. The decay rate constant (r) of I(pre) and the quantity of charge displaced to an inner position in the transporter (Q(in)(0)) depended on voltage and ionic conditions. Saturating GABA concentrations, applied under the same conditions, suppressed I(pre) (i.e. Q(in)( infinity ) = 0) and produced a transport-associated current with amplitude I(tr) = Q(in)(0)r. At non-saturating levels of GABA, changes of I(tr) were compensated by corresponding variations in Q(in), such that I(pre) and I(tr) complemented each other, according to the relation: I(tr) = (Q(in)(0) - Q(in)) r. Complementarity of magnitude, superimposable kinetic properties and equal dependence on voltage and [Na(+)](o) point to the uniqueness of the charge carrier for both processes, suggesting that transport and charge migration arise from the same molecular mechanism. The observed experimental relations were correctly predicted by a simple three-state kinetic model, in which GABA binding takes place after charge binding and inward migration have occurred. The model also predicts the observed voltage dependence of the apparent affinity of the transporter for GABA, and suggests a voltage-independent GABA binding rate with a value around 0.64 microM(-1) s(-1).
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