AtGAT1, a High Affinity Transporter for γ-Aminobutyric Acid in Arabidopsis thaliana*

By Andreas J. Meyer, S. Eskandari, Silke Grallath, D. Rentsch. Journal of Biological Chemistry, 2006

125 citations recorded by the source corpus.

Functional characterization of Arabidopsis thaliana GAT1 in heterologous expression systems, i.e. Saccharomyces cerevisiae and Xenopus laevis oocytes, revealed that AtGAT1 (At1g08230) codes for an H+-driven, high affinity γ-aminobutyric acid (GABA) transporter. In addition to GABA, other ω-aminofatty acids and butylamine are recognized. In contrast to the most closely related proteins of the proline transporter family, proline and glycine betaine are not transported by AtGAT1. AtGAT1 does not share sequence similarity with any of the non-plant GABA transporters described so far, and analyses of substrate selectivity and kinetic properties showed that AtGAT1-mediated transport is similar but distinct from that of mammalian, bacterial, and S. cerevisiae GABA transporters. Consistent with a role in GABA uptake into cells, transient expression of AtGAT1/green fluorescent protein fusion proteins in tobacco protoplasts revealed localization at the plasma membrane. In planta, AtGAT1 expression was highest in flowers and under conditions of elevated GABA concentrations such as wounding or senescence.

Subfields: Molecular Biology, Plant Science

View Paper: https://www.semanticscholar.org/paper/34b5b7052c6a261e5c948ffbbf6b233cd7f31d04

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Citations in the corpus

Non-protein amino acids: plant, soil and ecosystem interactions (2011, background): “Meyer et al. (2006) discovered AtGAT1 (At1g08230), which codes for a proton-driven, high affinity GABA transporter.”
Extracellular γ-Aminobutyrate Mediates Communication between Plants and Other Organisms1 (2006, background): “It is unknown whether extracellular GABA influences pollen tube growth via a plasma membrane-located uptake system (Meyer et al., 2006) or receptor (Bouché et al., 2003).”