Split personality of Aluminum Activated Malate Transporter family proteins: Facilitation of both GABA and malate transport
bioRxiv, ISSN: 2692-8205
2017
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Article Description
Plant aluminum activated malate transporters (ALMTs) are currently classified as anion channels; they are also known to be regulated by diverse signals leading to a range of physiological responses. Gamma-aminobutyric acid (GABA) regulation of anion flux through ALMT proteins requires the presence of a specific amino acid motif in ALMTs that shares similarity with a GABA-binding site in mammalian GABA receptors. Here, we explore why TaALMT1-activation leads to a negative correlation between malate efflux and endogenous GABA concentrations ([GABA]) in both wheat root tips and in heterologous expression systems. We show that TaALMT1 activation reduces [GABA] because TaALMT1 facilitates GABA efflux. TaALMT1-expression also leads to GABA transport into cells, demonstrated by a yeast complementation assay and via GABA uptake into TaALMT1-expressing Xenopus laevis oocytes; this was found to be a general feature of all ALMTs we examined. Mutation of the GABA motif (TaALMT1) prevented both GABA influx and efflux, and uncoupled the relationship between malate efflux and [GABA]. We conclude that ALMTs are likely to act as both GABA and anion transporters in planta. GABA and malate appear to interact with ALMTs in a complex manner regulating each other’s transport, suggestive of a role for ALMTs in communicating metabolic status.
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