Fig. 4.

Biochemical and bioinformatic analysis of the SLC25A12 variant. A. Structural homology model of the C. lupus C-terminal domain of the mitochondrial aspartate/glutamate carrier 1 (AGC1). The amino acid position of Leu349 that is mutated in Pro is shown in the box. B. Sequence alignment of AGC1 from different organisms (upper panel) and other members of the mitochondrial carrier family in Canis lupus familiaris (lower panel). C. Functional characterization of wild-type (WT) and mutated AGC1 form. The uptake rate of (¹⁴C) glutamate or (¹⁴C) aspartate was measured by adding 1 mM of radiolabeled glutamate or aspartate to liposomes reconstituted with purified WT AGC or with the mutant p.L349P and containing 20 mM of glutamate. The transport reaction was terminated after 1 min by adding 20mM pyridoxal 5^′-phosphate and bathophenanthroline. The means and SDs from three independent experiments are shown.