An amino-terminal point mutation increases EAAT2 anion currents without affecting glutamate transport rates.

ABSTRACT: Excitatory amino acid transporters (EAATs) are prototypical dual function proteins that function as coupled glutamate/Na⁺/H⁺/K⁺ transporters and as anion-selective channels. Both transport functions are intimately intertwined at the structural level: Secondary active glutamate transport is based on elevator-like movements of the mobile transport domain across the membrane, and the lateral movement of this domain results in anion channel opening. This particular anion channel gating mechanism predicts the existence of mutant transporters with changed anion channel properties, but without alteration in glutamate transport. We here report that the L46P mutation in the human EAAT2 transporter fulfills this prediction. L46 is a pore-forming residue of the EAAT2

SUBMITTER: Kolen B 

PROVIDER: S-EPMC7606670 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature