Rapid membrane turnover is the main 'redeployment' route for the immobile fraction of surface-expressed astroglial glutamate transporters that confine excitatory transmission to the synaptic cleft.

Novel evidence on the molecular determinants of the dual function, anion permeation and substrate transport, of excitatory amino acid transporters opens avenues toward illuminating how these transporters regulate synaptic function and contribute to neurological conditions.

Glutamate transporter homologs can efficiently bind and transport both L- and D- enantiomeric substrates with only slight rearrangements in the binding site.

Substrate releasing or inhibitor binding on the intracellular side of a glutamate transporter homologue require movements of the transport domain through the lipid membrane, which undergoes adaptive deformations.

Methodology for the in vitro assembly of multimeric membrane proteins and the utility of the approach for generating heteromeric variants of homo-multimeric proteins is described.

Sodium ions control the rates of both substrate binding and dissociation of an archaeal homologue of glutamate transporters in a manner that minimizes binding intermediates and maximizes transport efficiency.

Crystal structures of an archaeal homologue of mammalian glutamate transporters in apo and ion-only bound outward- and inward-facing states reveal ion-coupled conformational changes supporting mechanisms of coupling, gating, and transport.

Behavioral and functional analyses revealed that UBR-1 deficiency in Caenorhabditis elegans disrupts glutamate signaling and confers ivermectin resistance.

The conformational mechanism of a transporter protein is found to have profound and energetically costly effects on the morphology of the surrounding membrane.

First identification of the molecular determinants driving contact-dependent predation in Myxococcus..