Reconstitution of GABA, Glycine and Glutamate Transporters

Neurochem Res. 2022 Jan;47(1):85-110. doi: 10.1007/s11064-021-03331-z. Epub 2021 Apr 27.

Abstract

In contrast to water soluble enzymes which can be purified and studied while in solution, studies of solute carrier (transporter) proteins require both that the protein of interest is situated in a phospholipid membrane and that this membrane forms a closed compartment. An additional challenge to the study of transporter proteins has been that the transport depends on the transmembrane electrochemical gradients. Baruch I. Kanner understood this early on and first developed techniques for studying plasma membrane vesicles. This advanced the field in that the experimenter could control the electrochemical gradients. Kanner, however, did not stop there, but started to solubilize the membranes so that the transporter proteins were taken out of their natural environment. In order to study them, Kanner then had to find a way to reconstitute them (reinsert them into phospholipid membranes). The scope of the present review is both to describe the reconstitution method in full detail as that has never been done, and also to reveal the scientific impact that this method has had. Kanner's later work is not reviewed here although that also deserves a review because it too has had a huge impact.

Keywords: GABA transporter; Glutamate transporter; Glycine transporter; Liposomes; Reconstitution; Scientific history.

Publication types

  • Review

MeSH terms

  • Amino Acid Transport System X-AG*
  • GABA Plasma Membrane Transport Proteins
  • Glutamates
  • Glycine* / metabolism
  • gamma-Aminobutyric Acid / metabolism

Substances

  • Amino Acid Transport System X-AG
  • GABA Plasma Membrane Transport Proteins
  • Glutamates
  • gamma-Aminobutyric Acid
  • Glycine