Characterization of the interactions between the glycine transporters GLYT1 and GLYT2 and the SNARE protein syntaxin 1A

FEBS Lett. 2000 Mar 17;470(1):51-4. doi: 10.1016/s0014-5793(00)01297-7.

Abstract

In this study we have examined the effect of the SNARE protein syntaxin 1A on the glycine transporters GLYT1 and GLYT2. Our results demonstrate a functional and physical interaction between both glycine transporters and syntaxin 1A. Co-transfection of syntaxin 1A with GLYT1 or GLYT2 in COS cells resulted in approximately 40% inhibition in glycine transport. This inhibition was reversed by the syntaxin 1A-binding protein, Munc18. Furthermore, immunoprecipitation studies showed a physical interaction between syntaxin 1A and both transporters in COS cells and in rat brain tissue. Finally, we conclude that this physical interaction resulted in a partial removal of the glycine transporters from the plasma membrane as demonstrated by biotinylation studies.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Transport Systems, Neutral*
  • Animals
  • Antigens, Surface / genetics
  • Antigens, Surface / metabolism*
  • COS Cells
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Cell Membrane / metabolism
  • Glycine Plasma Membrane Transport Proteins
  • Membrane Proteins*
  • Nerve Tissue Proteins / genetics
  • Nerve Tissue Proteins / metabolism*
  • Rats
  • Synaptosomal-Associated Protein 25
  • Syntaxin 1

Substances

  • Amino Acid Transport Systems, Neutral
  • Antigens, Surface
  • Carrier Proteins
  • Glycine Plasma Membrane Transport Proteins
  • Membrane Proteins
  • Nerve Tissue Proteins
  • Slc6a5 protein, rat
  • Slc6a9 protein, rat
  • Snap25 protein, rat
  • Stx1a protein, rat
  • Synaptosomal-Associated Protein 25
  • Syntaxin 1