Assembly of Taurine Transporter (Slc6a6) with Na+ -H+ Exchanger Regulatory Factor 1 (Slc9a3r1) Improves GABA Transport Activity by Increasing the Maximum Transport Velocity

Biological & Pharmaceutical Bulletin
Masanori TachikawaKen-Ichi Hosoya

Abstract

Regulating γ-aminobutyric acid (GABA) uptake transport on the plasma membranes is required for its efficient clearance from the brain interstitial fluid. The purpose of this study was to clarify the assembly of taurine transporter (TauT/Slc6a6) and PSD-95/Disc-large/Zo-1 (PDZ) domain of Na+-H+ exchanger regulatory factor 1 (NHERF1) as a regulatory mechanism of TauT-mediated GABA transport activity. In vitro glutathione S-transferase (GST)-pull down assay and immunoblotting with anti-NHERF1 antibody revealed that NHERF1 protein was present in rat brain lysates as the binding protein of the GST-fusion TauT C-terminal protein with the PDZ-binding ETMM motif but not its corresponding deletion mutant lacking the motif. [3H]GABA uptake by TauT-NHERF1-coexpressing oocytes and TauT-singly expressing oocytes exhibited saturable kinetics with Michaelis-Menten constant values of 0.835±0.288 and 0.982±0.569 mM and a maximal transport velocity of 206±37 and 283±28 pmol/(h·oocyte), respectively. These results suggest that the assembly of TauT PDZ-binding motif and NHERF1 increases the maximal transport velocity of GABA rather than changes the affinity.

References

Sep 19, 2003·Neurobiology of Disease·Marcello MeloneFiorenzo Conti
Nov 4, 2004·Molecular Pharmacology·Yukio KatoAkira Tsuji
Oct 21, 2005·Journal of the American Society of Nephrology : JASN·Hiroki MiyazakiHitoshi Endou
Dec 4, 2012·Biochemical and Biophysical Research Communications·Kota SatoMutsumi Inaba

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