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KMID : 0613820080180070940
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Journal of Life Science
2008 Volume.18 No. 7 p.940 ~ p.946
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γ-Aminobutyric Acid Transporter 2 Binds to the PDZ Domain of Mammalian Lin-7
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Seog Dae-Hyun
Moon Il-Soo
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Abstract
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Neurotransmitter transporters, which remove neurotransmittesr from the synaptic cleft, are regulated by second messenger such as protein kinases and binding proteins. Neuronal γ-aminobutyric acid transporters (GATs) are responsible for removing the inhibitory neurotransmitter γ-aminobutyric acid (GABA) from the synaptic cleft. γ-aminobutyric acid transporters 2 (GAT2/BGT1) is involved in regulating neurotransmitter recycling, but the mechanism how they are stabilized and regulated by the specific binding protein has not yet been elucidated. Here, we used the yeast two-hybrid system to identify the specific binding protein(s) that interacts with the C-terminal region of GAT2 and found a specific interaction with the mammalian LIN-7b (MALS-2). MALS-2 protein bound to the tail region of GAT2 but not to other GAT members in the yeast two-hybrid assay. The “T-X-L” motif at the C-terminal end of GAT2 is essential for interaction with MALS-2. In addition, this protein showed specific interactions in the glutathione S-transferase (GST) pull-down assay. An antibody to GAT2 specifically co-immunoprecipitated MALS associated with GAT2 from mouse brain extracts. These results suggest that MALS may stabilize GAT2 in brain.
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KEYWORD
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γ-Aminobutyricacid, γ-aminobutyricacidtransporter, PDZDomain, protein-proteininteraction, mammalianLIN-7b
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