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KMID : 0613820120220091159
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Journal of Life Science
2012 Volume.22 No. 9 p.1159 ~ p.1165
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Betaine-γ-aminobutyric Acid Transporter 1 (BGT-1/mGAT2) Interacts with the PDZ Domain of Munc-18 Interacting Proteins (Mints)
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Kim Sang-Jin
Jeong Young-Joo
Choi Sun-Hee
Choi Chun-Yeon
Jun Hee-Jae
Moon Il-Soo
Seog Dae-Hyun
Jang Won-Hee
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Abstract
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The action of neuronally released r-aminobutyric acid (GABA) is terminated by uptake into the neurons by GABA transporters (GATs). The mechanism underlying the stabilization and regulation of GAT2 has not yet been elucidated. We used the yeast two-hybrid system to identify proteins that interact with and, thereby, regulate betaine-r-aminobutyric acid transporter 1 (BGT-1/mGAT2). We found an interaction between BGT-1/mGAT2 and Munc-18-interacting proteins (Mints). The "T-H-L" motif at the C-terminal end of BGT-1/mGAT2 was essential for the interaction with Mint2 in the yeast two-hybrid assay. Mint2 bound to the tail region of BGT-1/mGAT2, but not to other GAT members. When co-expressed in HEK-293T cells, Mint2 was co-immunoprecipitated with BGT-1/mGAT2. In addition, we demonstrated the cellular co-localization of BGT-1/mGAT2 and Mint2 in the cells. These results suggest that Mint2 contributes to the regulation of BGT-1/mGAT2.
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KEYWORD
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Neurotransmitter transporter, r-aminobutyric acid transporter, betaine-r-aminobutyric acid transporter 1 (BGT-1), Munc-18-interacting protein 2 (Mint2), PDZ Domain
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