SGD Paper 
Grishin A, et al. (2006) Identification of gamma-aminobutyric acid receptor-interacting factor 1 (TRAK2) as a trafficking factor for the K+ channel Kir2.1. J Biol Chem 281(40):30104-11
Abstract: To identify proteins that regulate potassium (K+) channel activity and expression, we performed functional screening of mammalian cDNA libraries in yeast that express the mammalian K+ channel Kir2.1. Growth of Kir2.1-expressing yeast in media with low K+ concentration is a function of K+ uptake via Kir2.1 channels. Therefore, the host strain was transformed with a human cDNA library and cDNA clones that rescued growth at low K+ concentration were selected. One of these clones was identical to the protein of unknown function isolated previously as GABA Receptor Interacting Factor (GRIF-1) (Beck, M., Brickley, K., Wilkinson, H. L., Sharma, S., Smith, M., Chazot, P. L., Pollard, S., and Stephenson F. A., (2002), J. Biol. Chem., 277, 30079-30090). GRIF-1 specifically enhanced Kir2.1-dependent growth in yeast and Kir2.1-mediated 86Rb+ uptake in HEK293 cells. Quantitative microscopy and flow cytometry analysis of immunolabeled surface Kir2.1 channel showed that GRIF-1 significantly increased the number of Kir2.1 channels in the plasma membrane of COS and HEK293 cells. Physical interaction of Kir2.1 channel and GRIF-1 was demonstrated by coimmunoprecipitation from HEK293 lysates and yeast two-hybrid assay. In vivo association of Kir2.1 and GRIF-1 was demonstrated by co-immunoprecipitation from brain lysate. Yeast two-hybrid assays showed that an N-terminal region of GRIF-1 interacts with a C-terminal region of Kir2.1. These results indicate that GRIF-1 binds to Kir2.1 and facilitates trafficking of this channel to the cell surface.
| Status: Published | Type: Journal Article | PubMed ID: 16895905 |
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