A novel GTP-binding protein hGBP3 interacts with NIK/HGK |
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Authors: | Luan Zhidong Zhang Yan Liu Aihua Man Yunfang Cheng Lu Hu Gengxi |
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Institution: | Laboratory of Gene Engineering, Institute for Molecular and Cellular Regulation, Gunma University, 3-39-15 Showa-machi, Maebashi, Gunma, Japan. |
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Abstract: | A novel human guanylate-binding protein (GBP) hGBP3 was identified and characterized. Similar as the two human guanylate-binding proteins hGBP1 and hGBP2, hGBP3 has the first two motifs of the three classical guanylate-binding motifs, GXXXXGKS (T) and DXXG, but lacks the N (T) KXD motif. Escherichia coli-expressed hGBP3 protein specifically binds to guanosine triphosphate (GTP). Using a yeast two-hybrid system, it was revealed that the N-terminal region of hGBP3 binds to the C-terminal regulatory domain of NIK/HGK, a member of the group I GCK (germinal center kinase) family. This interaction was confirmed by in vitro glutathione-S-transferase (GST) pull-down and co-immunoprecipitation assays. |
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Keywords: | Human guanylate-binding protein 3 Nck-interacting kinase/HPK/GCK-like kinase Yeast two-hybrid screening |
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