A novel GTP-binding protein hGBP3 interacts with NIK/HGK.
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.
Luan
Zhidong
Z
Max-Planck Guest Laboratory, Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, 320, Yye-Yang Road, Shanghai 200031, PR China.
Zhang
Yan
Y
Liu
Aihua
A
Man
Yunfang
Y
Cheng
Lu
L
Hu
Gengxi
G
D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites; D015152:Blotting, Northern; D001921:Brain / Q000378:metabolism; D002352:Carrier Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D003001:Cloning, Molecular; D018076:DNA, Complementary; D019204:GTP-Binding Proteins; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins; D008969:Molecular Sequence Data; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*
D002352:Carrier Proteins; D018076:DNA, Complementary; C113264:GBP3 protein, human; D047908:Intracellular Signaling Peptides and Proteins; C117090:MAP4K4 protein, human; D017346:Protein Serine-Threonine Kinases; D019204:GTP-Binding Proteins