Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.7.11.26 (GSK)
6,788 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Using human glycogen synthase kinase 3beta (GSK-3beta) as bait in the yeast two-hybrid system, we identified a novel human centrosome associated protein, hNinein. When the full length cDNA of hNinein was sequenced, it showed that an open reading frame encoded a protein consisting of 2047 amino acids with a predicted molecular mass of 239 kDa. The features of this protein include a potential GTP binding site, a large coiled-coil domain together with four leucine zipper domains and a GSK-3beta binding site. Fluorescence microscopy experiment showed that hNinein is localized in the pericentriolar matrix of the centrosome. In addition, hNinein also showed to react with centrosomal autoantibody sera. Our findings suggest that hNinein may be involved in the formation of centrosome matrix and interacts with the GSK-3beta, implying that it may also be regulated by GSK-3beta phosphorylation signaling.
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PMID:Cloning and characterization of a novel human ninein protein that interacts with the glycogen synthase kinase 3beta. 1100 22

The centrosome plays a key role in the formation of the mitotic spindle, cell polarity, and cell locomotion. Previously we identified a novel centrosomal associated protein hNinein using GSK-3beta as a bait in the yeast two-hybrid assay. In this report, the hNinein genome was found to correspond to 29 exons of genomic sequence on human chromosome 14q22. Promoter analysis predicts that hNinein contains a TATA, two CCAAT, and three GC boxes. The promoter exhibits the following potential transcription factor binding sites: Sp1, p300, and AP-1. In addition, an alternatively spliced isoform, encoded a 2041-amino-acid protein of 237,900 Da, which was designated hNinein-Lm (GenBank AF302773). The hNinein-Lm genome was found to correspond to 28 exons (2'-29). Amino acid sequence comparison with hNinein showed that hNinein-Lm exhibited an EF-hand Ca2+ binding domain in the N-terminus which similar to mouse ninein. Northern blot showed that this hNinein-Lm isoform was expressed more than hNinein in tissues examined. Differential RT-PCR combining Southern blotting also showed that hNinein-Lm is much more abundant compared to hNinein. Two forms of ninein may also imply the status of ninein associated with a pair of the centrioles in the centrosome structure. Furthermore, molecular characterization shows that human ninein is oligomerized at the C-terminal end which overlapped with GSK-3beta binding site, suggesting that oligomerization of ninein may be regulated by GSK-3beta phosphorylation.
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PMID:Genomic organization and molecular characterization of the human ninein gene. 1116 63