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Publication : Cloning and characterization of a novel human ninein protein that interacts with the glycogen synthase kinase 3beta.

First Author  Hong YR Year  2000
Journal  Biochim Biophys Acta Volume  1492
Issue  2-3 Pages  513-6
PubMed ID  11004522 Mgi Jnum  J:63649
Mgi Id  MGI:1861334 Doi  10.1016/s0167-4781(00)00127-5
Citation  Hong YR, et al. (2000) Cloning and characterization of a novel human ninein protein that interacts with the glycogen synthase kinase 3beta. Biochim Biophys Acta 1492(2-3):513-6
abstractText  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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