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Cloning and characterization of a novel human ninein protein that interacts with the glycogen synthase kinase 3β

  • Yi Ren Hong
  • , Chang Han Chen
  • , Jing Hon Chang
  • , Shang Kwei Wang
  • , Woei Di Sy
  • , Chen Kung Chou
  • , Shen Long Howng*
  • *Corresponding author for this work
  • Kaohsiung Medical University
  • Veterans General Hospital-Taipei

Research output: Contribution to journalJournal Article peer-review

42 Scopus citations

Abstract

Using human glycogen synthase kinase 3β (GSK-3β) 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-3β 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-3β, implying that it may also be regulated by GSK-3β phosphorylation signaling. Copyright (C) 2000 Elsevier Science B.V.

Original languageEnglish
Pages (from-to)513-516
Number of pages4
JournalBBA - Gene Structure and Expression
Volume1492
Issue number2-3
DOIs
StatePublished - 24 07 2000
Externally publishedYes

Keywords

  • Centrosome
  • Glycogen synthase kinase
  • Ninein

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