Site-specific phosphorylation of IkappaBalpha by a novel ubiquitination-dependent protein kinase activity.

@article{Chen1996SitespecificPO,
  title={Site-specific phosphorylation of IkappaBalpha by a novel ubiquitination-dependent protein kinase activity.},
  author={Zhijian J Chen and Lana Parent and Tom Maniatis},
  journal={Cell},
  year={1996},
  volume={84 6},
  pages={853-62}
}
Signal-induced activation of the transcription factor NF-kappaB requires specific phosphorylation of the inhibitor IkappaBalpha and its subsequent proteolytic degradation. Phosphorylation of serine residues 32 and 36 targets IkappaBalpha to the ubiquitin (Ub)-proteasome pathway. Here we report the identification of a large, multisubunit kinase (molecular mass approximately 700 kDa) that phosphorylates IkappaBalpha at S32 and S36. Remarkably, the activity of this kinase requires the Ub… CONTINUE READING
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