Preparing your results

Our searching services are busy right now. Your search will reload in five seconds.

Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

Deactivation of the kinase IKK by CUEDC2 through recruitment of the phosphatase PP1.

Despite rapid progress in elucidating the molecular mechanisms of activation of the kinase IKK, the processes that regulate IKK deactivation are still unknown. Here we demonstrate that CUE domain-containing 2 (CUEDC2) interacted with IKKalpha and IKKbeta and repressed activation of the transcription factor NF-kappaB by decreasing phosphorylation and activation of IKK. Notably, CUEDC2 also interacted with GADD34, a regulatory subunit of protein phosphatase 1 (PP1). We found that IKK, CUEDC2 and PP1 existed in a complex and that IKK was released from the complex in response to inflammatory stimuli such as tumor necrosis factor. CUEDC2 deactivated IKK by recruiting PP1 to the complex. Therefore, CUEDC2 acts as an adaptor protein to target IKK for dephosphorylation and inactivation by recruiting PP1.

Pubmed ID: 18362886


  • Li HY
  • Liu H
  • Wang CH
  • Zhang JY
  • Man JH
  • Gao YF
  • Zhang PJ
  • Li WH
  • Zhao J
  • Pan X
  • Zhou T
  • Gong WL
  • Li AL
  • Zhang XM


Nature immunology

Publication Data

May 21, 2008

Associated Grants


Mesh Terms

  • Animals
  • Antigens, Differentiation
  • Carrier Proteins
  • Catalytic Domain
  • Cell Cycle Proteins
  • Cells, Cultured
  • Female
  • Humans
  • I-kappa B Kinase
  • Inflammation
  • Interleukin-6
  • Macrophages
  • Membrane Proteins
  • Mice
  • Mice, Inbred C57BL
  • NF-kappa B
  • Phosphorylation
  • Protein Binding
  • Protein Phosphatase 1
  • Repressor Proteins
  • Up-Regulation