A novel function of Nur77: Physical and functional association with protein kinase C

Hyungsoo Kim, Bu Yeon Kim, Jae Won Soh, Eun Jung Cho, Jun O. Liu, Hong Duk Youn

Research output: Contribution to journalArticlepeer-review


Despite the involvement in diverse physiological process and pleiotropic expression profile, the molecular functions of Nur77 are not likely to be fully elucidated. From the effort to find a novel function of Nur77, we detected molecular interaction between Nur77 and PKC. Details of interaction revealed that C-terminal ligand binding domain (LBD) of Nur77 specifically interacted with highly conserved glycine-rich loop of PKC required for catalytic activity. This molecular interaction resulted in inhibition of catalytic activity of PKCθ by Nur77. C-terminal LBD of Nur77 is sufficient for inhibiting the phosphorylation of substrate by PKCθ. Ultimately, inhibition of catalytic activity by Nur77 is deeply associated with repression of PKC-mediated activation of AP-1 and NF-κB. Therefore, these findings demonstrate a novel function of Nur77 as a PKC inhibitor and give insights into molecular mechanisms of various Nur77-mediated physiological phenomena.

Original languageEnglish (US)
Pages (from-to)950-956
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - Sep 29 2006


  • Activation protein-1
  • Glycine-rich loop
  • Ligand binding domain
  • Nuclear factor-κB
  • Nur77
  • PKC

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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