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

15 Scopus citations


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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