Abstract
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 language | English (US) |
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Pages (from-to) | 950-956 |
Number of pages | 7 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 348 |
Issue number | 3 |
DOIs | |
State | Published - Sep 29 2006 |
Keywords
- Activation protein-1
- Glycine-rich loop
- Ligand binding domain
- Nuclear factor-κB
- Nur77
- PKC
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology