S-Space College of Medicine/School of Medicine (의과대학/대학원) Dept. of Biochemistry & Molecular Biology (생화학교실) Journal Papers (저널논문_생화학교실)
A novel function of Nur77: physical and functional association with protein kinase C
- Kim, Hyungsoo; Kim, Bu-Yeon; Soh, Jae-Won; Cho, Eun-Jung; Liu, Jun O.; Youn, Hong-Duk
- Issue Date
- Biochem Biophys Res Commun. 2006 Sep 29;348(3):950-6. Epub 2006 Aug 4.
- Animals; Catalytic Domain/physiology; Cell Line; DNA-Binding Proteins/*chemistry/metabolism/*physiology; Humans; Jurkat Cells; Mice; Mice, Transgenic; Protein Kinase C/antagonists & inhibitors/*metabolism/physiology; Receptors, Cytoplasmic and Nuclear/*chemistry/metabolism/*physiology; Receptors, Steroid/*chemistry/metabolism/*physiology; Transcription Factors/*chemistry/metabolism/*physiology; Two-Hybrid System Techniques
- 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 PKCtheta by Nur77. C-terminal LBD of Nur77 is sufficient for inhibiting the phosphorylation of substrate by PKCtheta. Ultimately, inhibition of catalytic activity by Nur77 is deeply associated with repression of PKC-mediated activation of AP-1 and NF-kappaB. 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.
- 0006-291X (Print)
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