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A novel function of Nur77: physical and functional association with protein kinase C.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2006 Sep 29; Vol. 348 (3), pp. 950-6. Date of Electronic Publication: 2006 Aug 04. - Publication Year :
- 2006
-
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 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.
- Subjects :
- Animals
Catalytic Domain physiology
Cell Line
DNA-Binding Proteins metabolism
Humans
Jurkat Cells
Mice
Mice, Transgenic
Nuclear Receptor Subfamily 4, Group A, Member 1
Protein Kinase C antagonists & inhibitors
Protein Kinase C physiology
Receptors, Cytoplasmic and Nuclear metabolism
Receptors, Steroid metabolism
Transcription Factors metabolism
Two-Hybrid System Techniques
DNA-Binding Proteins chemistry
DNA-Binding Proteins physiology
Protein Kinase C metabolism
Receptors, Cytoplasmic and Nuclear chemistry
Receptors, Cytoplasmic and Nuclear physiology
Receptors, Steroid chemistry
Receptors, Steroid physiology
Transcription Factors chemistry
Transcription Factors physiology
Subjects
Details
- Language :
- English
- ISSN :
- 0006-291X
- Volume :
- 348
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 16904076
- Full Text :
- https://doi.org/10.1016/j.bbrc.2006.07.167