Publications
Detailed Information
A novel function of Nur77: physical and functional association with protein kinase C
Cited 16 time in
Web of Science
Cited 16 time in Scopus
- Authors
- Issue Date
- 2006-08-15
- Publisher
- Elsevier
- Citation
- Biochem Biophys Res Commun. 2006 Sep 29;348(3):950-6. Epub 2006 Aug 4.
- Keywords
- 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
- 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.
- ISSN
- 0006-291X (Print)
- Language
- English
- URI
- http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16904076
https://hdl.handle.net/10371/22934
- Files in This Item:
- There are no files associated with this item.
Item View & Download Count
Items in S-Space are protected by copyright, with all rights reserved, unless otherwise indicated.