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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

Kim, Hyungsoo; Kim, Bu-Yeon; Soh, Jae-Won; Cho, Eun-Jung; Liu, Jun O.; Youn, Hong-Duk

Issue Date
2006-08-15
Publisher
Elsevier
Citation
Biochem Biophys Res Commun. 2006 Sep 29;348(3):950-6. Epub 2006 Aug 4.
Keywords
AnimalsCatalytic Domain/physiologyCell LineDNA-Binding Proteins/*chemistry/metabolism/*physiologyHumansJurkat CellsMiceMice, TransgenicProtein Kinase C/antagonists & inhibitors/*metabolism/physiologyReceptors, Cytoplasmic and Nuclear/*chemistry/metabolism/*physiologyReceptors, Steroid/*chemistry/metabolism/*physiologyTranscription Factors/*chemistry/metabolism/*physiologyTwo-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
DOI
https://doi.org/10.1016/j.bbrc.2006.07.167
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