A novel function of Nur77

Physical and functional association with protein kinase C

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

Research output: Contribution to journalArticleResearchpeer-review

14 Citations (Scopus)

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 languageEnglish
Pages (from-to)950-956
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume348
Issue number3
DOIs
StatePublished - 29 Sep 2006

Fingerprint

Physiological Phenomena
Protein Kinase C
Catalyst activity
Molecular interactions
Association reactions
Ligands
Transcription Factor AP-1
Glycine
Phosphorylation
Chemical activation
Substrates

Keywords

  • Activation protein-1
  • Glycine-rich loop
  • Ligand binding domain
  • Nuclear factor-κB
  • Nur77
  • PKC

Cite this

Kim, Hyungsoo ; Kim, Bu Yeon ; Soh, Jae Won ; Cho, Eun Jung ; Liu, Jun O. ; Youn, Hong-Duk. / A novel function of Nur77 : Physical and functional association with protein kinase C. In: Biochemical and Biophysical Research Communications. 2006 ; Vol. 348, No. 3. pp. 950-956.
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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.",
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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.

In: Biochemical and Biophysical Research Communications, Vol. 348, No. 3, 29.09.2006, p. 950-956.

Research output: Contribution to journalArticleResearchpeer-review

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T1 - A novel function of Nur77

T2 - Physical and functional association with protein kinase C

AU - Kim, Hyungsoo

AU - Kim, Bu Yeon

AU - Soh, Jae Won

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AU - Liu, Jun O.

AU - Youn, Hong-Duk

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