A peptide encoding the c-Jun δ domain inhibits the activity of a c-Jun amino-terminal protein kinase

Victor Adler, Tino Unlap, Andrew S. Kraft

Research output: Contribution to journalArticlepeer-review

33 Scopus citations

Abstract

Evidence suggests that the c-Jun protooncogene delta (δ) domain (amino acids 31-60) helps regulate the transcriptional activating capacity of c-Jun by modulating the amino-terminal phosphorylation of this protein. By using a peptide encoding the δ domain and purified amino-terminal c-Jun protein kinase, we demonstrate that the δ domain peptide inhibits phosphorylation of the amino terminus of both c-Jun and the related protein JunD. The δ domain peptide inhibited the activation of the c-Jun amino-terminal protein kinase by phorbol esters in permeabilized U937 leukemic cells. Mutation of c-Jun followed by transfection into U937 leukemic cells demonstrated that partial deletions of the δ domain are sufficient to block phosphorylation of the amino terminus of c-Jun. In vitro deletion of the amino-terminal (amino acids 31-44) half of the δ domain inhibited the phosphorylation of c-Jun. However, deletion of the carboxyl-terminal (amino acids 45-60) half only partially inhibited c-Jun phosphorylation. Therefore, these results indicate that the δ domain sequence is an important regulator of c-Jun amino-terminal phosphorylation.

Original languageEnglish (US)
Pages (from-to)11186-11191
Number of pages6
JournalJournal of Biological Chemistry
Volume269
Issue number15
StatePublished - Apr 15 1994
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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