Phosphorylation-dependent targeting of c-Jun ubiquitination by Jun N-kinase

Serge Y. Fuchs, Lisa Dolan, Roger J. Davis, Ze'ev Ronai

Research output: Contribution to journalArticlepeer-review

171 Scopus citations


Ubiquitination of key cellular regulatory proteins marks them for efficient degradation via the proteasome pathway. The δ domain of c-jun is essential for its ubiquitination and also for the activating phosphorylation of neighboring serines by the stress activated jun-N-terminal kinases (JNK). Using an in vitro model system we demonstrate that JNK is among the hydrophobic binding proteins that target c-jun for efficient ubiquitination. Immunodepletion of JNK markedly inhibits c-jun ubiquitination. Conversely, c-jun ubiquitination is increased by adding purified JNK2 or extracts prepared from cells transfected with JNK2. Although c-jun ubiquitination is enhanced by JNK, the phosphorylation of c-jun on Ser73 by JNK protects c-jun from ubiquitination and prolongs its half-life. The dual activity of JNK in targeting c-jun for ubiquitination protecting c-jun from entering this phosphorylation points to the role of JNK in the control of c-jun stability in cells exposed to environmental stress or inflammatory cytokines.

Original languageEnglish
Pages (from-to)1531-1535
Number of pages5
Issue number7
StatePublished - 1996
Externally publishedYes


  • Phosphorylation
  • Ubiquitination
  • c-jun
  • c-jun N-kinase


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