Stress-activated protein kinases bind directly to the δ domain of c-Jun in resting cells: Implications for repression of c-Jun function

T. Dai, E. Rubie, C. C. Franklin, A. Kraft, D. A.F. Gillespie, J. Avruch, J. M. Kyriakis, J. R. Woodgett

Research output: Contribution to journalArticlepeer-review

108 Scopus citations

Abstract

The transactivating function of the c-Jun proto-oncogene component of the AP-1 transcription factor is acutely regulated by a wide variety of cellular signals via modulation of phosphorylation of two serines (63 and 73). The viral oncoprotein, v-Jun, while containing homologous serines, is not phosphorylated in cells. A novel family of stress-activated protein kinases (SAPKs), also termed Jun N-terminal domain kinases (JNKs), are responsible for mediating S63/73 phosphorylation in response to a variety of cellular stimuli including tumor necrosis factor-α, heat stress and u.v. light. The p54α1, α2, p54β and p46β SAPKs are shown to bind directly to c-Jun but not to v-Jun, with an absolute requirement for c-Jun amino acids 31-47, a region deleted in v-Jun. Inactive SAPKs tightly bind c-Jun in resting cells and may be a manifestation of the 'δ' inhibitor, a previously described repressor of c-Jun function.

Original languageEnglish (US)
Pages (from-to)849-855
Number of pages7
JournalOncogene
Volume10
Issue number5
StatePublished - 1995

Keywords

  • AP-1
  • Jun
  • Kinase
  • SAPK

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Cancer Research

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