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, Andrew Kraft, D. A F Gillespie, J. Avruch, J. M. Kyriakis, J. R. Woodgett

Research output: Contribution to journalArticle

107 Citations (Scopus)

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
Externally publishedYes

Fingerprint

Heat-Shock Proteins
Protein Kinases
Serine
Phosphorylation
jun Genes
Oncogene Proteins
Transcription Factor AP-1
Phosphotransferases
Tumor Necrosis Factor-alpha
Hot Temperature
Light
Amino Acids

Keywords

  • AP-1
  • Jun
  • Kinase
  • SAPK

ASJC Scopus subject areas

  • Cancer Research
  • Genetics
  • Molecular Biology

Cite this

Dai, T., Rubie, E., Franklin, C. C., Kraft, A., Gillespie, D. A. F., Avruch, J., ... Woodgett, J. R. (1995). Stress-activated protein kinases bind directly to the δ domain of c-Jun in resting cells: Implications for repression of c-Jun function. Oncogene, 10(5), 849-855.

Stress-activated protein kinases bind directly to the δ domain of c-Jun in resting cells : Implications for repression of c-Jun function. / Dai, T.; Rubie, E.; Franklin, C. C.; Kraft, Andrew; Gillespie, D. A F; Avruch, J.; Kyriakis, J. M.; Woodgett, J. R.

In: Oncogene, Vol. 10, No. 5, 1995, p. 849-855.

Research output: Contribution to journalArticle

Dai, T, Rubie, E, Franklin, CC, Kraft, A, Gillespie, DAF, Avruch, J, Kyriakis, JM & Woodgett, JR 1995, 'Stress-activated protein kinases bind directly to the δ domain of c-Jun in resting cells: Implications for repression of c-Jun function', Oncogene, vol. 10, no. 5, pp. 849-855.
Dai, T. ; Rubie, E. ; Franklin, C. C. ; Kraft, Andrew ; Gillespie, D. A F ; Avruch, J. ; Kyriakis, J. M. ; Woodgett, J. R. / Stress-activated protein kinases bind directly to the δ domain of c-Jun in resting cells : Implications for repression of c-Jun function. In: Oncogene. 1995 ; Vol. 10, No. 5. pp. 849-855.
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