Jun turnover is controlled through JNK-dependent phosphorylation of the E3 ligase itch

Min Gao, Tord Labuda, Ying Xia, Ewen Gallagher, Deyu Fang, Yun Cai Liu, Michael Karin*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

313 Scopus citations

Abstract

The turnover of Jun proteins, like that of other transcription factors, is regulated through ubiquitin-dependent proteolysis. Usually, such processes are regulated by extracellular stimuli through phosphorylation of the target protein, which allows recognition by F box-containing E3 ubiquitin ligases. In the case of c-Jun and JunB, we found that extracellular stimuli also modulate protein turnover by regulating the activity of an E3 ligase by means of its phosphorylation. Activation of the Jun amino-terminal kinase (JNK) mitogen-activated protein kinase cascade after T cell stimulation accelerated degradation of c-Jun and JunB through phosphorylation-dependent activation of the E3 ligase Itch. This pathway modulates cytokine production by effector T cells.

Original languageEnglish (US)
Pages (from-to)271-275
Number of pages5
JournalScience
Volume306
Issue number5694
DOIs
StatePublished - Oct 8 2004

ASJC Scopus subject areas

  • General

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