title: Acetylation regulates Jun protein turnover in Drosophila.
abstract: C-Jun is a major transcription factor belonging to the activating protein 1 (AP-1) family. Phosphorylation has been shown to be critical for c-Jun activation and stability. Here, we report that Jra, the Drosophila Jun protein, is acetylated in vivo. We demonstrate that the acetylation of Jra leads to its rapid degradation in response to osmotic stress. Intriguingly, we also found that Jra phosphorylation antagonized its acetylation, indicating the opposite roles of acetylation and phosphorylation in Jra degradation process under osmotic stress. Our results provide new insights into how c-Jun proteins are precisely regulated by the interplay of different posttranslational modifications.
authors.affiliation: Stowers Institute for Medical Research, 1000 E. 50th Street, Kansas City, MO 64110, USA.
authors.forename: Daoyong
authors.initials: D
authors.lastname: Zhang
authors.forename: Tamaki
authors.initials: T
authors.lastname: Suganuma
authors.forename: Jerry L
authors.initials: JL
authors.lastname: Workman
mesh_terms: D000107:Acetylation; D000595:Amino Acid Sequence; D000818:Animals; D004330:Drosophila / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D010766:Phosphorylation; D016755:Proto-Oncogene Proteins c-jun / Q000737:chemistry / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D054875:Ubiquitination
chemical_list: D016755:Proto-Oncogene Proteins c-jun
keywords: AP-1; Acetylation; Degradation; HAT; HDAC; Jun; NAM; Phosphorylation; TSA; activating protein 1; histone acetyl transferase; histone deacetylase; nicotinamide; trichostatin A