@article{3712,
  keywords = {Animals, Drosophila Proteins, Humans, Cell Line, Phosphorylation, Protein Processing, Post-Translational, Drosophila melanogaster, Methylation, Interphase, Histones, Chromatin, Chromatin Assembly and Disassembly, Heterochromatin, Protein Serine-Threonine Kinases},
  author = {Christian Albig and Chao Wang and Geoffrey Dann and Felix Wojcik and Tam{\'a}s Schauer and Silke Krause and Sylvain Maenner and Weili Cai and Yeran Li and Jack Girton and Tom Muir and J{\o}rgen Johansen and Kristen Johansen and Peter Becker and Catherine Regnard},
  title = {JASPer controls interphase histone H3S10 phosphorylation by chromosomal kinase JIL-1 in Drosophila.},
  abstract = { <p>In flies, the chromosomal kinase JIL-1 is responsible for most interphase histone H3S10 phosphorylation and has been proposed to protect active chromatin from acquiring heterochromatic marks, such as dimethylated histone H3K9 (H3K9me2) and HP1. Here, we show that JIL-1{\textquoteright}s targeting to chromatin depends on a PWWP domain-containing protein JASPer (JIL-1 Anchoring and Stabilizing Protein). JASPer-JIL-1 (JJ)-complex is the major form of kinase in vivo and is targeted to active genes and telomeric transposons via binding of the PWWP domain of JASPer to H3K36me3 nucleosomes, to modulate~transcriptional output. JIL-1 and JJ-complex depletion in cycling cells lead to small changes in H3K9me2 distribution at active genes and telomeric transposons. Finally, we identify interactors of the endogenous JJ-complex and propose that JIL-1 not only prevents heterochromatin formation but also coordinates chromatin-based regulation in the transcribed part of the genome.</p> },
  year = {2019},
  journal = {Nat Commun},
  volume = {10},
  pages = {5343},
  month = {2019 Nov 25},
  issn = {2041-1723},
  doi = {10.1038/s41467-019-13174-6},
  language = {eng},
}