The polyserine domain of the lysyl-5 hydroxylase Jmjd6 mediates subnuclear localization.

@article{Wolf2013ThePD,
  title={The polyserine domain of the lysyl-5 hydroxylase Jmjd6 mediates subnuclear localization.},
  author={Alexander Wolf and Monica Mantri and Astrid Heim and Udo M{\"u}ller and Erika Fichter and Mukram Mohamed Mackeen and Lothar Schermelleh and Gregory Dadie and Heinrich Leonhardt and Catherine V{\'e}nien-Bryan and Benedikt M. Kessler and Christopher J. Schofield and A. Zbinden P. P. Bosshard E. C. B{\"o}ttger},
  journal={The Biochemical journal},
  year={2013},
  volume={453 3},
  pages={357-70}
}
Jmjd6 (jumonji-domain-containing protein 6) is an Fe(II)- and 2OG (2-oxoglutarate)-dependent oxygenase that catalyses hydroxylation of lysine residues in proteins involved in pre-mRNA splicing. Jmjd6 plays an essential role in vertebrate embryonic development and has been shown to modulate alternative splicing in response to hypoxic stress. In the present study we show that an alternatively spliced version of Jmjd6 lacking the polyS (polyserine) domain localizes to the nucleolus, predominantly… CONTINUE READING
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357–370 (Printed in Great Britain) doi:10.1042/BJ20130529 SUPPLEMENTARY ONLINE DATA The polyserine domain of the lysyl-5 hydroxylase Jmjd6 mediates subnuclear localization Alexander WOLF*1

  • J. Biochem
  • Monica MANTRI†1,
  • 2013

Self-hydroxylation of the splicing factor lysyl hydroxylase, JMJD6

  • M. Mantri, C. J. Webby, +7 authors A. Wolf
  • Med. Chem. Commum
  • 2012

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