Jmjd6, a JmjC dioxygenase with many interaction partners and pleiotropic functions

Chi Kwok, Marie O'Shea, David Hume, Andreas Lengeling

Research output: Contribution to journalLiterature reviewpeer-review

Abstract / Description of output

Lysyl hydroxylation and arginyl demethylation are posttranslational events that are important for many cellular processes. The jumonji domain containing protein 6 (JMJD6) has been reported to catalyze both lysyl hydroxylation and arginyl demethylation on diverse protein substrates. It also interacts directly with RNA. This review summarizes knowledge of JMJD6 functions that have emerged in the last 15 years and considers how a single Jumonji C (JmjC) domain-containing enzyme can target so many different substrates. New links and synergies between the three main proposed functions of Jmjd6 in histone demethylation, promoter proximal pause release of polymerase II and RNA splicing are discussed. The physiological context of the described molecular functions is considered and recently described novel roles for JMJD6 in cancer and immune biology are reviewed. The increased knowledge of JMJD6 functions has wider implications for our general understanding of the JmjC protein family of which JMJD6 is a member.
Original languageEnglish
Article number1664-8021
Pages (from-to)1-48
Number of pages48
JournalFrontiers in genetics
Issue number32
Early online date27 Feb 2017
Publication statusE-pub ahead of print - 27 Feb 2017

Keywords / Materials (for Non-textual outputs)

  • JmjC domain
  • demethylation
  • hydroxylation
  • chromatin
  • PSR
  • splicing
  • transcription
  • pausing


Dive into the research topics of 'Jmjd6, a JmjC dioxygenase with many interaction partners and pleiotropic functions'. Together they form a unique fingerprint.

Cite this