Abstract
Lysyl hydroxylation and arginyl demethylation are post-translational 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.
Highlights
The jumonji domain-containing protein 6 (Jmjd6) is a member of the large family of Jumonji C (JmjC) domain-containing metalloenzymes
In contrast to other members of the JmjC protein family, Jmjd6 has no other accessory domains such as plant homeodomain (PHD) zinc finger domains, AT-rich interacting domains, other types of zinc finger domains or TUDOR domains that control for example substrate specificities of larger histone KDMs (Kooistra and Helin, 2012)
It is very likely that Jmjd6 interacting proteins or co-factors are needed to make Jmjd6 reactions in vitro more efficient for mass spectrometry (MS) based quantification of reaction products
Summary
The jumonji domain-containing protein 6 (Jmjd6) is a member of the large family of JmjC domain-containing metalloenzymes. Jmjd6 contributes to the regulation of histone demethylation, transcriptional polymerase II promoter pause release and mRNA splicing (Chang et al, 2007; Webby et al, 2009; Liu et al, 2013) through its ability to catalyze two types of reactions, lysyl hydroxylation and N-methyl argininyl demethylation. Some studies have provided indirect evidence that Jmjd6 catalyzes demethylation of arginine residues in target proteins using methylation-specific antibodies in immunoprecipitation and/or western blot analyses (Supplementary Table S1).
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
