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

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

doi:10.3389/fgene.2017.00032

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

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

Research output: Contribution to journal › Literature review › peer-review

Abstract

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 language	English
Article number	1664-8021
Pages (from-to)	1-48
Number of pages	48
Journal	Frontiers in Genetics
Volume	8
Issue number	32
Early online date	27 Feb 2017
DOIs	https://doi.org/10.3389/fgene.2017.00032
Publication status	E-pub ahead of print - 27 Feb 2017

Keywords / Materials (for Non-textual outputs)

JmjC domain
demethylation
hydroxylation
chromatin
PSR
splicing
transcription
pausing

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10.3389/fgene.2017.00032

Jmjd6, a JmjC Dioxygenase with Many Interaction Partners and Pleiotropic Functions
Copyright © 2017 Kwok, O’Shea, Hume and Lengeling. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
Final published version, 3.63 MBLicence: Creative Commons: Attribution (CC-BY)

The role of alternative splicing in regulation of macrophage responses
Lengeling, A. (Principal Investigator)
Biotechnology and Biological Sciences Research Council
1/09/13 → 31/08/16
Project: Research
Innate immunity and endemic diseases in livestock species
Collie, D. (Principal Investigator), Beard, P. (Co-investigator), Bishop, S. (Co-investigator), Bronsvoort, M. (Co-investigator), Burt, D. (Co-investigator), Fitzgerald, R. (Co-investigator), Freeman, T. (Co-investigator), Gally, D. (Co-investigator), Gill, A. (Co-investigator), Glass, E. (Co-investigator), Hocking, P. (Co-investigator), Hope, J. (Co-investigator), Hume, D. (Co-investigator), Kaiser, P. (Co-investigator), Mabbott, N. (Co-investigator), McLachlan, G. (Co-investigator), Morrison, L. (Co-investigator), Stevens, J. (Co-investigator), Stevens, M. (Co-investigator) & Watson, M. (Co-investigator)
Biotechnology and Biological Sciences Research Council
1/04/12 → 31/03/17
Project: Research

Cite this

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

abstract = "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. ",

keywords = "JmjC domain, demethylation, hydroxylation, chromatin, PSR, splicing, transcription, pausing",

author = "Chi Kwok and Marie O'Shea and David Hume and Andreas Lengeling",

year = "2017",

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doi = "10.3389/fgene.2017.00032",

language = "English",

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journal = "Frontiers in Genetics",

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T1 - Jmjd6, a JmjC dioxygenase with many interaction partners and pleiotropic functions

AU - Kwok, Chi

AU - O'Shea, Marie

AU - Hume, David

AU - Lengeling, Andreas

PY - 2017/2/27

Y1 - 2017/2/27

N2 - 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.

AB - 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.

KW - JmjC domain

KW - demethylation

KW - hydroxylation

KW - chromatin

KW - PSR

KW - splicing

KW - transcription

KW - pausing

U2 - 10.3389/fgene.2017.00032

DO - 10.3389/fgene.2017.00032

M3 - Literature review

SN - 1664-8021

VL - 8

SP - 1

EP - 48

JO - Frontiers in Genetics

JF - Frontiers in Genetics

IS - 32

M1 - 1664-8021

ER -

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

Abstract

Keywords / Materials (for Non-textual outputs)

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Projects

The role of alternative splicing in regulation of macrophage responses

Innate immunity and endemic diseases in livestock species

Cite this