PuSH - Publikationsserver des Helmholtz Zentrums München

Export: TXT Text RIS Endnote (RIS) BIB BibTeX
Böttger, A.* ; Islam, M.S.* ; Chowdhury, R.* ; Schofield, C.J.* ; Wolf, A.

The oxygenase Jmjd6-a case study in conflicting assignments.

Biochem. J. 468, 191-202 (2015)
Verlagsversion DOI PMC
Open Access Gold
The Jumonji domain-containing protein 6 (Jmjd6) is a member of the superfamily of non-haem iron(II) and 2-oxoglutarate (2OG)-dependent oxygenases; it plays an important developmental role in higher animals. Jmjd6 was initially assigned a role as the phosphatidylserine receptor responsible for engulfment of apoptotic cells but this now seems unlikely. Jmjd6 has been shown to be a nuclear localized protein with a JmjC domain comprising a distorted double-stranded β-helical structure characteristic of the 2OG-dependent oxygenases. Jmjd6 was subsequently assigned a role in catalysing N-methyl-arginine residue demethylation on the N-terminus of the human histones H3 and H4; however, this function is also subject to conflicting reports. Jmjd6 does catalyse 2OG-dependent C-5 hydroxylation of lysine residues in mRNA splicing-regulatory proteins and histones; there is also accumulating evidence that Jmjd6 plays a role in splicing (potentially in an iron- and oxygen-dependent manner) as well as in other processes regulating gene expression, including transcriptional pause release. Moreover, a link with tumour progression has been suggested. In the present review we look at biochemical, structural and cellular work on Jmjd6, highlighting areas of controversy and consensus.
Impact Factor
Scopus SNIP
Web of Science
Times Cited
Scopus
Cited By
Altmetric
4.396
1.203
54
57
Tags
Anmerkungen
Besondere Publikation
Auf Hompepage verbergern

Zusatzinfos bearbeiten
Eigene Tags bearbeiten
Privat
Eigene Anmerkung bearbeiten
Privat
Auf Publikationslisten für
Homepage nicht anzeigen
Als besondere Publikation
markieren
Publikationstyp Artikel: Journalartikel
Dokumenttyp Review
Schlagwörter Alternative Splicing ; Arginine-demethylase ; Epigenetic Regulation ; Fe(ii) And 2-oxoglutarate Dependent Oxygenases ; Hydroxylysine ; Jmjc ; Jmjd6 ; Jumonji ; Lysine-hydroxylase ; Sr-proteins; Hypoxia-inducible Factor; Bromodomain Protein Brd4; Inhibiting-hif Fih; Vegf-receptor 1; Phosphatidylserine Receptor; Apoptotic Cells; 2-oxoglutarate Oxygenases; Lysyl Hydroxylase; Asparaginyl Hydroxylase; P-tefb
Sprache englisch
Veröffentlichungsjahr 2015
HGF-Berichtsjahr 2015
ISSN (print) / ISBN 0264-6021
e-ISSN 1470-8728
Zeitschrift Biochemical Journal / Reviews
Quellenangaben Band: 468, Heft: 2, Seiten: 191-202 Artikelnummer: , Supplement: ,
Verlag Portland Press
Verlagsort London
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Molecular Toxicology and Pharmacology (TOX)
POF Topic(s) 30504 - Mechanisms of Genetic and Environmental Influences on Health and Disease
Forschungsfeld(er) Enabling and Novel Technologies
PSP-Element(e) G-552500-001
PubMed ID 25997831
DOI 10.1042/BJ20150278
WOS ID WOS:000354942800001
Scopus ID 84934967447
Erfassungsdatum 2015-05-24
[➜Korrektur melden]