JMJD8 is a novel endoplasmic reticulum protein with a JmjC domain

Jumonji C (JmjC) domain-containing proteins have been shown to regulate cellular processes by hydroxylating or demethylating histone and non-histone targets. JMJD8 belongs to the JmjC domain-only family that was recently shown to be involved in angiogenesis and TNF-induced NF-κB signaling. Here, we...

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Main Authors: Yeo, K.S., Tan, M.C., Lim, Y.Y., Ea, C.K.
Format: Article
Published: Nature Publishing Group 2017
Subjects:
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author Yeo, K.S.
Tan, M.C.
Lim, Y.Y.
Ea, C.K.
author_facet Yeo, K.S.
Tan, M.C.
Lim, Y.Y.
Ea, C.K.
author_sort Yeo, K.S.
collection UM
description Jumonji C (JmjC) domain-containing proteins have been shown to regulate cellular processes by hydroxylating or demethylating histone and non-histone targets. JMJD8 belongs to the JmjC domain-only family that was recently shown to be involved in angiogenesis and TNF-induced NF-κB signaling. Here, we employed bioinformatic analysis and immunofluorescence microscopy to examine the physiological properties of JMJD8. We demonstrated that JMJD8 localizes to the lumen of endoplasmic reticulum and that JMJD8 forms dimers or oligomers in vivo. Furthermore, we identified potential JMJD8-interacting proteins that are known to regulate protein complex assembly and protein folding. Taken together, this work demonstrates that JMJD8 is the first JmjC domain-containing protein found in the lumen of the endoplasmic reticulum that may function in protein complex assembly and protein folding.
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spelling um.eprints-189412018-07-30T08:00:24Z http://eprints.um.edu.my/18941/ JMJD8 is a novel endoplasmic reticulum protein with a JmjC domain Yeo, K.S. Tan, M.C. Lim, Y.Y. Ea, C.K. Q Science (General) QH Natural history Jumonji C (JmjC) domain-containing proteins have been shown to regulate cellular processes by hydroxylating or demethylating histone and non-histone targets. JMJD8 belongs to the JmjC domain-only family that was recently shown to be involved in angiogenesis and TNF-induced NF-κB signaling. Here, we employed bioinformatic analysis and immunofluorescence microscopy to examine the physiological properties of JMJD8. We demonstrated that JMJD8 localizes to the lumen of endoplasmic reticulum and that JMJD8 forms dimers or oligomers in vivo. Furthermore, we identified potential JMJD8-interacting proteins that are known to regulate protein complex assembly and protein folding. Taken together, this work demonstrates that JMJD8 is the first JmjC domain-containing protein found in the lumen of the endoplasmic reticulum that may function in protein complex assembly and protein folding. Nature Publishing Group 2017 Article PeerReviewed Yeo, K.S. and Tan, M.C. and Lim, Y.Y. and Ea, C.K. (2017) JMJD8 is a novel endoplasmic reticulum protein with a JmjC domain. Scientific Reports, 7 (1). p. 15407. ISSN 2045-2322, DOI https://doi.org/10.1038/s41598-017-15676-z <https://doi.org/10.1038/s41598-017-15676-z>. http://dx.doi.org/10.1038/s41598-017-15676-z doi:10.1038/s41598-017-15676-z
spellingShingle Q Science (General)
QH Natural history
Yeo, K.S.
Tan, M.C.
Lim, Y.Y.
Ea, C.K.
JMJD8 is a novel endoplasmic reticulum protein with a JmjC domain
title JMJD8 is a novel endoplasmic reticulum protein with a JmjC domain
title_full JMJD8 is a novel endoplasmic reticulum protein with a JmjC domain
title_fullStr JMJD8 is a novel endoplasmic reticulum protein with a JmjC domain
title_full_unstemmed JMJD8 is a novel endoplasmic reticulum protein with a JmjC domain
title_short JMJD8 is a novel endoplasmic reticulum protein with a JmjC domain
title_sort jmjd8 is a novel endoplasmic reticulum protein with a jmjc domain
topic Q Science (General)
QH Natural history
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