JMJD8 is a novel endoplasmic reticulum protein with a JmjC domain

Kok Siong Yeo, Ming Cheang Tan, Yat Yuen Lim, Chee Kwee Ea

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Article number15407
JournalScientific Reports
Volume7
Issue number1
DOIs
StatePublished - Dec 1 2017

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Endoplasmic Reticulum
Protein Folding
Proteins
Computational Biology
Fluorescence Microscopy
Histones
Protein Domains

ASJC Scopus subject areas

  • General

Cite this

JMJD8 is a novel endoplasmic reticulum protein with a JmjC domain. / Yeo, Kok Siong; Tan, Ming Cheang; Lim, Yat Yuen; Ea, Chee Kwee.

In: Scientific Reports, Vol. 7, No. 1, 15407, 01.12.2017.

Research output: Contribution to journalArticle

Yeo, Kok Siong ; Tan, Ming Cheang ; Lim, Yat Yuen ; Ea, Chee Kwee. / JMJD8 is a novel endoplasmic reticulum protein with a JmjC domain. In: Scientific Reports. 2017 ; Vol. 7, No. 1.
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