Yeo Kok Siong, Tan Ming Cheang, Lim Yat-Yuen, Ea Chee-Kwee
Institute of Biological Sciences, Faculty of Science, University of Malaya, 50603, Kuala Lumpur, Malaysia.
Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX, 75390-9148, United States.
Sci Rep. 2017 Nov 13;7(1):15407. doi: 10.1038/s41598-017-15676-z.
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.
含Jumonji C（JmjC）结构域的蛋白质已被证明可通过对组蛋白和非组蛋白靶标进行羟基化或去甲基化来调节细胞过程。JMJD8属于仅含JmjC结构域的家族，最近被证明参与血管生成和肿瘤坏死因子诱导的核因子κB信号传导。在这里，我们采用生物信息学分析和免疫荧光显微镜来研究JMJD8的生理特性。我们证明JMJD8定位于内质网腔，并且JMJD8在体内形成二聚体或寡聚体。此外，我们鉴定了已知可调节蛋白质复合物组装和蛋白质折叠的潜在JMJD8相互作用蛋白。综上所述，这项工作表明JMJD8是在内质网腔中发现的首个含JmjC结构域的蛋白质，可能在蛋白质复合物组装和蛋白质折叠中发挥作用。
