Abstract
The surreptitious discoveries of the protease activities on arginine-methylated targets of a subfamily of Jumonji domain-containing family including JMJD5, JMJD6, and JMJD7 pose several questions regarding their authenticity, function, purpose, and relations with others. At the same time, despite several decades of efforts and massive accumulating data regarding the roles of the arginine methyltransferase family (PRMTs), the exact function of this protein family still remains a mystery, though it seems to play critical roles in transcription regulation, including activation and inactivation of a large group of genes, as well as other biological activities. In this review, we aim to elucidate that the function of JMJD5/6/7 and PRMTs are likely coupled. Besides roles in the regulation of the biogenesis of membrane-less organelles in cells, they are major players in regulating stimulating transcription factors to control the activities of RNA Polymerase II in higher eukaryotes, especially in the animal kingdom. Furthermore, we propose that arginine methylation by PRMTs could be a ubiquitous action marked for destruction after missions by a subfamily of the Jumonji protein family.
Highlights
We surreptitiously discovered that JMJD5 and JMJD7 could cleave at arginine-methylated sites as endopeptidases and continue to act as amino exopeptidases to trim histone tails [23,24]
An early report showed that JMJD7 and Pogo transposable element with ZNF domain (POGZ) work together to regulate the differentiation of Osteoclast, while JMJD7 was found to occupy the promoter regions of several genes associated with the Osteoclast differentiation [156], suggesting that JMJD7 is recruited to the promoter regions of these genes and possibly required for activation of these genes
Based on the detailed analysis presented in this study of the novel protease activities of JMJD5/6/7 and ubiquitous activities of PRMTs, we speculate that these two enzyme systems may build up a novel protein destruction pathway similar to that of ubiquitous pathways but responsible for more specific regulations by participating in the regulation of individual pathways
Summary
Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations. The exact function of arginine methylation on proteins is still controversial; accumulating data about its roles within a large number of RNA-binding proteins with intrinsic disorder regions (IDRs) or low complexity domains (LCDs) showed that it plays critical roles in the phase separation of these proteins and closely relates to neurodegenerative diseases, cancers, and other diseases [7] Most of these IDR-containing proteins are responsible for the formation of a large number of membrane-less organelles (MLOs) including the nucleus, nuclear speckles, nuclear stress bodies, histone locus body, Cajal body, PML nuclear body, paraspeckles, perinucleolar compartment, stress granules, P-bodies, germ cell granules/nuage, neuronal granules, etc.
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