Research Progress of Long Noncoding RNA in China
2016; 68 (11): 887-893
RNA is essential for all kingdoms of life and exerts important functions beyond transferring genetic information from DNA to protein. With the advent of the state-of-the-art deep sequencing technology, a large portion of noncoding transcripts in eukaryotic genomes has been broadly identified. Among them, long noncoding RNAs (lncRNAs) have been emerged as a new class of RNA molecules that have regulatory potential in a variety of physiological and pathological processes. Here we summarize recent research progresses that have been made by scientists in China on lncRNAs, including their biogenesis, functional implication and the underlying mechanism of action at the current stage. © 2016 IUBMB Life, 68(11):887-893, 2016.
View details for DOI 10.1002/iub.1564
View details for Web of Science ID 000388441400008
View details for PubMedID 27699981
Shedding light on paraspeckle structure by super-resolution microscopy
JOURNAL OF CELL BIOLOGY
2016; 214 (7): 789-791
The nuclear body paraspeckle is built on the lncRNA Neat1 and plays important roles in gene regulation. In this issue, West et al. (2016. J. Cell Biol http://dx.doi.org/10.1083/jcb.201601071) use super-resolution structured illumination microscopy to show that paraspeckles are organized in a core-shell spheroidal structure composed of Neat1 and seven proteins.
View details for DOI 10.1083/jcb.201609008
View details for Web of Science ID 000384707600003
View details for PubMedID 27646270
View details for PubMedCentralID PMC5037413
Protein arginine methyltransferase CARM1 attenuates the paraspeckle-mediated nuclear retention of mRNAs containing IRAlus
GENES & DEVELOPMENT
2015; 29 (6): 630-645
In many cells, mRNAs containing inverted repeated Alu elements (IRAlus) in their 3' untranslated regions (UTRs) are inefficiently exported to the cytoplasm. Such nuclear retention correlates with paraspeckle-associated protein complexes containing p54(nrb). However, nuclear retention of mRNAs containing IRAlus is variable, and how regulation of retention and export is achieved is poorly understood. Here we show one mechanism of such regulation via the arginine methyltransferase CARM1 (coactivator-associated arginine methyltransferase 1). We demonstrate that disruption of CARM1 enhances the nuclear retention of mRNAs containing IRAlus. CARM1 regulates this nuclear retention pathway at two levels: CARM1 methylates the coiled-coil domain of p54(nrb), resulting in reduced binding of p54(nrb) to mRNAs containing IRAlus, and also acts as a transcription regulator to suppress NEAT1 transcription, leading to reduced paraspeckle formation. These actions of CARM1 work together synergistically to regulate the export of transcripts containing IRAlus from paraspeckles under certain cellular stresses, such as poly(I:C) treatment. This work demonstrates how a post-translational modification of an RNA-binding protein affects protein-RNA interaction and also uncovers a mechanism of transcriptional regulation of the long noncoding RNA NEAT1.
View details for DOI 10.1101/gad.257048.114
View details for PubMedID 25792598
SnoVectors for nuclear expression of RNA
NUCLEIC ACIDS RESEARCH
2015; 43 (1)
Many long noncoding RNAs (lncRNAs) are constrained to the nucleus to exert their functions. However, commonly used vectors that were designed to express mRNAs have not been optimized for the study of nuclear RNAs. We reported recently that sno-lncRNAs are not capped or polyadenylated but rather are terminated on each end by snoRNAs and their associated proteins. These RNAs are processed from introns and are strictly confined to the nucleus. Here we have used these features to design expression vectors that can stably express virtually any sequence of interest and constrain its accumulation to the nucleus. Further, these RNAs appear to retain normal nuclear associations and function. SnoVectors should be useful in conditions where nuclear RNA function is studied or where export to the cytoplasm needs to be avoided.
View details for DOI 10.1093/nar/gku1050
View details for Web of Science ID 000350207100005
View details for PubMedID 25378317
View details for PubMedCentralID PMC4288147