The unfolded protein response sensor/transducer IRE1-mediated splicing of XBP1 mRNA encoding its active downstream transcription factor to maintain the homeostasis of the endoplasmic reticulum is sufficient for growth and development of medaka fish.

The need for efficient pre-RNA splicing during early embryonic development of Drosophila indicates that the constraints imposed by the cell cycle are a force capable of driving changes in Eukaryotic gene architecture.

Surprising connections between gene architecture and splicing kinetics are illuminated using short, progressive metabolic labeling/RNA sequencing and novel computational modeling approaches in Drosophila cells.

A single human cell makes 10-100 transcriptional errors per second; these errors affect splicing and may influence the evolution of coding sequences.

Structural and functional analyses show how the spliceosomal Prp3 protein concomitantly binds double- and single- stranded regions in U4/U6 di-snRNAs and serves to stabilize the U4/U6•U5 tri-snRNP for splicing.

Hinokiflavone is identified as a splicing modulator that blocks progression from spliceosome complex A to complex B and inhibits SUMO protease SENP1, causing hyper-SUMOylation affecting 6 U2 snRNP proteins.

Ire1's RNase specificity and its cleavage sites coordination shape the evolutionary specialization of the unfolded protein response.

The structural model of hnRNP A1 shows that it can bind with both RRMs to RNA, which is shown to be relevant for the SMN2 exon 7 splicing mechanism in vivo.

Deposition of the exon junction complex is thought to be the missing link between pre-mRNA splicing and translation in multicellular organisms, but no evidence of such deposition has been found in Drosophila.

Transcriptome analysis reveals an alternative splicing program induced in the arterial endothelium under low-flow inflammatory conditions by platelet and macrophage recruitment and dependent upon the RNA-binding splice factor Rbfox2.