PTBP2 ensures that adult protein variants are expressed only in mature neurons through regulation of alternative splicing during early neuronal development.
Extensive periodic regulation of alternative splicing during the cell cycle in genes is linked to cell cycle functions, and involves an auto-inhibitory mechanism that uses the protein kinase CLK1.
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.
New methods reveal that complex local splicing variations are more prevalent in animals than previously appreciated, and demonstrate that local splicing variations are relevant for studies of development, gene regulation and neurodegenerative diseases.
A conserved alternative splicing program is specific to planarian stem cells and is controlled by the highly conserved splicing factors CELF and MBNL; therefore, this mode of regulating stem cells is likely ancestral to all animals.
Identifying the translational targets of the shuttling protein, SRSF1, reveals that it is needed for normal cell division, and suggests that it couples pre-mRNA splicing and translation.
The RNA binding protein PTBP1 controls an extensive program of alternative splicing in embryonic stem cells, one function of which is to repress neuronal transcriptional programs.