A5022623550- RNA Research and Splicing
- RNA modifications and cancer
- RNA and protein synthesis mechanisms
- Digestive system and related health
- Amyotrophic Lateral Sclerosis Research
- Chromosomal and Genetic Variations
- Genomics and Phylogenetic Studies
- Genetic Mapping and Diversity in Plants and Animals
- Genetic Neurodegenerative Diseases
- Neonatal Respiratory Health Research
- Nuclear Structure and Function
- Mitochondrial Function and Pathology
- Heat shock proteins research
- Birth, Development, and Health
Goethe University Frankfurt
2020-2024
La Trobe University
2023
John Innes Centre
1999
Abstract Hypoxia induces massive changes in alternative splicing (AS) to adapt cells the lack of oxygen. Here, we identify factor SRSF6 as a key AS response hypoxia. The level is strongly reduced acute hypoxia, which serves dual purpose: it allows for exon skipping and triggers dispersal nuclear speckles. Our data suggest that use speckles reprogram their gene expression during hypoxic adaptation plays an important role cohesion Down-regulation achieved through inclusion poison cassette...
Nuclear RNA binding proteins (RBPs) are difficult to study because they often belong large protein families and form extensive networks of auto- crossregulation. They highly abundant many localize condensates with a slow turnover, requiring long depletion times or knockouts that cannot distinguish between direct indirect compensatory effects. Here, we developed system is optimized for the rapid degradation nuclear RBPs, called hGRAD. It comes as “one-fits-all” plasmid, integration into any...
Abstract Nuclear speckles (NS) and paraspeckles (PS) are adjacent condensates with distinct protein composition, serine-arginine-rich splicing factors (SRSFs) concentrated in NS. Surprisingly, we find that SRSF5 is present both. Combining super-resolution imaging, proximity proteomics iCLIP, show binds PS core proteins to the PS-scaffold RNA NEAT1 locates between spheres. Acute depletion results reduced differently packaged . Under stress, SRSF5’s association increases, without SRSF5,...
Abstract Nuclear RNA binding proteins (RBPs) are difficult to study because they often belong large protein families and form extensive networks of auto- cross- regulation. They highly abundant localize condensates with a slow turnover, requiring long depletion times or knockouts that cannot distinguish between direct indirect compensatory effects. Here, we developed system is optimized for the rapid degradation nuclear RBPs, called hGRAD. It comes as ʹone-fits-allʹ plasmid, integration into...