Journal
ELIFE
Volume 3, Issue -, Pages -Publisher
ELIFE SCIENCES PUBLICATIONS LTD
DOI: 10.7554/eLife.02028
Keywords
SR proteins; SRSF1; mRNA translation; alternative splicing; cell cycle; oncogenes
Categories
Funding
- MRC
- Wellcome Trust [095518/Z/11/Z]
- Marie Curie
- Consolider RNAREG [CSD2009-00080]
- Ministerio de Economia y Competitividad [BIO2011-23920]
- Sandra Ibarra Foundation [FSI2011-35]
- ICREA Funding Source: Custom
- Medical Research Council [MC_PC_U127584479] Funding Source: researchfish
- MRC [MC_PC_U127584479] Funding Source: UKRI
- Wellcome Trust [095518/Z/11/Z] Funding Source: Wellcome Trust
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The shuttling Serine/Arginine rich (SR) protein SRSF1 (previously known as SF2/ASF) is a splicing regulator that also activates translation in the cytoplasm. In order to dissect the gene network that is translationally regulated by SRSF1, we performed a high-throughput deep sequencing analysis of polysomal fractions in cells overexpressing SRSF1. We identified approximately 1,500 mRNAs that are translational targets of SRSF1. These include mRNAs encoding proteins involved in cell cycle regulation, such as spindle, kinetochore and M phase proteins, which are essential for accurate chromosome segregation. Indeed, we show that translational activity of SRSF1 is required for normal mitotic progression. Furthermore, we found that mRNAs that display alternative splicing changes upon SRSF1 overexpression are also its translational targets; strongly suggesting that SRSF1 couples pre-mRNA splicing and translation. These data provide insights on the complex role of SRSF1 in the control of gene expression at multiple levels and its implications in cancer.
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