Supplementary file 1-SRSF1 translational targetsData containing list of 1576 mRNAs that showed a 1.85-fold increase in polysomal-association in response to SRSF1 overexpression (translational targets tab). Data are supplied as an excel spreadsheet. Descriptions of columns are included in additional tab (descriptions of columns). Negative controls tab contains information on cellular abundance of mRNAs used as negative controls in all validation experiments.Supplementary file 1.xlsxSupplementary file 2-SILAC analysis following SRSF1 overexpressionList of proteins identified in SILAC experiment (SILAC tab). Data are supplied as an excel spreadsheet. Descriptions of columns are included in the additional tab (description of columns tab).Supplementary file 2.xlsxSupplementary file 3-Alternative splicing changes following SRSF1 overexpressionList of 382 SRSF1-regulated cassette exons determined by exon arrays (cassette exons tab) and list of SRSF1-regulated cassette exons with SRSF1-clip-tags CLIP tag over casette exon (clip tag over cassette exon tab). Data are supplied as an excel spreadsheet.Supplementary file 3.xlsxSupplementary file 4-SRSF1 translational consensus motif positionsBed file containing positions and sequences of the SRSF1 consensus motif in hg18 assembly of human genome. Data are supplied as a tab-delimited text file.CLIP_454_M2.hg18.005.ucsc.bed

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.