{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Schwich OD"],"funding":["Johann Wolfgang Goethe-Universität, Frankfurt am Main","Deutsche Forschungsgemeinschaft"],"pagination":["82"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7948361"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["22(1)"],"pubmed_abstract":["<h4>Background</h4>Alternative polyadenylation (APA) refers to the regulated selection of polyadenylation sites (PASs) in transcripts, which determines the length of their 3' untranslated regions (3'UTRs). We have recently shown that SRSF3 and SRSF7, two closely related SR proteins, connect APA with mRNA export. The mechanism underlying APA regulation by SRSF3 and SRSF7 remained unknown.<h4>Results</h4>Here we combine iCLIP and 3'-end sequencing and find that SRSF3 and SRSF7 bind upstream of proximal PASs (pPASs), but they exert opposite effects on 3'UTR length. SRSF7 enhances pPAS usage in a concentration-dependent but splicing-independent manner by recruiting the cleavage factor FIP1, generating short 3'UTRs. Protein domains unique to SRSF7, which are absent from SRSF3, contribute to FIP"],"journal":["Genome biology"],"pubmed_title":["SRSF3 and SRSF7 modulate 3'UTR length through suppression or activation of proximal polyadenylation sites and regulation of CFIm levels."],"pmcid":["PMC7948361"],"funding_grant_id":["Emmy Noether","SFB902 B13"],"pubmed_authors":["Mozos IRL","Poser I","Wegener M","Munch C","Keller M","Schwich OD","Zarnack K","Blumel N","Brunstein ME","Suess B","McNicoll F","Setty ST","Muller-McNicoll M"],"additional_accession":[]},"is_claimable":false,"name":"SRSF3 and SRSF7 modulate 3'UTR length through suppression or activation of proximal polyadenylation sites and regulation of CFIm levels.","description":"<h4>Background</h4>Alternative polyadenylation (APA) refers to the regulated selection of polyadenylation sites (PASs) in transcripts, which determines the length of their 3' untranslated regions (3'UTRs). We have recently shown that SRSF3 and SRSF7, two closely related SR proteins, connect APA with mRNA export. The mechanism underlying APA regulation by SRSF3 and SRSF7 remained unknown.<h4>Results</h4>Here we combine iCLIP and 3'-end sequencing and find that SRSF3 and SRSF7 bind upstream of proximal PASs (pPASs), but they exert opposite effects on 3'UTR length. SRSF7 enhances pPAS usage in a concentration-dependent but splicing-independent manner by recruiting the cleavage factor FIP1, generating short 3'UTRs. Protein domains unique to SRSF7, which are absent from SRSF3, contribute to FIP","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Mar","modification":"2026-05-02T16:49:20.53Z","creation":"2021-03-14T08:21:00Z"},"accession":"S-EPMC7948361","cross_references":{"pubmed":["33706811"],"doi":["10.1186/s13059-021-02298-y"]}}