دورية أكاديمية
أعرض في EDS

SRSF3 and SRSF7 modulate 3'UTR length through suppression or activation of proximal polyadenylation sites and regulation of CFIm levels.

التفاصيل البيبلوغرافية
العنوان: SRSF3 and SRSF7 modulate 3'UTR length through suppression or activation of proximal polyadenylation sites and regulation of CFIm levels.
المؤلفون: Schwich OD; Institute for Molecular Bio Science, Goethe University Frankfurt, Max-von-Laue-Str. 13, 60438, Frankfurt, Germany.; Buchmann Institute for Molecular Life Sciences, Goethe University Frankfurt, Max-von-Laue-Str. 15, 60438, Frankfurt, Germany., Blümel N; Institute for Molecular Bio Science, Goethe University Frankfurt, Max-von-Laue-Str. 13, 60438, Frankfurt, Germany., Keller M; Buchmann Institute for Molecular Life Sciences, Goethe University Frankfurt, Max-von-Laue-Str. 15, 60438, Frankfurt, Germany.; Faculty of Biological Sciences, Goethe University Frankfurt, 60438, Frankfurt am Main, Germany., Wegener M; Institute for Molecular Bio Science, Goethe University Frankfurt, Max-von-Laue-Str. 13, 60438, Frankfurt, Germany.; Buchmann Institute for Molecular Life Sciences, Goethe University Frankfurt, Max-von-Laue-Str. 15, 60438, Frankfurt, Germany., Setty ST; Buchmann Institute for Molecular Life Sciences, Goethe University Frankfurt, Max-von-Laue-Str. 15, 60438, Frankfurt, Germany., Brunstein ME; Institute of Biochemistry II, Medical School, Goethe University Frankfurt, Sandhofstr. 2-4, 60528, Frankfurt am Main, Germany., Poser I; Max Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstr. 108, 01307, Dresden, Germany., Mozos IRL; The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK., Suess B; Department of Biology, Technical University Darmstadt, Schnittspahnstr. 10, 64287, Darmstadt, Germany., Münch C; Institute of Biochemistry II, Medical School, Goethe University Frankfurt, Sandhofstr. 2-4, 60528, Frankfurt am Main, Germany., McNicoll F; Institute for Molecular Bio Science, Goethe University Frankfurt, Max-von-Laue-Str. 13, 60438, Frankfurt, Germany., Zarnack K; Buchmann Institute for Molecular Life Sciences, Goethe University Frankfurt, Max-von-Laue-Str. 15, 60438, Frankfurt, Germany. kathi.zarnack@bmls.de.; Faculty of Biological Sciences, Goethe University Frankfurt, 60438, Frankfurt am Main, Germany. kathi.zarnack@bmls.de., Müller-McNicoll M; Institute for Molecular Bio Science, Goethe University Frankfurt, Max-von-Laue-Str. 13, 60438, Frankfurt, Germany. mueller-mcnicoll@bio.uni-frankfurt.de.
المصدر: Genome biology [Genome Biol] 2021 Mar 11; Vol. 22 (1), pp. 82. Date of Electronic Publication: 2021 Mar 11.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: BioMed Central Ltd Country of Publication: England NLM ID: 100960660 Publication Model: Electronic Cited Medium: Internet ISSN: 1474-760X (Electronic) Linking ISSN: 14747596 NLM ISO Abbreviation: Genome Biol Subsets: MEDLINE
أسماء مطبوعة: Publication: London, UK : BioMed Central Ltd
Original Publication: London : Genome Biology Ltd., c2000-
مواضيع طبية MeSH: 3' Untranslated Regions* , Gene Expression Regulation* , Poly A*, Cleavage And Polyadenylation Specificity Factor/*genetics , Serine-Arginine Splicing Factors/*metabolism, Alternative Splicing ; Animals ; Base Sequence ; Mice ; Models, Biological ; Monomeric GTP-Binding Proteins/metabolism ; Neurons ; Phosphorylation ; Poly(A)-Binding Proteins/metabolism ; Polyadenylation ; Protein Binding ; Protein Interaction Domains and Motifs ; RNA, Messenger/genetics ; RNA, Messenger/metabolism
مستخلص: Background: 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.
Results: 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 FIP1 recruitment. In contrast, SRSF3 promotes distal PAS (dPAS) usage and hence long 3'UTRs directly by counteracting SRSF7, but also indirectly by maintaining high levels of cleavage factor Im (CFIm) via alternative splicing. Upon SRSF3 depletion, CFIm levels decrease and 3'UTRs are shortened. The indirect SRSF3 targets are particularly sensitive to low CFIm levels, because here CFIm serves a dual function; it enhances dPAS and inhibits pPAS usage by binding immediately downstream and assembling unproductive cleavage complexes, which together promotes long 3'UTRs.
Conclusions: We demonstrate that SRSF3 and SRSF7 are direct modulators of pPAS usage and show how small differences in the domain architecture of SR proteins can confer opposite effects on pPAS regulation.
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فهرسة مساهمة: Keywords: 3′UTR length; APA; CFIm; FIP1; MACE-seq; SRSF3; SRSF7; dPAS; iCLIP; pPAS
المشرفين على المادة: 0 (3' Untranslated Regions)
0 (Cleavage And Polyadenylation Specificity Factor)
0 (Poly(A)-Binding Proteins)
0 (RNA, Messenger)
0 (Srsf3 protein, mouse)
170974-22-8 (Serine-Arginine Splicing Factors)
24937-83-5 (Poly A)
EC 3.6.1.- (FiP1 protein, mouse)
EC 3.6.5.2 (Monomeric GTP-Binding Proteins)
تواريخ الأحداث: Date Created: 20210312 Date Completed: 20220111 Latest Revision: 20220111
رمز التحديث: 20240628
مُعرف محوري في PubMed: PMC7948361
DOI: 10.1186/s13059-021-02298-y
PMID: 33706811
قاعدة البيانات: MEDLINE
الوصف
تدمد:1474-760X
DOI:10.1186/s13059-021-02298-y