Journal
CELL REPORTS
Volume 20, Issue 5, Pages 1187-1200Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2017.06.091
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Funding
- Fondation Wiener - Anspach
- BBSRC [BB/J00779X/1]
- Newton Trust (University of Cambridge)
- CNRS PICS
- ANR [14-CE09-0013-01ANR]
- European Regional Development Fund
- Walloon Region
- BBSRC [BB/J00779X/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/J00779X/1] Funding Source: researchfish
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Pat1 RNA-binding proteins, enriched in processing bodies (P bodies), are key players in cytoplasmic 5' to 3' mRNA decay, activating decapping of mRNA in complex with the Lsm1-7 heptamer. Using co-immunoprecipitation and immunofluorescence approaches coupled with RNAi, we provide evidence for a nuclear complex of Pat1b with the Lsm2-8 heptamer, which binds to the spliceosomal U6 small nuclear RNA (snRNA). Furthermore, we establish the set of interactions connecting Pat1b/Lsm2-8/U6 snRNA/SART3 and additional U4/U6. U5 tri-small nuclear ribonucleoprotein particle (tri-snRNP) components in Cajal bodies, the site of snRNP biogenesis. RNA sequencing following Pat1b depletion revealed the preferential upregulation of mRNAs normally found in P bodies and enriched in 3' UTR AU-rich elements. Changes in > 180 alternative splicing events were also observed, characterized by skipping of regulated exons with weak donor sites. Our data demonstrate the dual role of a decapping enhancer in pre-mRNA processing as well as in mRNA decay via distinct nuclear and cytoplasmic Lsm complexes.
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