Journal
RNA BIOLOGY
Volume 15, Issue 6, Pages 689-695Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/15476286.2018.1457936
Keywords
Splicing; spliceosome; SR proteins; SRSF1; post-translational modifications; SUMO conjugation
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Funding
- Consejo Nacional de Investigaciones Cientificas y Tecnicas de Argentina (CONICET)
- Agencia Nacional de Investigaciones Cientificas y Tecnologicas of Argentina (ANPCyT) [2012-0136, 2014-2888]
- University of Buenos Aires, Argentina (UBACyT) [20020130100157BA]
- European Alternative Splicing Network (EURASNET)
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Spliceosomal proteins have been revealed as SUMO conjugation targets. Moreover, we have reported that many of these are in a SUMO-conjugated form when bound to a pre-mRNA substrate during a splicing reaction. We demonstrated that SUMOylation of Prp3 (PRPF3), a component of the U4/U6 di-snRNP, is required for U4/U6 center dot U5 tri-snRNP formation and/or recruitment to active spliceosomes. Expanding upon our previous results, we have shown that the splicing factor SRSF1 stimulates SUMO conjugation to several spliceosomal proteins. Given the relevance of the splicing process, as well as the complex and dynamic nature of its governing machinery, the spliceosome, the molecular mechanisms that modulate its function represent an attractive topic of research. We posit that SUMO conjugation could represent a way of modulating spliceosome assembly and thus, splicing efficiency. How cycles of SUMOylation/de-SUMOylation of spliceosomal proteins become integrated throughout the highly choreographed spliceosomal cycle awaits further investigation.
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