Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 107, Issue 37, Pages 16119-16124Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1004653107
Keywords
posttranslational modification; splicing factor; RNA processing; E3 ligase
Categories
Funding
- Agencia Nacional de Promocion Cientifica y Tecnologica of Argentina
- Universidad de Buenos Aires
- Consejo Nacional de Investigaciones Cientificas y Tecnicas of Argentina
- European Alternative Splicing Network
- MRC [G0301131] Funding Source: UKRI
- Medical Research Council [G0301131] Funding Source: researchfish
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Protein modification by conjugation of small ubiquitin-related modifier (SUMO) is involved in diverse biological functions, such as transcription regulation, subcellular partitioning, stress response, DNA damage repair, and chromatin remodeling. Here, we show that the serine/arginine-rich protein SF2/ASF, a factor involved in splicing regulation and other RNA metabolism-related processes, is a regulator of the sumoylation pathway. The overexpression of this protein stimulates, but its knockdown inhibits SUMO conjugation. SF2/ASF interacts with Ubc9 and enhances sumoylation of specific substrates, sharing characteristics with already described SUMO E3 ligases. In addition, SF2/ASF interacts with the SUMO E3 ligase PIAS1 (protein inhibitor of activated STAT-1), regulating PIAS1-induced overall protein sumoylation. The RNA recognition motif 2 of SF2/ASF is necessary and sufficient for sumoylation enhancement. Moreover, SF2/ASF has a role in heat shock-induced sumoylation and promotes SUMO conjugation to RNA processing factors. These results add a component to the sumoylation pathway and a previously unexplored role for the multifunctional SR protein SF2/ASF.
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