The serine/arginine-rich protein SF2/ASF regulates protein sumoylation

Federico Pelisch, Juan Gerez, Jimena Druker, Ignacio E. Schor, Manuel J. Munoz, Guillermo Risso, Ezequiel Petrillo, Belinda J. Westman, Angus I. Lamond, Eduardo Arzt, Anabella Srebrow

    Research output: Contribution to journalArticlepeer-review

    53 Citations (Scopus)

    Abstract

    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.

    Original languageEnglish
    Pages (from-to)16119-16124
    Number of pages6
    JournalProceedings of the National Academy of Sciences of the United States of America
    Volume107
    Issue number37
    DOIs
    Publication statusPublished - 14 Sept 2010

    Keywords

    • posttranslational modification
    • splicing factor
    • RNA processing
    • E3 ligase
    • SPLICING FACTOR ASF/SF2
    • HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEINS
    • HUMAN TOPOISOMERASE-I
    • MESSENGER-RNA
    • SR PROTEINS
    • SUMO MODIFICATION
    • GENE-EXPRESSION
    • E3 LIGASE
    • TRANSLATION INITIATION
    • PROTEOMIC ANALYSIS

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