The serine/arginine-rich protein SF2/ASF regulates protein sumoylation.
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.
Mesh Terms:
Cell Line, Heat-Shock Response, Humans, Nuclear Proteins, Protein Binding, RNA, Small Interfering, RNA-Binding Proteins, SUMO-1 Protein, Substrate Specificity, Tumor Suppressor Protein p53, Ubiquitin-Conjugating Enzymes
Cell Line, Heat-Shock Response, Humans, Nuclear Proteins, Protein Binding, RNA, Small Interfering, RNA-Binding Proteins, SUMO-1 Protein, Substrate Specificity, Tumor Suppressor Protein p53, Ubiquitin-Conjugating Enzymes
Proc. Natl. Acad. Sci. U.S.A.
Date: Sep. 14, 2010
PubMed ID: 20805487
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