The serine/arginine-rich protein SF2/ASF regulates protein sumoylation
Copyright policy )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.
- University of Dundee United Kingdom
- National Scientific and Technical Research Council Argentina
- University of Buenos Aires Argentina
RNA splicing, protein p53, protein binding, SPLICING FACTOR ASF/SF2, Substrate Specificity, nuclear protein, genetics, RNA, Small Interfering, E3 ligase, serine-arginine-rich splicing proteins, GENE-EXPRESSION, protein asf, Serine-Arginine Splicing Factors, sumoylation, article, protein processing, Nuclear Proteins, RNA-Binding Proteins, ubiquitin-conjugating enzyme UBC9, cell line, protein function, heat shock, unclassified drug, enzyme activity, ubiquitin conjugating enzyme, HUMAN TOPOISOMERASE-I, regulator protein, priority journal, protein protein interaction, PROTEOMIC ANALYSIS, SUMO protein, ubiquitin protein ligase E3, MESSENGER-RNA, signal transduction, conjugation, Protein Binding, 570, TRANSLATION INITIATION, regulatory mechanism, Ubiquitin-Conjugating Enzyme UBC9, SUMO-1 Protein, protein Ubc9, Cell Line, heat shock response, SR PROTEINS, HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEINS, Humans, controlled study, human, enzyme specificity, SUMO MODIFICATION, protein expression, protein inhibitor of activated STAT1, RNA metabolism, posttranslational modification, Splicing factor, protein inhibitor of activated STAT, human cell, SUMO E3 ligase, RNA binding protein, small interfering RNA, RNA processing, splicing factor, protein sf2, Ubiquitin-Conjugating Enzymes, RNA, Posttranslational modification, molecular recognition, Tumor Suppressor Protein p53, metabolism, SUMO 1 protein, Heat-Shock Response
RNA splicing, protein p53, protein binding, SPLICING FACTOR ASF/SF2, Substrate Specificity, nuclear protein, genetics, RNA, Small Interfering, E3 ligase, serine-arginine-rich splicing proteins, GENE-EXPRESSION, protein asf, Serine-Arginine Splicing Factors, sumoylation, article, protein processing, Nuclear Proteins, RNA-Binding Proteins, ubiquitin-conjugating enzyme UBC9, cell line, protein function, heat shock, unclassified drug, enzyme activity, ubiquitin conjugating enzyme, HUMAN TOPOISOMERASE-I, regulator protein, priority journal, protein protein interaction, PROTEOMIC ANALYSIS, SUMO protein, ubiquitin protein ligase E3, MESSENGER-RNA, signal transduction, conjugation, Protein Binding, 570, TRANSLATION INITIATION, regulatory mechanism, Ubiquitin-Conjugating Enzyme UBC9, SUMO-1 Protein, protein Ubc9, Cell Line, heat shock response, SR PROTEINS, HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEINS, Humans, controlled study, human, enzyme specificity, SUMO MODIFICATION, protein expression, protein inhibitor of activated STAT1, RNA metabolism, posttranslational modification, Splicing factor, protein inhibitor of activated STAT, human cell, SUMO E3 ligase, RNA binding protein, small interfering RNA, RNA processing, splicing factor, protein sf2, Ubiquitin-Conjugating Enzymes, RNA, Posttranslational modification, molecular recognition, Tumor Suppressor Protein p53, metabolism, SUMO 1 protein, Heat-Shock Response
citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).54 popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.Top 10% influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).Top 10% impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.Top 10%
Citations provided by BIP!Popularity provided by BIP!