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

• Autores: Pelisch, F.; Gerez, J.; Druker, J.; Schor, I.E.; Muñoz, M.J.; Risso, G.; Petrillo, E.; Westman, B.J.; Lamond, A.I.; Arzt, E.; Srebrow, A.
• Año de publicación: 2010
• Idioma: inglés
• Tipo de recurso: artículo
• Fuente: Proc. Natl. Acad. Sci. U. S. A. 2010;107(37):16119-16124
• Materia: E3 ligase; Posttranslational modification; RNA processing; Splicing factor; protein asf; protein inhibitor of activated STAT; protein inhibitor of activated STAT1; protein sf2; protein Ubc9; regulator protein; RNA; SUMO E3 ligase; SUMO protein; ubiquitin protein ligase E3; unclassified drug; nuclear protein; protein binding; protein p53; RNA binding protein; serine-arginine-rich splicing proteins; small interfering RNA; SUMO 1 protein; ubiquitin conjugating enzyme; ubiquitin-conjugating enzyme UBC9; article; conjugation; controlled study; enzyme activity; heat shock; human; human cell; molecular recognition; priority journal; protein expression; protein function; protein processing; protein protein interaction; regulatory mechanism; RNA metabolism; RNA splicing; signal transduction; sumoylation; cell line; enzyme specificity; genetics; heat shock response; metabolism; Cell Line; Heat-Shock Response; Humans; Nuclear Proteins; Protein Binding; RNA, Small Interfering; RNA-Binding Proteins; Substrate Specificity; SUMO-1 Protein; Tumor Suppressor Protein p53; Ubiquitin-Conjugating Enzymes
• Institución: Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales

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.
Fil:Pelisch, F. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Gerez, J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Druker, J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Schor, I.E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Muñoz, M.J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Risso, G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Petrillo, E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Srebrow, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.