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

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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 SF...

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Detalles Bibliográficos
Autores principales: 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.
Formato: JOUR
Materias:
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
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00278424_v107_n37_p16119_Pelisch
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
Descripción
Sumario: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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