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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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:	Artículo publishedVersion
Lenguaje:	Inglés
Publicado:	2010
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

id	paperaa:paper_00278424_v107_n37_p16119_Pelisch
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spelling	paperaa:paper_00278424_v107_n37_p16119_Pelisch2023-06-12T16:45:18Z The serine/arginine-rich protein SF2/ASF regulates protein sumoylation Proc. Natl. Acad. Sci. U. S. A. 2010;107(37):16119-16124 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. 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 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. 2010 info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion application/pdf eng info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00278424_v107_n37_p16119_Pelisch
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
language	Inglés
orig_language_str_mv	eng
topic	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
spellingShingle	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 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. The serine/arginine-rich protein SF2/ASF regulates protein sumoylation
topic_facet	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
description	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.
format	Artículo Artículo publishedVersion
author	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.
author_facet	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.
author_sort	Pelisch, F.
title	The serine/arginine-rich protein SF2/ASF regulates protein sumoylation
title_short	The serine/arginine-rich protein SF2/ASF regulates protein sumoylation
title_full	The serine/arginine-rich protein SF2/ASF regulates protein sumoylation
title_fullStr	The serine/arginine-rich protein SF2/ASF regulates protein sumoylation
title_full_unstemmed	The serine/arginine-rich protein SF2/ASF regulates protein sumoylation
title_sort	serine/arginine-rich protein sf2/asf regulates protein sumoylation
publishDate	2010
url	http://hdl.handle.net/20.500.12110/paper_00278424_v107_n37_p16119_Pelisch
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The serine/arginine-rich protein SF2/ASF regulates protein sumoylation

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