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

Federico Pelisch; Juan Gerez; Jimena Druker; Ignacio E. Schor; Manuel J. Munoz; Guillermo Risso; Ezequiel Petrillo; Belinda J. Westman; Angus I. Lamond; Eduardo Arzt; Anabella Srebrow

doi:10.1073/pnas.1004653107

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

Federico Pelisch
, Juan Gerez
, Jimena Druker
, Ignacio E. Schor
, Manuel J. Munoz
, Guillermo Risso
, Ezequiel Petrillo
, Belinda J. Westman
, Angus I. Lamond
, Eduardo Arzt
, Anabella Srebrow

Research output: Contribution to journal › Article › peer-review

55 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	16119-16124
Number of pages	6
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	107
Issue number	37
DOIs	https://doi.org/10.1073/pnas.1004653107
Publication status	Published - 14 Sept 2010

Keywords

posttranslational modification
splicing factor
RNA processing
E3 ligase
SPLICING FACTOR ASF/SF2
HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEINS
HUMAN TOPOISOMERASE-I
MESSENGER-RNA
SR PROTEINS
SUMO MODIFICATION
GENE-EXPRESSION
E3 LIGASE
TRANSLATION INITIATION
PROTEOMIC ANALYSIS

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10.1073/pnas.1004653107

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title = "The serine/arginine-rich protein SF2/ASF regulates protein sumoylation",

abstract = "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.",

keywords = "posttranslational modification, splicing factor, RNA processing, E3 ligase, SPLICING FACTOR ASF/SF2, HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEINS, HUMAN TOPOISOMERASE-I, MESSENGER-RNA, SR PROTEINS, SUMO MODIFICATION, GENE-EXPRESSION, E3 LIGASE, TRANSLATION INITIATION, PROTEOMIC ANALYSIS",

author = "Federico Pelisch and Juan Gerez and Jimena Druker and Schor, \{Ignacio E.\} and Munoz, \{Manuel J.\} and Guillermo Risso and Ezequiel Petrillo and Westman, \{Belinda J.\} and Lamond, \{Angus I.\} and Eduardo Arzt and Anabella Srebrow",

year = "2010",

month = sep,

day = "14",

doi = "10.1073/pnas.1004653107",

language = "English",

volume = "107",

pages = "16119--16124",

journal = "Proceedings of the National Academy of Sciences of the United States of America",

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publisher = "National Academy of Sciences",

number = "37",

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T1 - The serine/arginine-rich protein SF2/ASF regulates protein sumoylation

AU - Pelisch, Federico

AU - Gerez, Juan

AU - Druker, Jimena

AU - Schor, Ignacio E.

AU - Munoz, Manuel J.

AU - Risso, Guillermo

AU - Petrillo, Ezequiel

AU - Westman, Belinda J.

AU - Lamond, Angus I.

AU - Arzt, Eduardo

AU - Srebrow, Anabella

PY - 2010/9/14

Y1 - 2010/9/14

N2 - 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.

AB - 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.

KW - posttranslational modification

KW - splicing factor

KW - RNA processing

KW - E3 ligase

KW - SPLICING FACTOR ASF/SF2

KW - HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEINS

KW - HUMAN TOPOISOMERASE-I

KW - MESSENGER-RNA

KW - SR PROTEINS

KW - SUMO MODIFICATION

KW - GENE-EXPRESSION

KW - E3 LIGASE

KW - TRANSLATION INITIATION

KW - PROTEOMIC ANALYSIS

U2 - 10.1073/pnas.1004653107

DO - 10.1073/pnas.1004653107

M3 - Article

C2 - 20805487

SN - 0027-8424

VL - 107

SP - 16119

EP - 16124

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

IS - 37

ER -

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

Abstract

Keywords

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