The Serine-Arginine Rich Protein SF2/ASF Regulates Protein SUMOylation

FEDERICO PELISCH; JUAN GEREZ; JIMENA DRUKER; IGNACIO SCHOR; MANUEL MUÑOZ; GUILLERMO RISSO; EZEQUIEL PETRILLO; BELINDA WESTMAN; ANGUS LAMOND; EDUARDO ARZT; ANABELLA SREBROW

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

NATL ACAD SCIENCES

Lugar: Washington DC, USA; Año: 2010

0027-8424

Protein modification by conjugation of small ubiquitin-related modifier(SUMO) is involved in diverse biological functions such as transcription regulation, sub-cellular partitioning, stressresponse, DNA damage repair and chromatin remodeling. Here, we show that the serine/arginine-rich proteinSF2/ASF, a factor involved in splicing regulation and other RNA metabolism-related processes, is a regulator ofthe sumoylation pathway. Its overexpression stimulates while its knockdown inhibits SUMO conjugation. SF2/ASFinteracts 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, regulating PIAS1-inducedoverall protein sumoylation. The RNA recognition motif 2 of SF2/ASF is necessary and sufficient for sumoylationenhancement. Moreover, SF2/ASF has a role in heat shock-induced sumoylation and promotes SUMO conjugationto RNA processing factors. These results add a new component to the sumoylation pathway and a new role for themultifunctional SR protein SF2/ASF.