IFIBYNE   05513
INSTITUTO DE FISIOLOGIA, BIOLOGIA MOLECULAR Y NEUROCIENCIAS
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
The ser-arg rich protein SF2/ASF regulates protein SUMOylation
Autor/es:
FEDERICO PELISCH; ANABELLA SREBROW
Lugar:
Riva del Grada, Italia
Reunión:
Conferencia; UBIQUITIN AND UBIQUITINLIKE MODIFIERS IN HEALTH AND DISEASE; 2009
Institución organizadora:
EMBO
Resumen:
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Protein modification by conjugation
of small ubiquitin-related modifiers (SUMO1, 2 and 3) is involved in diverse
biological functions, namely transcription regulation, sub-cellular
partitioning, stress response, DNA damage repair and chromatin remodeling. Since
its discovery more than a decade ago, there has been an enormous advance in the
knowledge of many aspects of the sumoylation pathway. However, there is a great
void regarding components, mechanisms and consequences. We found that the
serine/arginine-rich protein SF2/ASF functions at two levels in the sumoylation
cascade. It interacts with ubc9 and enhances the sumoylation of specific target
proteins, behaving as an E3 ligase and also interacts with the SUMO E3 ligase
PIAS1 and regulates its activity. SF2/ASF enhances overall protein sumoylation
and, furthermore, the stimulatory effect of PIAS1 on sumoylation depends on
SF2/ASF, showing that these two proteins cooperate to regulate sumoylation.
These results not only add a further level of regulation to the sumoylation
pathway but also a new role for the multifunctional SR protein SF2/ASF.