Analysis of SUMOylated proteins using SUMO-traps
Date
2013-04-22Author
Da Silva Ferrada, Elisa
Xolalpa, Wendy
Lang, Valerie
Aillet, Fabienne
Martín-Ruiz, Itziar
De la Cruz-Herrera, Carlos F.
Lopitz Otsoa, Fernando
Goldenberg, Seth J.
Rivas, Carmen
England, Patrick
Rodríguez, Manuel S.
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Scientific Reports 3 : (2013) // Article N. 1690
Abstract
SUMO-modified proteins are recognized by SUMO interacting motifs (SIMs), thus triggering diverse cellular responses. Here SIMs were used to develop SUMO-traps to capture endogenous SUMOylated proteins. Our results show that these small peptides are transferable motifs that maintain their SUMO binding capacity when fused to the heterologous carrier protein GST. The tandem disposition of SIMs increases the binding capacity of SUMO-traps to specifically interact with polySUMO but not poly-Ubiquitin chains. We demonstrate that this SUMO capturing system purifies SUMOylated proteins such as I kappa B alpha, PTEN, PML or p53 in vitro and in vivo. These properties can be used to explore the many critical functions regulated by protein SUMOylation