Analysis of SUMOylated proteins using SUMO-traps - Archive ouverte HAL Access content directly
Journal Articles Scientific Reports Year : 2013

Analysis of SUMOylated proteins using SUMO-traps

(1, 2) , (1, 2) , (2) , (2) , (1) , (3) , (1) , (1, 4, 5) , , (3) , (6, 7) , (1, 2)
1
2
3
4
5
6
7

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 IκBα, PTEN, PML or p53 in vitro and in vivo. These properties can be used to explore the many critical functions regulated by protein SUMOylation.
Fichier principal
Vignette du fichier
SUMO traps Sci Rep april 2013.pdf (892.81 Ko) Télécharger le fichier
Origin : Files produced by the author(s)

Dates and versions

pasteur-03525526 , version 1 (13-01-2022)

Licence

Attribution - NonCommercial - ShareAlike - CC BY 4.0

Identifiers

Cite

Elisa da Silva-Ferrada, Wendy Xolalpa, Valérie Lang, Fabienne Aillet, Itziar Martin-Ruiz, et al.. Analysis of SUMOylated proteins using SUMO-traps. Scientific Reports, 2013, 3 (1), pp.1690. ⟨10.1038/srep01690⟩. ⟨pasteur-03525526⟩

Collections

PASTEUR CNRS
13 View
32 Download

Altmetric

Share

Gmail Facebook Twitter LinkedIn More