HAL will be down for maintenance from Friday, June 10 at 4pm through Monday, June 13 at 9am. More information
Skip to Main content Skip to Navigation
Journal articles

Analysis of SUMOylated proteins using SUMO-traps

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.
Document type :
Journal articles
Complete list of metadata

https://hal-pasteur.archives-ouvertes.fr/pasteur-03525526
Contributor : Patrick England Connect in order to contact the contributor
Submitted on : Thursday, January 13, 2022 - 10:57:11 PM
Last modification on : Thursday, May 19, 2022 - 12:52:14 PM
Long-term archiving on: : Friday, April 15, 2022 - 2:02:41 AM

File

SUMO traps Sci Rep april 2013....
Files produced by the author(s)

Licence


Distributed under a Creative Commons Attribution - NonCommercial - ShareAlike 4.0 International License

Identifiers

Collections

Citation

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

Share

Metrics

Record views

6

Files downloads

9