Proteomics Unit, CIC bioGUNE, CIBERehd, Bd. 801A, Bizkaia Technology Park, Derio, 48160, Bizkaia, Spain.
Sci Rep. 2013;3:1690. doi: 10.1038/srep01690.
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.
SUMO 修饰的蛋白质被 SUMO 相互作用基序（SIMs）识别，从而触发多种细胞反应。 在这里，SIMs 被用来开发 SUMO 陷阱以捕获内源性 SUMO 化蛋白质。 我们的结果表明，这些小肽是可转移的基序，当它们融合到异源载体蛋白 GST 上时，它们保持 SUMO 结合能力。 SIMs 的串联排列增加了 SUMO 陷阱的结合能力，使其能够特异性地与多 SUMO 而不是多泛素链相互作用。 我们证明，这种 SUMO 捕获系统可在体外和体内纯化 SUMO 化蛋白质，如 IκBα、PTEN、PML 或 p53。 这些特性可用于探索受蛋白质 SUMO 化调节的许多关键功能。
