bioRxiv · 10.1101/2020.12.09.418111
TRIM28 regulates Kaiso SUMOylation
Abstract
Tripartite motif protein 28 (TRIM28), a universal mediator of Kruppel-associated box domain zinc fingers (KRAB-ZNFs), is known to regulate DNA methylation of many repetitive elements and several imprinted loci. TRIM28 serves as a scaffold unit that is essential for the formation of stable repressor complexes. In the present study we found that TRIM28 is a binding partner for methyl-DNA binding protein Kaiso. Kaiso is a transcription factor that belongs to the BTB/POZ -zinc finger family. Recent data suggest that deficiency of Kaiso led to reduction of DNA methylation within the imprinting control region of H19/IGF2. Thus, we hypothesized that Kaiso and TRIM28 may cooperate to control methylated genes. We demonstrated that Kaiso interacts with TRIM28 via its two domains: BTB/POZ and three zinc finger domains. When bound to Kaisos zinc finger domains TRIM28 weakens their interactions with methylated DNA in vitro. Specific association of TRIM28 with BTB/POZ domain causes Kaiso hyperSUMOylation. Altogether our data describe a putative role of TRIM28 as a regulator of Kaiso activity.
Explore related subjects
Keep this discovery
Explore connections, maps & timelines
Filonova, G., Lobanova, Y., Kaplun, D., Zhenilo, S.. 2020-12-09. TRIM28 regulates Kaiso SUMOylation. https://doi.org/10.1101/2020.12.09.418111
Cite the original work for its findings. Save a collection to share your selection of sources.