Evidence map›Paper›PMID 39847191›Full record

ArticleMolecular biology reports2025

SUMOylation of TRIM28 is positively modulated by the BTB/POZ domain of Kaiso.

Yaroslava Lobanova, Alexander Mazur, Daria Kaplun, Egor Prokchortchouk, Svetlana Zhenilo

Abstract read
PubMed Publisher
In one paragraph

Article in Molecular biology reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Yaroslava LobanovaFederal Research Centre «Fundamentals of Biotechnology», Russian Academy of Sciences, Moscow, Russia, 119071.
Alexander MazurFederal Research Centre «Fundamentals of Biotechnology», Russian Academy of Sciences, Moscow, Russia, 119071.
Daria KaplunFederal Research Centre «Fundamentals of Biotechnology», Russian Academy of Sciences, Moscow, Russia, 119071.
Egor ProkchortchoukFederal Research Centre «Fundamentals of Biotechnology», Russian Academy of Sciences, Moscow, Russia, 119071.
Svetlana ZheniloFederal Research Centre «Fundamentals of Biotechnology», Russian Academy of Sciences, Moscow, Russia, 119071. szhenilo@gmail.com.

Funding

Ministry of Science and Higher Education of the Russian Federation АААА-А20-120121790092-6Russian Science Foundation 19-74-30026
6 · The paper itself

Abstract

backgroundTRIM28 plays a crucial role in maintaining genomic stability and establishing imprinting, facilitated by the diversity of KRAB zinc finger proteins. The SUMOylation of TRIM28 is essential for its function and is enhanced in the presence of the KRAB domain. Previously, we demonstrated that Kaiso, another factor capable of interacting with TRIM28, can promote its SUMOylation. Here we investigate which structural elements of Kaiso are necessary for the hyper-SUMOylation of TRIM28. METHODS AND

resultsWe found that the SUMO-interacting motifs (SIMs) of Kaiso are not responsible for TRIM28 SUMOylation. The SUMOylation of individual TRIM28 domains in the presence of Kaiso was not observed, suggesting the importance of TRIM28's structural integrity for this process. The Kaiso BTB/POZ domain, but not its closest homolog ZBTB4, is sufficient for the effective hyper-SUMOylation of TRIM28. Also, using single-cell sequencing data of mouse embryos, we identified cells in which co-expression of Kaiso and TRIM28 occurs, including the immune system, nervous system and various epithelial cells.

conclusionsBTB/POZ domain of Kaiso may function similarly to KRAB domains in its interaction with TRIM28 regulating its SUMOylation.

Indexed as

SumoylationTranscription FactorsTripartite Motif-Containing Protein 28AnimalsHEK293 CellsHumansMiceProtein BindingProtein DomainsRepressor ProteinsRepressor ProteinsTranscription FactorsTRIM28 protein, humanTrim28 protein, mouseTripartite Motif-Containing Protein 28BTB/POZ domainKaisoSUMO interacting motifsSUMOylationTRIM28

Identifiers

PMID39847191

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.