Evidence map›Paper›PMID 40704418›Full record

ArticleChembiochem : a European journal of chemical biology2025

Dominant-Negative Effects of p53 R337 Variants in Li-Fraumeni Syndrome: Impact on Tetramer Formation and Transcriptional Activity.

Rui Kamada, Shuya Sakaguchi, Madoka Kanno, Takaaki Ozawa, Natsumi Nakagawa, James G Omichinski, Kazuyasu Sakaguchi

Abstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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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

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3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

7 authors.

Rui KamadaLaboratory of Biological Chemistry, Department of Chemistry, Faculty of Science, Hokkaido University, Sapporo, 060-0810, Japan.ORCID https://orcid.org/0000-0002-6118-5091
Shuya SakaguchiLaboratory of Biological Chemistry, Department of Chemistry, Faculty of Science, Hokkaido University, Sapporo, 060-0810, Japan.
Madoka KannoLaboratory of Biological Chemistry, Department of Chemistry, Faculty of Science, Hokkaido University, Sapporo, 060-0810, Japan.
Takaaki OzawaLaboratory of Biological Chemistry, Department of Chemistry, Faculty of Science, Hokkaido University, Sapporo, 060-0810, Japan.
Natsumi NakagawaLaboratory of Biological Chemistry, Department of Chemistry, Faculty of Science, Hokkaido University, Sapporo, 060-0810, Japan.
James G OmichinskiDépartement de Biochimie et Médicine Moléculaire, Université de Montréal, C.P. 6128 Succursale Centre-Ville, Montréal, QC H3C 3J7, Canada.
Kazuyasu SakaguchiLaboratory of Biological Chemistry, Department of Chemistry, Faculty of Science, Hokkaido University, Sapporo, 060-0810, Japan.ORCID https://orcid.org/0000-0002-8434-4171

Funding

Japan Society for the Promotion of Science 20H02873Japan Society for the Promotion of Science 23K13838Natural Science and Engineering Research Councilthe Photo-excitonix Project at Hokkaido University
6 · The paper itself

Abstract

Li-Fraumeni syndrome (LFS) is an inherited cancer predisposition disorder caused by heterozygous TP53 mutations. Among these, missense mutations at Arg337-such as R337C and R337H-are common in LFS patients. Although many studies have characterized individual p53 variants in LFS, the impact of tetramerization domain (TD) mutations on wild-type (WT) p53 function remains unclear. Herein, a novel FRET-based assay system that enables the simultaneous detection of heterotetramer formation and p53-dependent transcriptional activity in live cells is developed. These results show that the heteromultimerization of the R337C variant with WT p53 is only slightly reduced compared to WT homotetramers, yet its transcriptional activity is diminished by over 50%. In contrast, the R337H variant forms heterotetramers at near-normal levels but exhibits markedly compromised transcriptional activity. These findings reveal a previously unrecognized dominant-negative-like effect, suggesting reduced p53 function is due not only to decreased tetramer formation but also to diminished heterotetramer stability. Moreover, the LFS-associated p53TD variants show a greater loss of activity against the low-affinity, apoptosis-inducing bax response element than against the high-affinity, cell cycle arrest-related CDKN1A response element. Collectively, this study demonstrates that p53TD mutations can exert dominant-negative effects, advancing the understanding of p53 heteromultimer function in LFS pathogenesis. These mechanistic insights into p53 heterotetramer stability may not only inform genetic screening strategies for LFS but also support future therapeutic approaches aimed at restoring p53 function by stabilizing mutant tetramers.

Indexed as

Li-Fraumeni SyndromeTumor Suppressor Protein p53Fluorescence Resonance Energy TransferHumansProtein MultimerizationTranscription, GeneticTP53 protein, humanTumor Suppressor Protein p53DNA bindingdominant‐negativehetero‐oligomerizationtranscriptional activitytumor suppressor protein p53

Identifiers

PMID40704418
PMCPMC12631009

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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.