Evidence map›Paper›PMID 40348811›Full record

ArticleCommunications biology2025

Ubiquitin-activating enzyme1 (TgUAE1) acts as a key regulator of Toxoplasma gondii lytic cycle and homeostasis.

Qi-Xin Zhou, Dai-Qiang Lu, Si-Yu Tian, Yao Lv, Ming-Wei Chen, Xin Tian, Yan-Tao Wu, Fang-Jun Luo, Feng Tan, Ya-Ni Mou

Abstract read
In one paragraph

Article in Communications biology, 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

10 authors.

Qi-Xin Zhou *Department of Parasitology, School of Basic Medical Sciences, Wenzhou Medical University, Wenzhou, 325035, Zhejiang, China.
Dai-Qiang Lu *Department of Parasitology, School of Basic Medical Sciences, Wenzhou Medical University, Wenzhou, 325035, Zhejiang, China.
Si-Yu TianDepartment of Parasitology, School of Basic Medical Sciences, Wenzhou Medical University, Wenzhou, 325035, Zhejiang, China.
Yao LvDepartment of Parasitology, School of Basic Medical Sciences, Wenzhou Medical University, Wenzhou, 325035, Zhejiang, China.
Ming-Wei ChenDepartment of Parasitology, School of Basic Medical Sciences, Wenzhou Medical University, Wenzhou, 325035, Zhejiang, China.
Xin TianDepartment of Parasitology, School of Basic Medical Sciences, Wenzhou Medical University, Wenzhou, 325035, Zhejiang, China.
Yan-Tao WuDepartment of Parasitology, School of Basic Medical Sciences, Wenzhou Medical University, Wenzhou, 325035, Zhejiang, China.ORCID http://orcid.org/0009-0008-2141-0013
Fang-Jun LuoDepartment of Clinical Laboratory, Zhuji People's Hospital, Zhuji, Zhejiang, China.
Feng TanDepartment of Parasitology, School of Basic Medical Sciences, Wenzhou Medical University, Wenzhou, 325035, Zhejiang, China. tanfengsong@163.com.ORCID http://orcid.org/0000-0003-2856-4310
Ya-Ni MouDepartment of Parasitology, School of Basic Medical Sciences, Wenzhou Medical University, Wenzhou, 325035, Zhejiang, China. mouyaniq@163.com.ORCID http://orcid.org/0000-0002-4003-3291

Funding

National Natural Science Foundation of China (National Science Foundation of China) 82402659Natural Science Foundation of Zhejiang Province (Zhejiang Provincial Natural Science Foundation) LQN25H190007
6 · The paper itself

Abstract

Ubiquitylation, regulated by the ubiquitin-proteasome system (UPS), is crucial for cell division and cycle transitions in Toxoplasma gondii. However, the primary E1 ubiquitin-activating enzyme (UAE1) in this process has been unclear. This study identified and characterized TGGT1_290290 (TgUAE1) as the canonical E1 enzyme in T. gondii. Through a combination of bioinformatics, biochemical, pharmacological, and genetic approaches, TgUAE1 was shown to exhibit typical E1 activity, particularly in forming K48- and K63-linked polyubiquitin chains. TAK-243, a UAE1 inhibitor, can effectively inhibit the ubiquitin pathway in T. gondii, as thermal stabilization experiments identified TgUAE1 as its intracellular target. Disruption of TgUAE1 severely impaired parasite homeostasis and suppressed the lytic cycle, highlighting its critical role in T. gondii fitness. Mutation of C634 in TgUAE1 confirmed that its enzymatic activity is essential for function. Transcriptomics and quantitative ubiquitin proteomics revealed TgUAE1 as a key regulator of the ubiquitination process and the broader gene expression network in T. gondii. These findings not only underscore the indispensable role of TgUAE1 in the life cycle of T. gondii but also offer valuable data that could inform future studies on parasite biology and the development of novel therapeutic strategies.

Indexed as

HomeostasisProtozoan ProteinsToxoplasmaUbiquitin-Activating EnzymesHumansUbiquitinUbiquitinationProtozoan ProteinsUbiquitinUbiquitin-Activating Enzymes

Identifiers

PMID40348811
PMCPMC12065787

What OpenQuestion holds

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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.