Evidence map›Paper›PMID 41501012›Full record

ArticleNature communications2026

Targeted stress granule regulation by engineering a non-catalytic O-GlcNAc transferase.

Na Wang, Fanjia Hou, Sihui Ma, Silan Liu, Haimei Wei, Weicheng Fang, Ke Zhang, Yun Ge

Abstract read
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. 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

8 authors.

Na WangState Key Laboratory of Chemical Oncogenomics, School of Chemical Biology and Biotechnology, Peking University Shenzhen Graduate School, Shenzhen, China.
Fanjia HouInstitute of Neurological and Psychiatric Disorders, Shenzhen Bay Laboratory, Shenzhen, China.
Sihui MaInstitute of Chemical Biology, Shenzhen Bay Laboratory, Shenzhen, China.
Silan LiuInstitute of Chemical Biology, Shenzhen Bay Laboratory, Shenzhen, China.
Haimei WeiInstitute of Chemical Biology, Shenzhen Bay Laboratory, Shenzhen, China.
Weicheng FangInstitute of Chemical Biology, Shenzhen Bay Laboratory, Shenzhen, China.
Ke ZhangInstitute of Neurological and Psychiatric Disorders, Shenzhen Bay Laboratory, Shenzhen, China.ORCID http://orcid.org/0000-0002-4794-8355
Yun GeState Key Laboratory of Chemical Oncogenomics, School of Chemical Biology and Biotechnology, Peking University Shenzhen Graduate School, Shenzhen, China. geyun@szbl.ac.cn.ORCID http://orcid.org/0000-0001-6769-5458

Funding

National Natural Science Foundation of China (National Science Foundation of China) 22277080National Natural Science Foundation of China (National Science Foundation of China) 92478103
6 · The paper itself

Abstract

Stress granules (SGs) are disease-relevant dynamic ribonucleoprotein condensates formed by liquid-liquid phase separation (LLPS) of proteins and mRNAs. Understanding their regulators and developing interventions are critical for therapeutic development. O-GlcNAc transferase (OGT) has been implicated in SG regulation, but functions beyond O-GlcNAcylation remain unclear. Here we uncover that, upon induced proximity, OGT suppresses LLPS of the SG marker G3BP1 and thereby SG assembly, independent of its catalytic activity. We repurpose OGT into an SG modulator by fusing its N-catalytic and intervening domains (NI) to induced-proximity modules. This inhibitory effect arises from targeted protein immobilization that rigidifies G3BP1 under prolonged stress. This tool recognizes G3BP1's domain organization, thus generalizes to four additional proteins featuring similar architectures, suppressing condensate formation with mobility reduction. This modular, genetically encoded strategy enables SG regulation and functional dissection by interfering material properties of critical SG proteins and illuminates the cryptic non-catalytic function of OGT.

Indexed as

N-AcetylglucosaminyltransferasesStress GranulesBiomolecular CondensatesDNA HelicasesHumansPhase SeparationPoly-ADP-Ribose Binding ProteinsProtein DomainsProtein EngineeringRNA HelicasesRNA Recognition Motif ProteinsDNA HelicasesG3BP1 protein, humanN-AcetylglucosaminyltransferasesO-GlcNAc transferaseOGT protein, humanPoly-ADP-Ribose Binding ProteinsRNA HelicasesRNA Recognition Motif Proteins

Identifiers

PMID41501012
PMCPMC12779947

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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 Socratic graph.