Evidence map›Paper›PMID 40102608›Full record

ArticleCommunications biology2025

POT, an optogenetics-based endogenous protein degradation system.

Yunyue Chen, Siyifei Wang, Luhao Zhang, Dandan Peng, Ke Huang, Baohua Ji, Junfen Fu, Yingke Xu

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 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

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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.

Yunyue Chen *Department of Biomedical Engineering, MOE Key Laboratory of Biomedical Engineering, State Key Laboratory of Extreme Photonics and Instrumentation, Zhejiang Provincial Key Laboratory of Cardio-Cerebral Vascular Detection Technology and Medicinal Effectiveness Appraisal, Zhejiang University, Hangzhou, Zhejiang, China.
Siyifei Wang *Department of Biomedical Engineering, MOE Key Laboratory of Biomedical Engineering, State Key Laboratory of Extreme Photonics and Instrumentation, Zhejiang Provincial Key Laboratory of Cardio-Cerebral Vascular Detection Technology and Medicinal Effectiveness Appraisal, Zhejiang University, Hangzhou, Zhejiang, China.
Luhao ZhangDepartment of Biomedical Engineering, MOE Key Laboratory of Biomedical Engineering, State Key Laboratory of Extreme Photonics and Instrumentation, Zhejiang Provincial Key Laboratory of Cardio-Cerebral Vascular Detection Technology and Medicinal Effectiveness Appraisal, Zhejiang University, Hangzhou, Zhejiang, China.
Dandan PengDepartment of Endocrinology, Children's Hospital of Zhejiang University School of Medicine, National Clinical Research Center for Children's Health, Hangzhou, Zhejiang, China.
Ke HuangDepartment of Endocrinology, Children's Hospital of Zhejiang University School of Medicine, National Clinical Research Center for Children's Health, Hangzhou, Zhejiang, China.
Baohua JiDepartment of Engineering Mechanics, Biomechanics and Biomaterials Laboratory, Zhejiang University, Hangzhou, China.
Junfen FuDepartment of Endocrinology, Children's Hospital of Zhejiang University School of Medicine, National Clinical Research Center for Children's Health, Hangzhou, Zhejiang, China.
Yingke XuDepartment of Biomedical Engineering, MOE Key Laboratory of Biomedical Engineering, State Key Laboratory of Extreme Photonics and Instrumentation, Zhejiang Provincial Key Laboratory of Cardio-Cerebral Vascular Detection Technology and Medicinal Effectiveness Appraisal, Zhejiang University, Hangzhou, Zhejiang, China. yingkexu@zju.edu.cn.ORCID http://orcid.org/0000-0002-8317-0608

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Precise regulation of protein abundance is critical for cellular homeostasis, whose dysfunction may directly lead to human diseases. Optogenetics allows rapid and reversible control of precisely defined cellular processes, which has the potential to be utilized for regulation of protein dynamics at various scales. Here, we developed a novel optogenetics-based protein degradation system, namely Peptide-mediated OptoTrim-Away (POT) which employs expressed small peptides to effectively target endogenous and unmodified proteins. By engineering the light-induced oligomerization of the E3 ligase TRIM21, POT can rapidly trigger protein degradation via the proteasomal pathway. Our results showed that the developed POT-PI3K and POT-GPX4 modules, which used the iSH2 and FUNDC1 domains to specifically target phosphoinositide 3-kinase (PI3K) and glutathione peroxidase 4 (GPX4) respectively, were able to potently induce the degradation of these endogenous proteins by light. Both live-cell imaging and biochemical experiments validated the potency of these tools in downregulating cancer cell migration, proliferation, and even promotion of cell apoptosis. Therefore, we believe the POT offers an alternative and practical solution for rapid manipulation of endogenous protein levels, and it could potentially be employed to dissect complex signaling pathways in cell and for targeted cellular therapies.

Indexed as

OptogeneticsPeptidesProteolysisApoptosisCell MovementGlutathione PeroxidaseHEK293 CellsHumansPhosphatidylinositol 3-KinasesGlutathione PeroxidasePeptidesPhosphatidylinositol 3-Kinases

Identifiers

PMID40102608
PMCPMC11920400

What Socratic holds

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LicenceCC BY-NC-ND
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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 Socratic graph.