Evidence map›Paper›PMID 41284752›Full record

ArticlePLoS biology2025

STUPPIT is a proximity labeling tool for labeling intermediary proteins that bridge two non-interacting proteins.

Lin Xie, Lijuan Gao, Weihong Fu, Gangyun Wu, Hua Li, Wenxiu Ning

Abstract read
In one paragraph

Article in PLoS 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.

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

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

6 authors.

Lin XieYunnan Key Laboratory of Cell Metabolism and Diseases in Yunnan Center for Life Sciences, School of Life Sciences, Yunnan University, Kunming, China.
Lijuan GaoYunnan Key Laboratory of Cell Metabolism and Diseases in Yunnan Center for Life Sciences, School of Life Sciences, Yunnan University, Kunming, China.
Weihong FuYunnan Key Laboratory of Cell Metabolism and Diseases in Yunnan Center for Life Sciences, School of Life Sciences, Yunnan University, Kunming, China.
Gangyun WuYunnan Key Laboratory of Cell Metabolism and Diseases in Yunnan Center for Life Sciences, School of Life Sciences, Yunnan University, Kunming, China.
Hua LiYunnan Key Laboratory of Cell Metabolism and Diseases in Yunnan Center for Life Sciences, School of Life Sciences, Yunnan University, Kunming, China.
Wenxiu NingYunnan Key Laboratory of Cell Metabolism and Diseases in Yunnan Center for Life Sciences, School of Life Sciences, Yunnan University, Kunming, China.ORCID 0000-0003-1028-8151

Funding

Applied Basic Research Foundation of Yunnan ProvinceNational Natural Science Foundation of China
6 · The paper itself

Abstract

Decoding the complexities of signaling pathways is fundamental for deciphering the mechanisms underlying tissue development, homeostasis, and disease pathogenesis. Proximity labeling tools have been instrumental in identifying upstream or downstream effectors of specific proteins within signaling pathways. However, currently, there are no tools available to directly label and capture intermediary proteins that bridge two non-interacting proteins. Here, we developed Split-TurboID and PUP-IT based Protein Identification Tool (STUPPIT), a novel method combining split-TurboID and PUP-IT to biotinylate intermediary proteins of two non-interacting proteins through a two-step enzymatic reaction. STUPPIT was validated using three well-characterized protein triads, including YAP1/AMOT/β-actin, YAP1/LATS1/MOB1A, and β-catenin/α-catenin/β-actin using HEK293T human cell lines. Combining STUPPIT and proteomics, we identified novel intermediary proteins including ERC1 and USP7, which interacted both with β-catenin and SMAD4, key components of the Wnt and BMP signaling pathways. In conclusion, STUPPIT represents a powerful tool for labeling and capturing intermediary proteins between non-interacting partners, offering new insights into protein-protein interactions and advancing signal transduction research.

Indexed as

Protein Interaction MappingActinsAdaptor Proteins, Signal Transducingbeta CateninBiotinylationHEK293 CellsHumansProteomicsSignal TransductionTranscription FactorsUbiquitin ThiolesteraseYAP-Signaling ProteinsActinsAdaptor Proteins, Signal Transducingbeta CateninTranscription FactorsUbiquitin ThiolesteraseYAP1 protein, humanYAP-Signaling Proteins

Identifiers

PMID41284752
PMCPMC12668627

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.