Evidence map›Paper›PMID 35987950›Full record

ArticleNature communications2022

Spatiotemporal-resolved protein networks profiling with photoactivation dependent proximity labeling.

Yansheng Zhai, Xiaoyan Huang, Keren Zhang, Yuchen Huang, Yanlong Jiang, Jingwei Cui, Zhe Zhang, Cookson K C Chiu, Weiye Zhong, Gang Li

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
8.1field-weighted citation impact, top 1% of its field
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

45 citing papers in PubMed, 77 citations in OpenAlex.

  1. Review
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  20. Precise andACS central science · 2025
    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 at 3 institutions in 2 countries.

Yansheng Zhai *Institute of Systems and Physical Biology, Shenzhen Bay Laboratory, Shenzhen, 518132, China.
Xiaoyan Huang *Institute of Systems and Physical Biology, Shenzhen Bay Laboratory, Shenzhen, 518132, China.
Keren ZhangInstitute of Systems and Physical Biology, Shenzhen Bay Laboratory, Shenzhen, 518132, China.
Yuchen HuangInstitute of Systems and Physical Biology, Shenzhen Bay Laboratory, Shenzhen, 518132, China.
Yanlong JiangDepartment of Chemistry, UF Scripps Biomedical Research, 130 Scripps Way, Jupiter, FL, 33458, USA.
Jingwei CuiInstitute of Systems and Physical Biology, Shenzhen Bay Laboratory, Shenzhen, 518132, China.
Zhe ZhangInstitute of Systems and Physical Biology, Shenzhen Bay Laboratory, Shenzhen, 518132, China.
Cookson K C ChiuMulti-omics Mass Spectrometry Core, Office of Core Facility, Shenzhen Bay Laboratory, Shenzhen, 518132, China.
Weiye ZhongInstitute of Systems and Physical Biology, Shenzhen Bay Laboratory, Shenzhen, 518132, China.
Gang LiInstitute of Systems and Physical Biology, Shenzhen Bay Laboratory, Shenzhen, 518132, China. ligang@szbl.ac.cn.ORCID 0000-0003-4434-4756
Shenzhen Bay Laboratory · CNScripps Research Institute · USUniversity of Science and Technology of China · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzymatic-based proximity labeling approaches based on activated esters or phenoxy radicals have been widely used for mapping subcellular proteome and protein interactors in living cells. However, activated esters are poorly reactive which leads to a wide labeling radius and phenoxy radicals generated by peroxide treatment may disturb redox-sensitive pathways. Herein, we report a photoactivation-dependent proximity labeling (PDPL) method designed by genetically attaching photosensitizer protein miniSOG to a protein of interest. Triggered by blue light and tunned by irradiation time, singlet oxygen is generated, thereafter enabling spatiotemporally-resolved aniline probe labeling of histidine residues. We demonstrate its high-fidelity through mapping of organelle-specific proteomes. Side-by-side comparison of PDPL with TurboID reveals more specific and deeper proteomic coverage by PDPL. We further apply PDPL to the disease-related transcriptional coactivator BRD4 and E3 ligase Parkin, and discover previously unknown interactors. Through over-expression screening, two unreported substrates Ssu72 and SNW1 are identified for Parkin, whose degradation processes are mediated by the ubiquitination-proteosome pathway.

Indexed as

Nuclear ProteinsProteomicsEstersProteomeTranscription FactorsUbiquitin-Protein LigasesEstersNuclear ProteinsProteomeTranscription FactorsUbiquitin-Protein Ligases

Identifiers

PMID35987950
PMCPMC9392063
OpenAlexW4292415248

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.