Evidence map›Paper›PMID 33397984›Full record

ArticleNature communications2021

Spatiotemporal profiling of cytosolic signaling complexes in living cells by selective proximity proteomics.

Mi Ke, Xiao Yuan, An He, Peiyuan Yu, Wendong Chen, Yu Shi, Tony Hunter, Peng Zou, Ruijun Tian

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
6.0field-weighted citation impact, top 2% 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

30 citing papers in PubMed, 67 citations in OpenAlex.

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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

9 authors at 3 institutions in 2 countries.

Mi KeDepartment of Chemistry, School of Science, Southern University of Science and Technology, Shenzhen, China.
Xiao YuanDepartment of Chemistry, School of Science, Southern University of Science and Technology, Shenzhen, China.
An HeDepartment of Chemistry, School of Science, Southern University of Science and Technology, Shenzhen, China.
Peiyuan YuDepartment of Chemistry, School of Science, Southern University of Science and Technology, Shenzhen, China.ORCID 0000-0002-4367-6866
Wendong ChenDepartment of Chemistry, School of Science, Southern University of Science and Technology, Shenzhen, China.
Yu ShiMolecular and Cell Biology Laboratory, Salk Institute for Biological Studies, La Jolla, CA, USA.
Tony HunterMolecular and Cell Biology Laboratory, Salk Institute for Biological Studies, La Jolla, CA, USA.ORCID 0000-0002-7691-6993
Peng ZouCollege of Chemistry and Molecular Engineering, Peking University, Beijing, China.ORCID 0000-0002-9798-5242
Ruijun TianDepartment of Chemistry, School of Science, Southern University of Science and Technology, Shenzhen, China. tianrj@sustech.edu.cn.ORCID 0000-0001-9521-5124
Southern University of Science and Technology · CNSalk Institute for Biological Studies · USPeking University · CN

Funding

Viral Vector Core (VVC)P30CA014195 · NCI · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI Reuben Shaw · 1985 to 2026
$82.8M
NCI NIH HHS P30 CA014195
6 · The paper itself

Abstract

Signaling complexes are often organized in a spatiotemporal manner and on a minute timescale. Proximity labeling based on engineered ascorbate peroxidase APEX2 pioneered in situ capture of spatiotemporal membrane protein complexes in living cells, but its application to cytosolic proteins remains limited due to the high labeling background. Here, we develop proximity labeling probes with increased labeling selectivity. These probes, in combination with label-free quantitative proteomics, allow exploring cytosolic protein assemblies such as phosphotyrosine-mediated protein complexes formed in response to minute-scale EGF stimulation. As proof-of-concept, we systematically profile the spatiotemporal interactome of the EGFR signaling component STS1. For STS1 core complexes, our proximity proteomics approach shows comparable performance to affinity purification-mass spectrometry-based temporal interactome profiling, while also capturing additional-especially endosomally-located-protein complexes. In summary, we provide a generic approach for exploring the interactome of mobile cytosolic proteins in living cells at a temporal resolution of minutes.

Indexed as

ProteomicsSignal TransductionBiotinCell SurvivalCytosolEpidermal Growth FactorHeLa CellsHumansPhenolsProtein Interaction MappingSubcellular FractionsTime FactorsBiotinEpidermal Growth FactorPhenols

Identifiers

PMID33397984
PMCPMC7782698
OpenAlexW3120897007

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.