Evidence map›Paper›PMID 32189389›Full record

ArticleProtein science : a publication of the Protein Society2020

Mapping p38α mitogen-activated protein kinase signaling by proximity-dependent labeling.

Emmanuel Prikas, Anne Poljak, Arne Ittner

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

18 citing papers in PubMed, 31 citations in OpenAlex.

  1. Proximity Labeling inBio-protocol · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Cancers · 2025
    Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Evaluating Cellular Viability by iTRAQ Proteomic Profiling.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Review
  17. Mapping p38α mitogen-activated protein kinase signaling by proximity-dependent labeling.Protein science : a publication of the Protein Society · 2020
    Article
  18. Functions of p38 MAP Kinases in the Central Nervous System.Frontiers in molecular neuroscience · 2020
    Review
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

3 authors at 2 institutions in 1 country.

Emmanuel PrikasDementia Research Centre, Faculty of Medicine, Health and Human Sciences, Macquarie University, Sydney, Australia.
Anne PoljakMark Wainwright Analytical Centre, University of New South Wales, Sydney, Australia.
Arne IttnerDementia Research Centre, Faculty of Medicine, Health and Human Sciences, Macquarie University, Sydney, Australia.ORCID 0000-0001-5244-6897
Macquarie University · AUUNSW Sydney · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitogen-activated protein (MAP) kinase signaling is central to multiple cellular responses and processes. MAP kinase p38α is the best characterized member of the p38 MAP kinase family. Upstream factors and downstream targets of p38α have been identified in the past by conventional methods such as coimmunoprecipitation. However, a complete picture of its interaction partners and substrates in cells is lacking. Here, we employ a proximity-dependent labeling approach using biotinylation tagging to map the interactome of p38α in cultured 293T cells. Fusing the advanced biotin ligase BioID2 to the N-terminus of p38α, we used mass spectrometry to identify 37 biotin-labeled proteins that putatively interact with p38α. Gene ontology analysis confirms known upstream and downstream factors in the p38 MAP kinase cascade (e.g., MKK3, MAPKAPK2, TAB2, and c-jun). We furthermore identify a cluster of zinc finger (ZnF) domain-containing proteins that is significantly enriched among proximity-labeled interactors and is involved in gene transcription and DNA damage response. Fluorescence imaging and coimmunoprecipitation with overexpressed p38α in cells supports an interaction of p38α with ZnF protein XPA, a key factor in the DNA damage response, that is promoted by UV irradiation. These results define an extensive network of interactions of p38α in cells and new direct molecular targets of MAP kinase p38α in gene regulation and the DNA damage response.

Indexed as

Signal TransductionBiotinylationCarbon-Nitrogen LigasesEscherichia coli ProteinsHEK293 CellsHumansMass Spectrometryp38 Mitogen-Activated Protein KinasesRepressor ProteinsUltraviolet RaysbirA protein, E coliCarbon-Nitrogen LigasesEscherichia coli Proteinsp38 Mitogen-Activated Protein KinasesRepressor ProteinsBioIDbiotinylationinteractomeMAP kinasep38p38αprotein-protein interactionproximity-dependent labeling

Identifiers

PMID32189389
PMCPMC7184780
OpenAlexW3010827019

What OpenQuestion holds

Textmetadata
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.