Evidence map›Paper›PMID 35013300›Full record

ArticleNature communications2022

A proximity biotinylation-based approach to identify protein-E3 ligase interactions induced by PROTACs and molecular glues.

Satoshi Yamanaka, Yuto Horiuchi, Saya Matsuoka, Kohki Kido, Kohei Nishino, Mayaka Maeno, Norio Shibata, Hidetaka Kosako, Tatsuya Sawasaki

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 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
7.1field-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

38 citing papers in PubMed, 85 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Proteomics-Driven Strategies for Proximity-Inducing Drug Discovery.Angewandte Chemie (International ed. in English) · 2026
    Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Hydrogen-Deuterium Exchange Mass Spectrometry for Molecular Glue Characterization.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Review
  20. 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

9 authors at 3 institutions in 1 country.

Satoshi YamanakaDivision of Cell-Free Sciences, Proteo-Science Center, Ehime University, Matsuyama, 790-8577, Japan.ORCID http://orcid.org/0000-0001-8825-7481
Yuto HoriuchiDivision of Cell-Free Sciences, Proteo-Science Center, Ehime University, Matsuyama, 790-8577, Japan.
Saya MatsuokaDivision of Cell-Free Sciences, Proteo-Science Center, Ehime University, Matsuyama, 790-8577, Japan.
Kohki KidoDivision of Cell-Free Sciences, Proteo-Science Center, Ehime University, Matsuyama, 790-8577, Japan.
Kohei NishinoDivision of Cell Signaling, Fujii Memorial Institute of Medical Sciences, Tokushima University, Tokushima, 770-8503, Japan.
Mayaka MaenoDepartment of Nanopharmaceutical Sciences, Nagoya Institute of Technology, Nagoya, 466-8555, Japan.
Norio ShibataDepartment of Nanopharmaceutical Sciences, Nagoya Institute of Technology, Nagoya, 466-8555, Japan.ORCID http://orcid.org/0000-0002-3742-4064
Hidetaka KosakoDivision of Cell Signaling, Fujii Memorial Institute of Medical Sciences, Tokushima University, Tokushima, 770-8503, Japan.
Tatsuya SawasakiDivision of Cell-Free Sciences, Proteo-Science Center, Ehime University, Matsuyama, 790-8577, Japan. sawasaki@ehime-u.ac.jp.ORCID http://orcid.org/0000-0002-7952-0556
CellFree Sciences (Japan) · JPNagoya Institute of Technology · JPTokushima University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteolysis-targeting chimaeras (PROTACs) as well as molecular glues such as immunomodulatory drugs (IMiDs) and indisulam are drugs that induce interactions between substrate proteins and an E3 ubiquitin ligases for targeted protein degradation. Here, we develop a workflow based on proximity-dependent biotinylation by AirID to identify drug-induced neo-substrates of the E3 ligase cereblon (CRBN). Using AirID-CRBN, we detect IMiD-dependent biotinylation of CRBN neo-substrates in vitro and identify biotinylated peptides of well-known neo-substrates by mass spectrometry with high specificity and selectivity. Additional analyses reveal ZMYM2 and ZMYM2-FGFR1 fusion protein-responsible for the 8p11 syndrome involved in acute myeloid leukaemia-as CRBN neo-substrates. Furthermore, AirID-DCAF15 and AirID-CRBN biotinylate neo-substrates targeted by indisulam and PROTACs, respectively, suggesting that this approach has the potential to serve as a general strategy for characterizing drug-inducible protein-protein interactions in cells.

Indexed as

Biological AssayAdaptor Proteins, Signal TransducingBiotinylationCell Line, TumorDNA-Binding ProteinsGene Expression RegulationHEK293 CellsHepatocytesHumansImmunologic FactorsIntracellular Signaling Peptides and ProteinsLymphocytesNeuronsProtein BindingProtein Interaction MappingProteolysisAdaptor Proteins, Signal TransducingCRBN protein, humanDCAF15 protein, humanDNA-Binding ProteinsFGFR1 protein, humanImmunologic FactorsIntracellular Signaling Peptides and ProteinsN-(3-chloro-7-indolyl)-1,4-benzenedisulphonamideReceptor, Fibroblast Growth Factor, Type 1SulfonamidesTranscription FactorsUbiquitin-Protein LigasesZMYM2 protein, human

Identifiers

PMID35013300
PMCPMC8748630
OpenAlexW4205305242

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.