Evidence map›Paper›PMID 34795231›Full record

ArticleNature communications2021

Identification of proximal SUMO-dependent interactors using SUMO-ID.

Orhi Barroso-Gomila, Fredrik Trulsson, Veronica Muratore, Iñigo Canosa, Laura Merino-Cacho, Ana Rosa Cortazar, Coralia Pérez, Mikel Azkargorta, Ibon Iloro, Arkaitz Carracedo and 6 more

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 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
3.1field-weighted citation impact, top 7% 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

48 citing papers in PubMed, 54 citations in OpenAlex.

  1. Review
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  5. USP7 at PML Nuclear Bodies: A Protein Interaction Network Perspective.International journal of molecular sciences · 2026
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  20. The SUMO Pathway.Methods in molecular biology (Clifton, N.J.) · 2025
    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

16 authors at 4 institutions in 2 countries.

Orhi Barroso-GomilaCenter for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, Building 801 A, 48160, Derio, Spain.ORCID http://orcid.org/0000-0002-1472-032X
Fredrik TrulssonCell and Chemical Biology, Leiden University Medical Center (LUMC), 2333 ZA, Leiden, The Netherlands.
Veronica MuratoreCenter for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, Building 801 A, 48160, Derio, Spain.
Iñigo CanosaCenter for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, Building 801 A, 48160, Derio, Spain.
Laura Merino-CachoCenter for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, Building 801 A, 48160, Derio, Spain.ORCID http://orcid.org/0000-0003-1551-4074
Ana Rosa CortazarCenter for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, Building 801 A, 48160, Derio, Spain.
Coralia PérezCenter for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, Building 801 A, 48160, Derio, Spain.ORCID http://orcid.org/0000-0002-1195-2563
Mikel AzkargortaCenter for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, Building 801 A, 48160, Derio, Spain.
Ibon IloroCenter for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, Building 801 A, 48160, Derio, Spain.
Arkaitz CarracedoCenter for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, Building 801 A, 48160, Derio, Spain.ORCID http://orcid.org/0000-0001-5957-1260
Ana M AransayCenter for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, Building 801 A, 48160, Derio, Spain.ORCID http://orcid.org/0000-0002-8271-612X
Felix ElortzaCenter for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, Building 801 A, 48160, Derio, Spain.ORCID http://orcid.org/0000-0001-8839-5438
Ugo MayorIkerbasque, Basque Foundation for Science, 48011, Bilbao, Spain.ORCID http://orcid.org/0000-0003-2812-8287
Alfred C O VertegaalCell and Chemical Biology, Leiden University Medical Center (LUMC), 2333 ZA, Leiden, The Netherlands.
Rosa BarrioCenter for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, Building 801 A, 48160, Derio, Spain. rbarrio@cicbiogune.es.ORCID http://orcid.org/0000-0002-9663-0669
James D SutherlandCenter for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, Building 801 A, 48160, Derio, Spain. jsutherland@cicbiogune.es.ORCID http://orcid.org/0000-0003-3229-793X
CIC bioGUNE · ESInstituto de Salud Carlos III · ESIkerbasque · ESLeiden University Medical Center · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The fast dynamics and reversibility of posttranslational modifications by the ubiquitin family pose significant challenges for research. Here we present SUMO-ID, a technology that merges proximity biotinylation by TurboID and protein-fragment complementation to find SUMO-dependent interactors of proteins of interest. We develop an optimized split-TurboID version and show SUMO interaction-dependent labelling of proteins proximal to PML and RANGAP1. SUMO-dependent interactors of PML are involved in transcription, DNA damage, stress response and SUMO modification and are highly enriched in SUMO Interacting Motifs, but may only represent a subset of the total PML proximal proteome. Likewise, SUMO-ID also allow us to identify interactors of SUMOylated SALL1, a less characterized SUMO substrate. Furthermore, using TP53 as a substrate, we identify SUMO1, SUMO2 and Ubiquitin preferential interactors. Thus, SUMO-ID is a powerful tool that allows to study the consequences of SUMO-dependent interactions, and may further unravel the complexity of the ubiquitin code.

Indexed as

Protein Interaction MapsProtein Processing, Post-TranslationalSumoylationCell Line, TumorGTPase-Activating ProteinsHEK293 CellsHumansPromyelocytic Leukemia ProteinProtein BindingProtein Interaction MappingSmall Ubiquitin-Related Modifier ProteinsSUMO-1 ProteinTranscription FactorsTumor Suppressor Protein p53UbiquitinGTPase-Activating ProteinsPromyelocytic Leukemia ProteinRANGAP1 protein, humanSALL1 protein, humanSmall Ubiquitin-Related Modifier ProteinsSUMO-1 ProteinSUMO1 protein, humanSUMO2 protein, humanTranscription FactorsTumor Suppressor Protein p53Ubiquitin

Identifiers

PMID34795231
PMCPMC8602451
OpenAlexW3212792200

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.