Evidence map›Paper›PMID 37010886›Full record

ArticleeLife2023

Cohesin-independent STAG proteins interact with RNA and R-loops and promote complex loading.

Hayley Porter, Yang Li, Maria Victoria Neguembor, Manuel Beltran, Wazeer Varsally, Laura Martin, Manuel Tavares Cornejo, Dubravka Pezić, Amandeep Bhamra, Silvia Surinova and 3 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2023. 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
4.3field-weighted citation impact, top 5% 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, 29 citations in OpenAlex.

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  11. Transcriptional machinery as an architect of genome structure.Current opinion in structural biology · 2024
    Review
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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

13 authors at 3 institutions in 3 countries.

Hayley Porter *Research Department of Cancer Biology, Cancer Institute, University College London, London, United Kingdom.ORCID 0009-0004-1184-5583
Yang Li *Research Department of Cancer Biology, Cancer Institute, University College London, London, United Kingdom.ORCID 0000-0003-0943-6196
Maria Victoria NeguemborCentre for Genomic Regulation (CRG), Barcelona Institute of Science and Technology, Barcelona, Spain.ORCID 0000-0002-1583-1304
Manuel BeltranRegulatory Genomics Group, Cancer Institute, University College London, London, United Kingdom.ORCID 0000-0002-7945-2020
Wazeer VarsallyResearch Department of Cancer Biology, Cancer Institute, University College London, London, United Kingdom.
Laura MartinCentre for Genomic Regulation (CRG), Barcelona Institute of Science and Technology, Barcelona, Spain.ORCID 0000-0001-8801-6637
Manuel Tavares CornejoRegulatory Genomics Group, Cancer Institute, University College London, London, United Kingdom.
Dubravka PezićResearch Department of Cancer Biology, Cancer Institute, University College London, London, United Kingdom.ORCID 0000-0002-9833-8469
Amandeep BhamraProteomics Research Translational Technology Platform, Cancer Institute, University College London, London, United Kingdom.
Silvia SurinovaProteomics Research Translational Technology Platform, Cancer Institute, University College London, London, United Kingdom.ORCID 0000-0003-0442-9595
Richard G JennerRegulatory Genomics Group, Cancer Institute, University College London, London, United Kingdom.ORCID 0000-0002-2946-6811
Maria Pia CosmaCentre for Genomic Regulation (CRG), Barcelona Institute of Science and Technology, Barcelona, Spain.ORCID 0000-0003-4207-5097
Suzana HadjurResearch Department of Cancer Biology, Cancer Institute, University College London, London, United Kingdom.ORCID 0000-0002-3146-3118
Cancer Institute (WIA) · INCentre for Genomic Regulation · ESInstitució Catalana de Recerca i Estudis Avançats · ES

Funding

Cancer Research UK C416/A25145Wellcome TrustWellcome Trust 106985/Z/15/Z
6 · The paper itself

Abstract

Most studies of cohesin function consider the Stromalin Antigen (STAG/SA) proteins as core complex members given their ubiquitous interaction with the cohesin ring. Here, we provide functional data to support the notion that the SA subunit is not a mere passenger in this structure, but instead plays a key role in the localization of cohesin to diverse biological processes and promotes loading of the complex at these sites. We show that in cells acutely depleted for RAD21, SA proteins remain bound to chromatin, cluster in 3D and interact with CTCF, as well as with a wide range of RNA binding proteins involved in multiple RNA processing mechanisms. Accordingly, SA proteins interact with RNA, and R-loops, even in the absence of cohesin. Our results place SA1 on chromatin upstream of the cohesin ring and reveal a role for SA1 in cohesin loading which is independent of NIPBL, the canonical cohesin loader. We propose that SA1 takes advantage of structural R-loop platforms to link cohesin loading and chromatin structure with diverse functions. Since SA proteins are pan-cancer targets, and R-loops play an increasingly prevalent role in cancer biology, our results have important implications for the mechanistic understanding of SA proteins in cancer and disease.

Indexed as

R-Loop StructuresRNACCCTC-Binding FactorCell Cycle ProteinsChromatinChromosomal Proteins, Non-HistoneCohesinsCCCTC-Binding FactorCell Cycle ProteinsChromatinChromosomal Proteins, Non-HistoneCohesinsRNAcell biologychromosomescohesin loadinggene expressionhumanR-loopsRNA binding proteinsSTAG proteins

Identifiers

PMID37010886
PMCPMC10238091
OpenAlexW4362507033

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.