Evidence map›Paper›PMID 34634806›Full record

ArticleNucleic acids research2021

The comprehensive interactomes of human adenosine RNA methyltransferases and demethylases reveal distinct functional and regulatory features.

Helena Covelo-Molares, Ales Obrdlik, Ivana Poštulková, Michaela Dohnálková, Pavlína Gregorová, Ranjani Ganji, David Potěšil, Lisa Gawriyski, Markku Varjosalo, Štěpánka Vaňáčová

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

33 citing papers in PubMed, 54 citations in OpenAlex.

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  13. Structures and mechanisms of the RNA mActa biochimica et biophysica Sinica · 2024
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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

10 authors at 2 institutions in 2 countries.

Helena Covelo-MolaresCentral European Institute of Technology (CEITEC), Masaryk University, Brno 62500, Czech Republic.
Ales ObrdlikCentral European Institute of Technology (CEITEC), Masaryk University, Brno 62500, Czech Republic.
Ivana PoštulkováCentral European Institute of Technology (CEITEC), Masaryk University, Brno 62500, Czech Republic.
Michaela DohnálkováCentral European Institute of Technology (CEITEC), Masaryk University, Brno 62500, Czech Republic.
Pavlína GregorováCentral European Institute of Technology (CEITEC), Masaryk University, Brno 62500, Czech Republic.
Ranjani GanjiCentral European Institute of Technology (CEITEC), Masaryk University, Brno 62500, Czech Republic.
David PotěšilCentral European Institute of Technology (CEITEC), Masaryk University, Brno 62500, Czech Republic.
Lisa GawriyskiInstitute of Biotechnology & HiLIFE - Helsinki Institute of Life Science, University of Helsinki, Helsinki 00014, Finland.
Markku VarjosaloInstitute of Biotechnology & HiLIFE - Helsinki Institute of Life Science, University of Helsinki, Helsinki 00014, Finland.
Štěpánka VaňáčováCentral European Institute of Technology (CEITEC), Masaryk University, Brno 62500, Czech Republic.ORCID 0000-0001-8807-0684
Central European Institute of Technology · CZUniversity of Helsinki · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

N6-methyladenosine (m6A) and N6,2'-O-dimethyladenosine (m6Am) are two abundant modifications found in mRNAs and ncRNAs that can regulate multiple aspects of RNA biology. They function mainly by regulating interactions with specific RNA-binding proteins. Both modifications are linked to development, disease and stress response. To date, three methyltransferases and two demethylases have been identified that modify adenosines in mammalian mRNAs. Here, we present a comprehensive analysis of the interactomes of these enzymes. PCIF1 protein network comprises mostly factors involved in nascent RNA synthesis by RNA polymerase II, whereas ALKBH5 is closely linked with most aspects of pre-mRNA processing and mRNA export to the cytoplasm. METTL16 resides in subcellular compartments co-inhabited by several other RNA modifiers and processing factors. FTO interactome positions this demethylase at a crossroad between RNA transcription, RNA processing and DNA replication and repair. Altogether, these enzymes share limited spatial interactomes, pointing to specific molecular mechanisms of their regulation.

Indexed as

Adaptor Proteins, Signal TransducingAdenosineAlkB Homolog 5, RNA DemethylaseAlpha-Ketoglutarate-Dependent Dioxygenase FTODNA RepairDNA ReplicationGene OntologyHEK293 CellsHumansMethyltransferasesMolecular Sequence AnnotationNuclear ProteinsOxidoreductases, N-DemethylatingProtein BindingProtein Interaction MappingProtein IsoformsAdaptor Proteins, Signal TransducingAdenosineALKBH5 protein, humanAlkB Homolog 5, RNA DemethylaseAlpha-Ketoglutarate-Dependent Dioxygenase FTOFTO protein, humanMethyltransferasesMETTL16 protein, humanN(6),N(6)-dimethyladenosineN-methyladenosineNuclear ProteinsOxidoreductases, N-DemethylatingPCIF1 protein, humanProtein IsoformsRNA, MessengerRNA, Untranslated

Identifiers

PMID34634806
PMCPMC8565353
OpenAlexW3205773396

What OpenQuestion holds

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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.