Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Dynamic assembly of the mRNA m6A methyltransferase complex is regulated by METTL3 phase separation.

PLoS biology - 1 Feb 2022

Han Dasol, Longhini Andrew P, Zhang Xuemei, Hoang Vivian, Wilson Maxwell Z, Kosik Kenneth S

Abstract excerpt

m6A methylation is the most abundant and reversible chemical modification on mRNA with approximately one-fourth of eukaryotic mRNAs harboring at least one m6A-modified base. The recruitment of the mRNA m6A methyltransferase writer complex to phase-separated nuclear speckles is likely to be crucial in its regulation; however, control over the activity of the complex remains unclear. Supported by our observation...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Catalytic Domain
Share to Cryptochromes
Share to Luminescent Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Methyltransferases

Share to Microscopy, Confocal

Share to Multiprotein Complexes

Share to Red Fluorescent Protein

Share to S-Adenosylmethionine

Source

Open in PubMed Open full text

Identifiers

PMID: 35143475
DOI: 10.1371/journal.pbio.3001535
PMCID: PMC8865655

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Dynamic assembly of the mRNA m6A methyltransferase complex is regulated by METTL3 phase separation.PMID 35143475Read ↗

METTL3 regulates exocytosis independently of m <sup>6</sup> ASemantic proximity Read ↗

AI-empowered integrative structural characterization of m6A methyltransferase complexSemantic proximity Read ↗

Phase Separation of a Novel form of Euchromatic Histone Methyltransferasel (EHMT1 <sup>N/C</sup> ) into cytoplasmic RNA viral Inclusion bodies facilitates their coalescence, thereby enhancing viral replicationSemantic proximity Read ↗

cGAS phase separation inhibits TREX1-mediated DNA degradation and enhances cytosolic DNA sensing.Semantic proximity Read ↗

Cancer mutations rewire the RNA methylation specificity of METTL3-METTL14.Semantic proximity Read ↗

PRMT1-methylated MSX1 phase separates to control palate development.Semantic proximity Read ↗

Structural insights into the molecular mechanism of the m6A writer complexSemantic proximity Read ↗

Structure of METTL3-METTL14 with an m6A nucleotide reveals insights into m6A conversion and sensingSemantic proximity Read ↗

m5C RNA modiﬁcation upregulates E2F1 expression dependently on YBX1 phase separation and promotes tumor progression in ovarian cancerSemantic proximity Read ↗

Condensate formation of the human RNA-binding protein SMAUG1 is controlled by its intrinsically disordered regions and interactions with 14-3-3 proteinsSemantic proximity Read ↗

m6A-binding YTHDF proteins promote stress granule formation.Semantic proximity Read ↗

DOT1L interaction partner AF10 controls patterning of H3K79 methylation and RNA polymerase II to maintain cell identitySemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.