Evidence map›Paper›PMID 35279775›Full record

ReviewCellular and molecular life sciences : CMLS2022

Multifaceted roles of YEATS domain-containing proteins and novel links to neurological diseases.

Ranchana Yeewa, Pawita Chaiya, Salinee Jantrapirom, Vorasuk Shotelersuk, Luca Lo Piccolo

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

12 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Proceedings of the National Academy of Sciences of the United States of America · 2026
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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

5 authors at 2 institutions in 1 country.

Ranchana YeewaCentre of Multidisciplinary Technology for Advanced Medicine (CMUTEAM), Faculty of Medicine, Chiang Mai University, Chiang Mai, 50200, Thailand.ORCID http://orcid.org/0000-0003-3915-0260
Pawita ChaiyaCentre of Multidisciplinary Technology for Advanced Medicine (CMUTEAM), Faculty of Medicine, Chiang Mai University, Chiang Mai, 50200, Thailand.
Salinee JantrapiromDrosophila Centre for Human Diseases and Drug Discovery (DHD), Faculty of Medicine, Chiang Mai University, Chiang Mai, 50200, Thailand.ORCID http://orcid.org/0000-0002-3111-5658
Vorasuk ShotelersukCentre of Excellence for Medical Genomics, Medical Genomics Cluster, Department of Paediatrics, Faculty of Medicine, Chulalongkorn University, Bangkok, 10330, Thailand.ORCID http://orcid.org/0000-0002-1856-0589
Luca Lo PiccoloCentre of Multidisciplinary Technology for Advanced Medicine (CMUTEAM), Faculty of Medicine, Chiang Mai University, Chiang Mai, 50200, Thailand. lopiccolo.l@cmu.ac.th.ORCID http://orcid.org/0000-0003-0558-356X
Chiang Mai University · THChulalongkorn University · TH

Funding

Chulalongkorn University 764002-HE01Chulalongkorn University CU_FRB640001_01_30_10Faculty of Medicine, Chiang Mai University 030/2564Health Systems Research Institute 64/122Health Systems Research Institute 64/132Medical Council of Thailand 012/2534
6 · The paper itself

Abstract

The so-called Yaf9, ENL, AF9, Taf14, and Sas5 (YEATS) domain-containing proteins, hereafter referred to as YD proteins, take control over the transcription by multiple steps of regulation either involving epigenetic remodelling of chromatin or guiding the processivity of RNA polymerase II to facilitate elongation-coupled mRNA 3' processing. Interestingly, an increasing amount of evidence suggest a wider repertoire of YD protein's functions spanning from non-coding RNA regulation, RNA-binding proteins networking, post-translational regulation of a few signalling transduction proteins and the spindle pole formation. However, such a large set of non-canonical roles is still poorly characterized. Notably, four paralogous of human YEATS domain family members, namely eleven-nineteen-leukaemia (ENL), ALL1-fused gene from chromosome 9 protein (AF9), YEATS2 and glioma amplified sequence 41 (GAS41), have a strong link to cancer yet new findings also highlight a potential novel role in neurological diseases. Here, in an attempt to more comprehensively understand the complexity of four YD proteins and to gain more insight into the novel functions they may accomplish in the neurons, we summarized the YD protein's networks, systematically searched and reviewed the YD genetic variants associated with neurodevelopmental disorders and finally interrogated the model organism Drosophila melanogaster.

Indexed as

AnimalsChromosomal Proteins, Non-HistoneDrosophila ProteinsEpigenesis, GeneticEvolution, MolecularHumansNervous System DiseasesProtein DomainsTranscriptional Elongation FactorsTranscription FactorsChromosomal Proteins, Non-HistoneDrosophila ProteinsELL protein, humanTranscriptional Elongation FactorsTranscription FactorsYEATS2 protein, humanYEATS4 protein, humanDrosophila melanogasterEpigenetic regulationNeurological diseasesYEATS domain

Identifiers

PMID35279775
PMCPMC11071958
OpenAlexW4221076279

What OpenQuestion holds

Textmetadata
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.