Evidence map›Paper›PMID 37240065›Full record

ArticleInternational journal of molecular sciences2023

The Males Absent on the First (MOF) Mediated Acetylation Alters the Protein Stability and Transcriptional Activity of YY1 in HCT116 Cells.

Tingting Wu, Bingxin Zhao, Chengyu Cai, Yuyang Chen, Yujuan Miao, Jinmeng Chu, Yi Sui, Fuqiang Li, Wenqi Chen, Yong Cai and 2 more

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.2field-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

5 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Novel Therapeutic Targets in Cancers.International journal of molecular sciences · 2023
    Article
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

12 authors at 1 institution in 1 country.

Tingting WuSchool of Life Sciences, Jilin University, Changchun 130012, China.
Bingxin ZhaoSchool of Life Sciences, Jilin University, Changchun 130012, China.
Chengyu CaiSchool of Life Sciences, Jilin University, Changchun 130012, China.
Yuyang ChenSchool of Life Sciences, Jilin University, Changchun 130012, China.
Yujuan MiaoSchool of Life Sciences, Jilin University, Changchun 130012, China.
Jinmeng ChuSchool of Life Sciences, Jilin University, Changchun 130012, China.
Yi SuiSchool of Life Sciences, Jilin University, Changchun 130012, China.
Fuqiang LiSchool of Life Sciences, Jilin University, Changchun 130012, China.
Wenqi ChenSchool of Life Sciences, Jilin University, Changchun 130012, China.
Yong CaiSchool of Life Sciences, Jilin University, Changchun 130012, China.
Fei WangSchool of Life Sciences, Jilin University, Changchun 130012, China.ORCID 0000-0002-6799-9432
Jingji JinSchool of Life Sciences, Jilin University, Changchun 130012, China.ORCID 0000-0001-9432-5954
Jilin University · CN

Funding

National Natural Science Foundation of China No. 32170599 (JJ) and 31771421 (YC)
6 · The paper itself

Abstract

Yin Yang 1 (YY1) is a well-known transcription factor that controls the expression of many genes and plays an important role in the occurrence and development of various cancers. We previously found that the human males absent on the first (MOF)-containing histone acetyltransferase (HAT) complex may be involved in regulating YY1 transcriptional activity; however, the precise interaction between MOF-HAT and YY1, as well as whether the acetylation activity of MOF impacts the function of YY1, has not been reported. Here, we present evidence that the MOF-containing male-specific lethal (MSL) HAT complex regulates YY1 stability and transcriptional activity in an acetylation-dependent manner. First, the MOF/MSL HAT complex was bound to and acetylated YY1, and this acetylation further promoted the ubiquitin-proteasome degradation pathway of YY1. The MOF-mediated degradation of YY1 was mainly related to the 146-270 amino acid residues of YY1. Further research clarified that acetylation-mediated ubiquitin degradation of YY1 mainly occurred through lysine 183. A mutation at the YY1K183 site was sufficient to alter the expression level of p53-mediated downstream target genes, such as

Indexed as

Transcription FactorsUbiquitinAcetylationHCT116 CellsHumansMaleProtein StabilityYY1 Transcription FactorTranscription FactorsUbiquitinYY1 protein, humanYY1 Transcription Factorcell proliferationhistone acetyltransferaseMOFtranscription factorYin Yang 1

Identifiers

PMID37240065
PMCPMC10217912
OpenAlexW4378515354

What Socratic 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 Socratic graph.