Evidence map›Paper›PMID 37679528›Full record

ArticleCancer gene therapy2023

α-Catenin acetylation is essential for its stability and blocks its tumor suppressor effects in breast cancer through Yap1.

Yuxi Yang, Shujing Li, Yulin Li, Linlin Lv, Dongman Ye, Jie Kang, Tao Yu, Yaming Wang, Huijian Wu

Erratum issuedAbstract read
PubMed Publisher
In one paragraph

Article in Cancer gene therapy, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 36% 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

3 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 1 country.

Yuxi Yang *School of Bioengineering & Key Laboratory of Protein Modification and Disease, Liaoning Province, Dalian University of Technology, Dalian, China.
Shujing Li *School of Bioengineering & Key Laboratory of Protein Modification and Disease, Liaoning Province, Dalian University of Technology, Dalian, China.ORCID 0000-0002-8643-1244
Yulin LiSchool of Bioengineering & Key Laboratory of Protein Modification and Disease, Liaoning Province, Dalian University of Technology, Dalian, China.
Linlin LvSchool of Bioengineering & Key Laboratory of Protein Modification and Disease, Liaoning Province, Dalian University of Technology, Dalian, China.
Dongman YeCancer Hospital of Dalian University of Technology, Shenyang, China.
Jie KangSchool of Bioengineering & Key Laboratory of Protein Modification and Disease, Liaoning Province, Dalian University of Technology, Dalian, China.
Tao YuCancer Hospital of Dalian University of Technology, Shenyang, China. yutao@cancerhosp-ln-cmu.com.
Yaming WangThe first affiliated Hospital of Dalian Medical University, Dalian, China. dlwym@mail.dlut.edu.cn.ORCID 0009-0000-4455-3123
Huijian WuSchool of Bioengineering & Key Laboratory of Protein Modification and Disease, Liaoning Province, Dalian University of Technology, Dalian, China. wuhj@dlut.edu.cn.ORCID 0000-0001-5257-0089
Dalian University of Technology · CNDalian Medical University · CN

Funding

National Natural Science Foundation of China (National Science Foundation of China) 81872263
6 · The paper itself

Abstract

α-Catenin plays a critical role in tissue integrity, repair, and embryonic development. However, the post-translational modifications of α-catenin and the correlative roles in regulating cancer progression remain unclear. Here, we report that α-catenin is acetylated by p300, and identify three acetylation sites, K45, K866, and K881. Conversely, α-catenin acetylation can be reversed by deacetylase HDAC6. Mechanistically, α-catenin acetylation releases the transcriptional coactivator Yes-associated protein 1 (Yap1) by blocking the interaction between α-catenin and Yap1, and promotes the accumulation of Yap1 in the nucleus. Through this mechanism, acetylation weakens the capacity of α-catenin to inhibit breast cancer cell proliferation and tumor growth in mice. Meanwhile, we show that CDDP induces acetylation of α-catenin, and acetylated α-catenin resists the apoptosis under CDDP conditions. Additionally, acetylation inhibits the proteasome-dependent degradation of α-catenin, thus enhancing the stability of α-catenin for storage. Taken together, our results demonstrate that α-catenin can be acetylated, an event that is key for the subcellular distribution of Yap1 and subsequent facilitation of breast tumorigenesis.

Indexed as

beta CateninBreast NeoplasmsAcetylationAdaptor Proteins, Signal Transducingalpha CateninAnimalsCell Line, TumorCell ProliferationMiceProtein Processing, Post-TranslationalTranscription FactorsYAP-Signaling ProteinsAdaptor Proteins, Signal Transducingalpha Cateninbeta CateninCtnna1 protein, mouseTranscription FactorsYap1 protein, mouseYAP-Signaling Proteins

Identifiers

PMID37679528
OpenAlexW4386515603

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.