Evidence map›Paper›PMID 38172614›Full record

ArticleNature cell biology2024

A chaperone-like function of FUS ensures TAZ condensate dynamics and transcriptional activation.

Yangqing Shao, Xin Shu, Yi Lu, Wenxuan Zhu, Ran Li, Huanyi Fu, Chengyu Li, Wei Sun, Zhuo Li, Yitong Zhang and 9 more

Abstract read
PubMed Publisher
In one paragraph

Article in Nature cell biology, 2024. 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
7.2field-weighted citation impact, top 2% 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, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Biomolecular condensates in Hippo pathway regulation.Journal of Zhejiang University. Science. B · 2025
    Review
  5. Review
  6. Article
  7. Article
  8. Transcription regulation by biomolecular condensates.Nature reviews. Molecular cell biology · 2025
    Review
  9. Article
  10. Review
  11. Review
  12. YAP/TAZ Signalling Controls Epidermal Keratinocyte Fate.International journal of molecular sciences · 2024
    Review
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

19 authors at 6 institutions in 2 countries.

Yangqing Shao *Zhejiang Provincial Key Laboratory for Cancer Molecular Cell Biology, Life Sciences Institute, Zhejiang University, Hangzhou, China.
Xin Shu *Zhejiang Provincial Key Laboratory for Cancer Molecular Cell Biology, Life Sciences Institute, Zhejiang University, Hangzhou, China.
Yi Lu *Tongji University Cancer Center, Shanghai Tenth People's Hospital, School of Medicine, Tongji University, Shanghai, China.
Wenxuan ZhuZhejiang Provincial Key Laboratory for Cancer Molecular Cell Biology, Life Sciences Institute, Zhejiang University, Hangzhou, China.
Ran LiThe Eighth Affiliated Hospital, Sun Yat-Sen University, Shenzhen, China.
Huanyi FuZhejiang Provincial Key Laboratory for Cancer Molecular Cell Biology, Life Sciences Institute, Zhejiang University, Hangzhou, China.
Chengyu LiZhejiang Provincial Key Laboratory for Cancer Molecular Cell Biology, Life Sciences Institute, Zhejiang University, Hangzhou, China.
Wei SunZhejiang Provincial Key Laboratory for Cancer Molecular Cell Biology, Life Sciences Institute, Zhejiang University, Hangzhou, China.
Zhuo LiZhejiang Provincial Key Laboratory for Cancer Molecular Cell Biology, Life Sciences Institute, Zhejiang University, Hangzhou, China.
Yitong ZhangZhejiang Provincial Key Laboratory for Cancer Molecular Cell Biology, Life Sciences Institute, Zhejiang University, Hangzhou, China.
Xiaolei CaoZhejiang Provincial Key Laboratory for Cancer Molecular Cell Biology, Life Sciences Institute, Zhejiang University, Hangzhou, China.
Xifu YeTongji University Cancer Center, Shanghai Tenth People's Hospital, School of Medicine, Tongji University, Shanghai, China.
Emmanuel AjiboyeDepartment of Chemistry and Biochemistry, Wichita State University, Wichita, KS, USA.
Bin ZhaoZhejiang Provincial Key Laboratory for Cancer Molecular Cell Biology, Life Sciences Institute, Zhejiang University, Hangzhou, China.ORCID http://orcid.org/0000-0002-1690-646X
Long ZhangZhejiang Provincial Key Laboratory for Cancer Molecular Cell Biology, Life Sciences Institute, Zhejiang University, Hangzhou, China.ORCID http://orcid.org/0000-0001-8139-0474
Haifan WuDepartment of Chemistry and Biochemistry, Wichita State University, Wichita, KS, USA.
Xin-Hua FengZhejiang Provincial Key Laboratory for Cancer Molecular Cell Biology, Life Sciences Institute, Zhejiang University, Hangzhou, China.ORCID http://orcid.org/0000-0002-4418-0811
Bing YangZhejiang Provincial Key Laboratory for Cancer Molecular Cell Biology, Life Sciences Institute, Zhejiang University, Hangzhou, China. bingyang@zju.edu.cn.ORCID http://orcid.org/0000-0001-6739-2932
Huasong LuZhejiang Provincial Key Laboratory for Cancer Molecular Cell Biology, Life Sciences Institute, Zhejiang University, Hangzhou, China. huasong_lu@zju.edu.cn.ORCID http://orcid.org/0000-0003-0875-5531
Zhejiang University · CNZhejiang Cancer Hospital · CNShaoxing University · CNTongji University · CNWichita State University · USSun Yat-sen University · CN

Funding

National Natural Science Foundation of China (National Science Foundation of China) 22074132National Natural Science Foundation of China (National Science Foundation of China) 32070632National Natural Science Foundation of China (National Science Foundation of China) 32270745National Natural Science Foundation of China (National Science Foundation of China) 92053114
6 · The paper itself

Abstract

The Hippo pathway has important roles in organ development, tissue homeostasis and tumour growth. Its downstream effector TAZ is a transcriptional coactivator that promotes target gene expression through the formation of biomolecular condensates. However, the mechanisms that regulate the biophysical properties of TAZ condensates to enable Hippo signalling are not well understood. Here using chemical crosslinking combined with an unbiased proteomics approach, we show that FUS associates with TAZ condensates and exerts a chaperone-like effect to maintain their proper liquidity and robust transcriptional activity. Mechanistically, the low complexity sequence domain of FUS targets the coiled-coil domain of TAZ in a phosphorylation-regulated manner, which ensures the liquidity and dynamicity of TAZ condensates. In cells lacking FUS, TAZ condensates transition into gel-like or solid-like assembles with immobilized TAZ, which leads to reduced expression of target genes and inhibition of pro-tumorigenic activity. Thus, our findings identify a chaperone-like function of FUS in Hippo regulation and demonstrate that appropriate biophysical properties of transcriptional condensates are essential for gene activation.

Indexed as

Protein Serine-Threonine KinasesTrans-ActivatorsCell Line, TumorSignal TransductionTranscriptional ActivationTranscriptional Coactivator with PDZ-Binding Motif ProteinsProtein Serine-Threonine KinasesTrans-ActivatorsTranscriptional Coactivator with PDZ-Binding Motif Proteins

Identifiers

PMID38172614
OpenAlexW4390571966

What OpenQuestion holds

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Registered trials

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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.