Evidence map›Paper›PMID 35473936›Full record

ArticleCell discovery2022

PPARγ phase separates with RXRα at PPREs to regulate target gene expression.

Zhean Li, Lingling Luo, Wenxia Yu, Ping Li, Danfeng Ou, Jia Liu, Hanhui Ma, Qinhu Sun, Aibin Liang, Cheng Huang and 3 more

Abstract read
In one paragraph

Article in Cell discovery, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

38 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
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  5. Current Challenges of Transcription Compartmentalization Research.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 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

13 authors.

Zhean Li *School of Life Science and Technology, ShanghaiTech University, Shanghai, China.
Lingling Luo *School of Pharmacy, Shanghai University of Traditional Chinese Medicine, Shanghai, China.
Wenxia YuSchool of Life Science and Technology, ShanghaiTech University, Shanghai, China.
Ping LiDepartment of Hematology, Tongji Hospital of Tongji University, Shanghai, China.
Danfeng OuInternational Academy of Optoelectronics at Zhaoqing, South China Normal University, Zhaoqing, Guangdong, China.
Jia LiuShanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, Shanghai, China.
Hanhui MaSchool of Life Science and Technology, ShanghaiTech University, Shanghai, China.
Qinhu SunShanghai R&D Center for Standardization of Chinese Medicines, Shanghai, China.
Aibin LiangDepartment of Hematology, Tongji Hospital of Tongji University, Shanghai, China.
Cheng HuangSchool of Pharmacy, Shanghai University of Traditional Chinese Medicine, Shanghai, China.
Tian ChiSchool of Life Science and Technology, ShanghaiTech University, Shanghai, China.
Xingxu HuangSchool of Life Science and Technology, ShanghaiTech University, Shanghai, China. huangxx@shanghaitech.edu.ORCID http://orcid.org/0000-0001-8934-1247
Yu ZhangSchool of Life Science and Technology, ShanghaiTech University, Shanghai, China. zhangy@shanghaitech.edu.cn.

Funding

National Natural Science Foundation of China (National Science Foundation of China) 81830004
6 · The paper itself

Abstract

Peroxisome proliferator-activated receptor (PPAR)-γ is a key transcription activator controlling adipogenesis and lipid metabolism. PPARγ binds PPAR response elements (PPREs) as the obligate heterodimer with retinoid X receptor (RXR) α, but exactly how PPARγ orchestrates the transcriptional response is unknown. This study demonstrates that PPARγ forms phase-separated droplets in vitro and solid-like nuclear condensates in cell, which is intriguingly mediated by its DNA binding domain characterized by the zinc finger motif. Furthermore, PPARγ forms nuclear condensates at PPREs sites through phase separation to compartmentalize its heterodimer partner RXRα to initiate PPARγ-specific transcriptional activation. Finally, using an optogenetic approach, the enforced formation of PPARγ/RXRα condensates leads to preferential enrichment at PPREs sites and significantly promotes the expression of PPARγ target genes. These results define a novel mechanism by which PPARγ engages the phase separation principles for efficient and specific transcriptional activation.

Identifiers

PMID35473936
PMCPMC9043196

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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.