FOXA1 forms biomolecular condensates that unpack condensed chromatin to function as a pioneer factor

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成果类型：

期刊论文

作者：

Ji, Dengyu;Shao, Changrong;Yu, Juan;Hou, Yaoyao;Gao, Xiao;...

通讯作者：

Chen, P;Wang, Liang;Wang, L

作者机构：

[Chen, P; Chen, Ping; Wu, Yichuan; Shao, Changrong; Ji, Dengyu; Gao, Xiao] Capital Med Univ, Sch Basic Med Sci, Dept Immunol, Beijing Key Lab Tumor Invas & Metastasis, Beijing 100069, Peoples R China.

[Chen, P; Chen, Ping; Hou, Yaoyao; Wang, Liang; Yu, Juan] Chinese Acad Sci, Inst Biophys, CAS Ctr Excellence Biomacromolecules, Natl Lab Biomacromolecules, Beijing 100101, Peoples R China.

[Hou, Yaoyao] Cent China Normal Univ, Sch Life Sci, Hubei Key Lab Genet Regulat & Integrat Biol, Wuhan, Peoples R China.

[Wang, Liang] Tsinghua Univ, Beijing Frontier Res Ctr Biol Struct, Sch Life Sci, Beijing 100084, Peoples R China.

通讯机构：

[Chen, P ; Wang, L] C

[Wang, L ] T

Capital Med Univ, Sch Basic Med Sci, Dept Immunol, Beijing Key Lab Tumor Invas & Metastasis, Beijing 100069, Peoples R China.

Chinese Acad Sci, Inst Biophys, CAS Ctr Excellence Biomacromolecules, Natl Lab Biomacromolecules, Beijing 100101, Peoples R China.

Tsinghua Univ, Beijing Frontier Res Ctr Biol Struct, Sch Life Sci, Beijing 100084, Peoples R China.

语种：

英文

关键词：

FOXA1, biomolecular condensates, chromatin, pioneer factor

期刊：

Molecular Cell

ISSN：

1097-2765

年：

2024

卷：

期：

页码：

244-260.e7

DOI：

10.1016/j.molcel.2023.11.020

基金类别：

Ministry of Science and Technology of the People's Republic of China#&#&#2018YFE0203302#&#&#2022YFA0912400 Tsinghua University National Natural Science Foundation of China#&#&#32022014#&#&#32100417

机构署名：

本校为其他机构

院系归属：

生命科学学院

摘要：

Eukaryotic DNA is packaged into chromatin in the nucleus, restricting the binding of transcription factors (TFs) to their target DNA sites. FOXA1 functions as a pioneer TF to bind condensed chromatin and initiate the opening of local chromatin for gene expression. However, the principles of FOXA1 recruitment and how it subsequently unpacks the condensed chromatin remain elusive. Here, we revealed that FOXA1 intrinsically forms submicron-sized condensates through its N- and C-terminal intrinsically disordered regions (IDRs). Notably, both IDRs enable FOXA1 to dissolve the condensed chromatin. I...

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FOXA1 forms biomolecular condensates that unpack condensed chromatin to function as a pioneer factor

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